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Academic literature on the topic 'Chaperones'

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Published: 4 June 2021
Last updated: 6 September 2023

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Journal articles on the topic "Chaperones"

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Large, Andrew T., Martin D. Goldberg, and Peter A. Lund. "Chaperones and protein folding in the archaea." Biochemical Society Transactions 37, no. 1 (January 20, 2009): 46–51. http://dx.doi.org/10.1042/bst0370046.

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A survey of archaeal genomes for the presence of homologues of bacterial and eukaryotic chaperones reveals several interesting features. All archaea contain chaperonins, also known as Hsp60s (where Hsp is heat-shock protein). These are more similar to the type II chaperonins found in the eukaryotic cytosol than to the type I chaperonins found in bacteria, mitochondria and chloroplasts, although some archaea also contain type I chaperonin homologues, presumably acquired by horizontal gene transfer. Most archaea contain several genes for these proteins. Our studies on the type II chaperonins of the genetically tractable archaeon Haloferax volcanii have shown that only one of the three genes has to be present for the organisms to grow, but that there is some evidence for functional specialization between the different chaperonin proteins. All archaea also possess genes for prefoldin proteins and for small heat-shock proteins, but they generally lack genes for Hsp90 and Hsp100 homologues. Genes for Hsp70 (DnaK) and Hsp40 (DnaJ) homologues are only found in a subset of archaea. Thus chaperone-assisted protein folding in archaea is likely to display some unique features when compared with that in eukaryotes and bacteria, and there may be important differences in the process between euryarchaea and crenarchaea.
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Hervás, Rubén, and Javier Oroz. "Mechanistic Insights into the Role of Molecular Chaperones in Protein Misfolding Diseases: From Molecular Recognition to Amyloid Disassembly." International Journal of Molecular Sciences 21, no. 23 (December 2, 2020): 9186. http://dx.doi.org/10.3390/ijms21239186.

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Age-dependent alterations in the proteostasis network are crucial in the progress of prevalent neurodegenerative diseases, such as Alzheimer’s, Parkinson’s, or amyotrophic lateral sclerosis, which are characterized by the presence of insoluble protein deposits in degenerating neurons. Because molecular chaperones deter misfolded protein aggregation, regulate functional phase separation, and even dissolve noxious aggregates, they are considered major sentinels impeding the molecular processes that lead to cell damage in the course of these diseases. Indeed, members of the chaperome, such as molecular chaperones and co-chaperones, are increasingly recognized as therapeutic targets for the development of treatments against degenerative proteinopathies. Chaperones must recognize diverse toxic clients of different orders (soluble proteins, biomolecular condensates, organized protein aggregates). It is therefore critical to understand the basis of the selective chaperone recognition to discern the mechanisms of action of chaperones in protein conformational diseases. This review aimed to define the selective interplay between chaperones and toxic client proteins and the basis for the protective role of these interactions. The presence and availability of chaperone recognition motifs in soluble proteins and in insoluble aggregates, both functional and pathogenic, are discussed. Finally, the formation of aberrant (pro-toxic) chaperone complexes will also be disclosed.
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Scalia, Federica, Alessandra Maria Vitale, Radha Santonocito, Everly Conway de Macario, Alberto J. L. Macario, and Francesco Cappello. "The Neurochaperonopathies: Anomalies of the Chaperone System with Pathogenic Effects in Neurodegenerative and Neuromuscular Disorders." Applied Sciences 11, no. 3 (January 20, 2021): 898. http://dx.doi.org/10.3390/app11030898.

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The chaperone (or chaperoning) system (CS) constitutes molecular chaperones, co-chaperones, and chaperone co-factors, interactors and receptors, and its canonical role is protein quality control. A malfunction of the CS may cause diseases, known as the chaperonopathies. These are caused by qualitatively and/or quantitatively abnormal molecular chaperones. Since the CS is ubiquitous, chaperonopathies are systemic, affecting various tissues and organs, playing an etiologic-pathogenic role in diverse conditions. In this review, we focus on chaperonopathies involved in the pathogenic mechanisms of diseases of the central and peripheral nervous systems: the neurochaperonopathies (NCPs). Genetic NCPs are linked to pathogenic variants of chaperone genes encoding, for example, the small Hsp, Hsp10, Hsp40, Hsp60, and CCT-BBS (chaperonin-containing TCP-1- Bardet–Biedl syndrome) chaperones. Instead, the acquired NCPs are associated with malfunctional chaperones, such as Hsp70, Hsp90, and VCP/p97 with aberrant post-translational modifications. Awareness of the chaperonopathies as the underlying primary or secondary causes of disease will improve diagnosis and patient management and open the possibility of investigating and developing chaperonotherapy, namely treatment with the abnormal chaperone as the main target. Positive chaperonotherapy would apply in chaperonopathies by defect, i.e., chaperone insufficiency, and consist of chaperone replacement or boosting, whereas negative chaperonotherapy would be pertinent when a chaperone actively participates in the initiation and progression of the disease and must be blocked and eliminated.
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Scalia, Federica, Antonella Marino Gammazza, Everly Conway de Macario, Alberto J. L. Macario, and Francesco Cappello. "Myelin Pathology: Involvement of Molecular Chaperones and the Promise of Chaperonotherapy." Brain Sciences 9, no. 11 (October 30, 2019): 297. http://dx.doi.org/10.3390/brainsci9110297.

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The process of axon myelination involves various proteins including molecular chaperones. Myelin alteration is a common feature in neurological diseases due to structural and functional abnormalities of one or more myelin proteins. Genetic proteinopathies may occur either in the presence of a normal chaperoning system, which is unable to assist the defective myelin protein in its folding and migration, or due to mutations in chaperone genes, leading to functional defects in assisting myelin maturation/migration. The latter are a subgroup of genetic chaperonopathies causing demyelination. In this brief review, we describe some paradigmatic examples pertaining to the chaperonins Hsp60 (HSPD1, or HSP60, or Cpn60) and CCT (chaperonin-containing TCP-1). Our aim is to make scientists and physicians aware of the possibility and advantages of classifying patients depending on the presence or absence of a chaperonopathy. In turn, this subclassification will allow the development of novel therapeutic strategies (chaperonotherapy) by using molecular chaperones as agents or targets for treatment.
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Wang, Lisha, Liza Bergkvist, Rajnish Kumar, Bengt Winblad, and Pavel F. Pavlov. "Targeting Chaperone/Co-Chaperone Interactions with Small Molecules: A Novel Approach to Tackle Neurodegenerative Diseases." Cells 10, no. 10 (September 29, 2021): 2596. http://dx.doi.org/10.3390/cells10102596.

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The dysfunction of the proteostasis network is a molecular hallmark of neurodegenerative diseases such as Alzheimer’s disease, Parkinson’s disease, Huntington’s disease, and amyotrophic lateral sclerosis. Molecular chaperones are a major component of the proteostasis network and maintain cellular homeostasis by folding client proteins, assisting with intracellular transport, and interfering with protein aggregation or degradation. Heat shock protein 70 kDa (Hsp70) and 90 kDa (Hsp90) are two of the most important chaperones whose functions are dependent on ATP hydrolysis and collaboration with their co-chaperones. Numerous studies implicate Hsp70, Hsp90, and their co-chaperones in neurodegenerative diseases. Targeting the specific protein–protein interactions between chaperones and their particular partner co-chaperones with small molecules provides an opportunity to specifically modulate Hsp70 or Hsp90 function for neurodegenerative diseases. Here, we review the roles of co-chaperones in Hsp70 or Hsp90 chaperone cycles, the impacts of co-chaperones in neurodegenerative diseases, and the development of small molecules modulating chaperone/co-chaperone interactions. We also provide a future perspective of drug development targeting chaperone/co-chaperone interactions for neurodegenerative diseases.
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Zahn, Ralph. "Prion propagation and molecular chaperones." Quarterly Reviews of Biophysics 32, no. 4 (November 1999): 309–70. http://dx.doi.org/10.1017/s0033583500003553.

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1. Introduction 3102. Protein-only hypothesis 3123. The scrapie prion protein PrPSc3133.1 Purification of PrP 27–30 3133.2 Proteinase K resistance 3143.3 Scrapie-associated fibrils 3143.4 Smallest infectious unit 3163.5 Conformational properties 3163.6 Dissociation and stability 3194. The cellular prion protein PrPC3214.1 Prnp expression 3214.2 Biosynthetic pathway 3224.3 NMR structures 3244.4 Copper binding 3265. Post-translational PrP conversion 3275.1 Conformational isoforms 3275.2 Location of propagation 3295.3 Minimal PrP sequence 3305.4 Prion species barrier 3315.5 Prion strains 3326. Effect of familial TSE mutations 3336.1 Thermodynamic stability of PrPC 3346.2 De novo synthesis of PrPSc 3356.3 Transmembrane PrP forms 3377. Physical properties of synthetic PrP 3377.1 Amyloidogenic peptides 3377.2 Folding intermediates 3398. Hypothetical protein X 3408.1 Two species-specific epitopes 3408.2 Mapping the protein X epitope 3419. Chaperone-mediated PrP conversion 3439.1 Hsp60 and Hsp10 chaperonins 3439.2 GroEL promoted PrP-res formation 3459.3 Membrane-associated chaperonins 3459.4 Preference of GroEL for positive charges 3479.5 Potential GroEL/Hsp60 epitopes on PrP 3479.6 Conformations of chaperonin-bound PrP 3499.7 Conserved Hsp60 substrate binding sites 3499.8 Requirement of ATP-hydrolysis 3519.9 Hsp60-mediated prion propagation 35410. Template-assisted annealing model 35511. Acknowledgments 35712. References 357Although the central paradigm of protein folding (Anfinsen, 1973), that the unique three-dimensional structure of a protein is encoded in its amino acid sequence, is well established, its generality has been questioned due to two recent developments in molecular biology, the ‘prion’ and ‘molecular chaperone’. Biochemical characterization of infectious scrapie material causing central nervous system (CNS) degeneration indicates that the necessary component for disease propagation is proteinaceous (Prusiner, 1982), as first outlined by Griffith (1967) in general terms, and involves a conversion from a cellular prion protein, denoted PrPC, into a toxic scrapie form, PrPSc, which is facilitated by PrPSc acting as a template for PrPC to form new PrPSc molecules (Prusiner, 1987). The ‘protein-only’ hypothesis implies that the same polypeptide sequence, in the absence of any post-translational modifications, can adopt two considerably different stable protein conformations (Fig. 1). Thus, in the case of prions it is possible, although not proven, that they violate the central paradigm of protein folding. There is some indirect evidence that another factor, provisionally named ‘protein X’, might be involved in the conformational conversion process (Prusiner et al. 1998), which includes a dramatic change from α-helical into β-sheet secondary structure (Fig. 1). This factor has not been identified yet, but it has been proposed that protein X may act as a molecular chaperone. The idea that molecular chaperones play a critical role in the generation of PrPSc is appealing also from a theoretical point of view, because PrPSc formation involves changes in protein folding and possibly intermolecular aggregation (Fig. 1), processes in which chaperones are known to participate (Musgrove & Ellis, 1986). The discovery and functional analysis of more than a dozen molecular chaperones made it clear that these proteins do not complement folding information that is not already contained in the genetic code (Ellis et al. 1989); rather they facilitate the folding and assembly of proteins by preventing misfolding and refolding misfolded proteins (Hartl, 1996). Whether a molecular chaperone or another type of macromolecule is identified as the conversion factor, therefore, the molecular chaperone concept is likely to contribute to the understanding of the molecular nature of PrPC to PrPSc conversion.In this review I consider the prion concept from the view of a structural biologist whose main interest focuses on spontaneous and chaperone-mediated conformational changes in proteins.
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Muronetz, Vladimir I., Sofia S. Kudryavtseva, Evgeniia V. Leisi, Lidia P. Kurochkina, Kseniya V. Barinova, and Elena V. Schmalhausen. "Regulation by Different Types of Chaperones of Amyloid Transformation of Proteins Involved in the Development of Neurodegenerative Diseases." International Journal of Molecular Sciences 23, no. 5 (March 2, 2022): 2747. http://dx.doi.org/10.3390/ijms23052747.

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The review highlights various aspects of the influence of chaperones on amyloid proteins associated with the development of neurodegenerative diseases and includes studies conducted in our laboratory. Different sections of the article are devoted to the role of chaperones in the pathological transformation of alpha-synuclein and the prion protein. Information about the interaction of the chaperonins GroE and TRiC as well as polymer-based artificial chaperones with amyloidogenic proteins is summarized. Particular attention is paid to the effect of blocking chaperones by misfolded and amyloidogenic proteins. It was noted that the accumulation of functionally inactive chaperones blocked by misfolded proteins might cause the formation of amyloid aggregates and prevent the disassembly of fibrillar structures. Moreover, the blocking of chaperones by various forms of amyloid proteins might lead to pathological changes in the vital activity of cells due to the impaired folding of newly synthesized proteins and their subsequent processing. The final section of the article discusses both the little data on the role of gut microbiota in the propagation of synucleinopathies and prion diseases and the possible involvement of the bacterial chaperone GroE in these processes.
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Ellis, R. John. "Assembly chaperones: a perspective." Philosophical Transactions of the Royal Society B: Biological Sciences 368, no. 1617 (May 5, 2013): 20110398. http://dx.doi.org/10.1098/rstb.2011.0398.

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The historical origins and current interpretation of the molecular chaperone concept are presented, with the emphasis on the distinction between folding chaperones and assembly chaperones. Definitions of some basic terms in this field are offered and misconceptions pointed out. Two examples of assembly chaperone are discussed in more detail: the role of numerous histone chaperones in fundamental nuclear processes and the co-operation of assembly chaperones with folding chaperones in the production of the world's most important enzyme.
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Zuehlke, Abbey D., Michael A. Moses, and Len Neckers. "Heat shock protein 90: its inhibition and function." Philosophical Transactions of the Royal Society B: Biological Sciences 373, no. 1738 (December 4, 2017): 20160527. http://dx.doi.org/10.1098/rstb.2016.0527.

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The molecular chaperone heat shock protein 90 (Hsp90) facilitates metastable protein maturation, stabilization of aggregation-prone proteins, quality control of misfolded proteins and assists in keeping proteins in activation-competent conformations. Proteins that rely on Hsp90 for function are delivered to Hsp90 utilizing a co-chaperone–assisted cycle. Co-chaperones play a role in client transfer to Hsp90, Hsp90 ATPase regulation and stabilization of various Hsp90 conformational states. Many of the proteins chaperoned by Hsp90 (Hsp90 clients) are essential for the progression of various diseases, including cancer, Alzheimer's disease and other neurodegenerative diseases, as well as viral and bacterial infections. Given the importance of these clients in different diseases and their dynamic interplay with the chaperone machinery, it has been suggested that targeting Hsp90 and its respective co-chaperones may be an effective method for combating a large range of illnesses. This article is part of the theme issue ‘Heat shock proteins as modulators and therapeutic targets of chronic disease: an integrated perspective’.
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Modgil, V., R. Barratt, DJ Summerton, and A. Muneer. "Chaperone use amongst UK urological surgeons – an evaluation of current practice and opinion." Annals of The Royal College of Surgeons of England 98, no. 04 (April 1, 2016): 268–69. http://dx.doi.org/10.1308/rcsann.2016.0071.

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Introduction Intimate examinations are routinely performed by urologists as part of clinical practice. To protect patients and doctors, the General Medical Council offers guidance on the use of chaperones for intimate examinations. We assessed the opinions and use of chaperones amongst members of the British Association of Urological Surgeons (BAUS). Methods An online questionnaire comprising 12 questions on the use of chaperones in clinical practice was sent to all full, trainee and speciality doctor members of BAUS. Results The questionnaire had a response rate of 26% (n=331). The majority of respondents were consultant urologists, comprising 78.8% (n=261), with a wide range of years of experience. Of the respondents, 38.9% were not aware of the GMC guidance on chaperones. While 72.5% always used a chaperone., 22.9% never use a chaperone when the patient was of the same sex. Chaperones were most commonly used for intimate examinations (64.6%), and for examinations involving members of the opposite sex (77.3%). A majority of respondents felt that chaperones protect both the patient (77.3%), and the doctor (96.6%). However, 42.5% did not feel that using a chaperone assists the doctor’s examination, and some (17.2%) participants felt that chaperones were unnecessary. Conclusions This study shows considerable variability amongst urologists in their use of chaperones. A significant proportion of respondents were not aware of the GMC guidelines and did not regularly use a chaperone during an intimate examination. In addition, practice appears to be gender biased. Further study and education is suggested.
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Dissertations / Theses on the topic "Chaperones"

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Gomes, Francisco Edvan Rodrigues. "Clonagem, expressão e estudo de 3 co-chaperonas de Leishmania braziliensis." Universidade de São Paulo, 2011. http://www.teses.usp.br/teses/disponiveis/75/75132/tde-16092011-160310/.

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A leishmaniose é uma enfermidade infecciosa causada por várias espécies de parasitas do gênero Leishmania e representa um dos principais problemas de saúde pública nos países subdesenvolvidos. No hospedeiro, a sobrevivência do protozoário causador dessa doença depende de uma classe especial de proteínas, as chaperonas moleculares ou proteínas de choque térmico como também são conhecidas. A função dessas proteínas é auxiliar no processo de enovelamento protéico, no transporte de proteínas entre as membranas e em muitas outras importantes funções celulares. Neste processo, as chaperonas moleculares são auxiliadas pelas suas co-chaperonas que desempenham função de destaque. Dentre as principais famílias de chaperonas moleculares temos as Hsp70 e as Hsp90 com suas respectivas co-chaperonas, as Hsp40 e a Aha1. O presente trabalho pretendeu inicialmente expressar e purificar as co-chaperonas moleculares Hsp40I e Hsp40II de L. braziliensis para realizar estudos de caracterização estrutural por meio das técnicas de dicroísmo circular e fluorescência. Contudo, a insolubilidade dessas proteínas, que pode ter sido causada pela presença de mutações nas sequências de DNA, motivou a caracterização de outra co-chaperona, a Aha1 de L. braziliensis (LbAha1). A LbAha1 foi expressa no sobrenadante celular e purificada por três etapas cromatográficas (troca aniônica, afinidade por íons cálcio e gel filtração). A análise da sequência de aminoácidos dessa proteína mostra que ela possui 9 resíduos de triptofano distribuídos nos dois domínios característicos da LbAha1. Estudos de desnaturação química por uréia, monitorados pelas técnicas de dicroísmo circular e fluorescência, mostram que os dois domínios da LbAha1 apresentam estabilidades diferentes. Os estudos estruturais realizados permitiram identificar as transições com o respectivo domínio.
Leishmaniasis is an infectious disease caused by several species of Leishmania species and represents major public health problems in developing countries. In the harborer, the survival of the parasite that cause this disease depends on a special class of proteins, molecular chaperones or heat shock proteins as they are also known. The function of these proteins is to assist in protein folding, transport of proteins and many other important cellular functions. In this process the molecular chaperones are helped by their co-chaperones that play a prominent role. Among the main families of molecular chaperones, there are Hsp70 and Hsp90 with their respective co-chaperones, Hsp40 and the Aha1. The present work, initially pretended to express and purify the molecular co-chaperones Hsp40I and Hsp40II of the L. braziliensis for structural characterization by spectroscopic techniques like fluorescence and circular dichroism. However, the insolubility of these proteins, possibly caused by the presence of mutations in their DNA sequences, led to the characterization of another co-chaperone, the Aha1 of the L. braziliensis. These proteins were expressed in the cell supernatant and purified by three chromatographic steps (anion exchange, affinity for calcium ions and gel filtration). The analysis of the DNA sequence of this protein shows that it has nine Trp residues distributed between the two domains and by urea denaturation studies monitored by fluorescence techniques and circular dichroism show that they have different stabilities.
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Moosavi, Behrooz. "The Role of Molecular Chaperone Hsp104 and its Co-chaperones in the Yeast [PSI+] Propagation." Thesis, University of Kent, 2008. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.499804.

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Gonçalves, Danieli Cristina 1986. "Estudos iniciais de ineraçãos da HSP90 através da caracterização funcioanl de um transgênico e biofísica de uma co-chaperona." [s.n.], 2012. http://repositorio.unicamp.br/jspui/handle/REPOSIP/314030.

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Orientadoesr: Carlos Henrique Inácio Ramos, Gonçalo Amarante Guimarães Pereira
Dissertação (mestrado) - Universidade Estadual de Campinas, Instituto de Biologia
Made available in DSpace on 2018-08-20T06:21:14Z (GMT). No. of bitstreams: 1 Goncalves_DanieliCristina_M.pdf: 10469841 bytes, checksum: df29d5b11d3cdd27679b971b2bbcb032 (MD5) Previous issue date: 2012
Resumo: Chaperonas moleculares (Heat Shock proteins - HSPs) são componentes chave do sistema de controle de qualidade de proteínas (PQC - Protein Quality Control), que é essencial para a vida, sendo responsável por manter a homeostase proteica e a adequada função de diversas vias. Problemas no processo de enovelamento estão relacionados a doenças degenerativas, amilóides e câncer. Em plantas, as chaperonas moleculares desempenham um papel crucial na proteção contra estresses bióticos e abióticos, pois como organismos sésseis, as plantas devem ser capazes de responder rapidamente a mudanças na temperatura, salinidade, déficit hídrico, entre outros. A chaperona molecular Hsp90 (Heat Shock protein 90 kDa) compreende uma família ubíqua, considerada um 'hub' por interagir com chaperonas, co-chaperonas e ter como clientes proteínas regulatórias essenciais como fatores de transcrição, quinases, receptores de hormônios, entre outros. A Hsp90 age em conjunto com co-chaperonas, as quais modulam e direcionam sua função. Uma destas co-chaperonas é a Hop (Hsp70-Hsp90 organizing protein), capaz de interagir simultaneamente com a Hsp90 e Hsp70, mediando a transferência de substratos. A Hop é composta por três domínios com repetições de tetratricopeptídeos (TPR) (TPR1, TPR2A e TPR2B), responsáveis pela interação com as chaperonas, porém a dinâmica desta interação não está bem entendida, uma vez que ainda não há estrutura da Hop inteira e o estado oligomérico desta co-chaperona ainda é controverso na literatura. Neste trabalho apresentamos a classificação de um gene de Hsp90 de cana-de-açúcar, e o início de sua caracterização funcional através de transgenia em Arabidopsis thaliana. Apresentamos também a caracterização biofísica de uma importante co-chaperona da Hsp90, a Hop (Hsp70-Hsp90 organizing protein) humana. Através da análise de sequências a Hsp90 de cana-de-açúcar foi classificada como Hsp90-3, uma isoforma citosólica. Plantas transgênicas de A. thaliana, produzidas a partir da inserção do gene da Hsp90-3 de cana-de-açúcar, apresentaram níveis reduzidos de Hsp90. Tal perturbação nos níveis de Hsp90 parece ter afetado a expressão de outras proteínas da rede de interações, relacionadas com processos diversos como resposta imune e fotossíntese. As plantas transgênicas também exibiram germinação mais rápida e raízes mais longas em relação ao controle. Sob estresse térmico, linhagens transgênicas apresentaram maior suscetibilidade à alta temperatura em relação ao controle. Tais resultados sugerem que a Hsp90 tem um importante papel na fisiologia celular e no desenvolvimento, e que os níveis de Hsp90 são críticos para a resposta frente a estresses. A caracterização biofísica do mutante Hop D456G, uma mutação no domínio TPR2B, mostrou que esta proteína é uma mistura de monômeros, dímeros e oligômeros maiores, porém com prevalência do estado monomérico. O resíduo D456 pode ter uma participação na dinâmica de dimerização e é possível que o estado oligomérico da Hop seja regulado entre os estados monomérico e dimérico, com a finalidade de facilitar sua atividade adaptadora
Abstract: Molecular chaperones (heat shock proteins - HSPs) are key components of protein quality-control system (PQC - Protein Quality Control), which maintains protein homeostasis and the proper function of several pathways, being essential for life. Defects in folding processes are related to degenerative diseases, amyloidosis and cancer. In plants, which as sessile organisms must be able to respond rapidly to changes in temperature, salinity, water deficit, and others, molecular chaperones play a crucial role in protecting against such biotic and abiotic stresses. Molecular chaperone Hsp90 (Heat Shock Protein 90 kDa) comprise an ubiquitous family, considered a hub as it interacts with chaperones, co-chaperones, and have as clients key regulatory proteins such as transcription factors, kinases, hormone receptors, and others. The chaperone acts together with co-chaperones, which modulate and guide Hsp90 function. The co-chaperone Hop (Hsp70-Hsp90 organizing protein), interacts simultaneously with Hsp90 and Hsp70, mediating substrate transfer. Hop has three TPR domains (TPR1, and TPR2A TPR2B) responsible for interaction with the chaperones, but this interaction dynamics remains unclear, since there is no structure of full length Hop and its oligomeric state is controversial in literature reports. This work presents the classification of an Hsp90 gene from sugarcane, and primary functional characterization studies in Arabidopsis thaliana transgenic lines. We also present the biophysical characterization of the human Hsp90 co-chaperone Hop (Hsp70-Hsp90 organizing protein). Through sequence analysis the Hsp90 from sugarcane has been classified as Hsp90-3, a cytosolic isoform. Transgenic A. thaliana, produced by Hsp90-3 insertion, exhibited reduced transcript levels of Hsp90. This disruption in Hsp90 levels seems to affect the expression of other proteins from the interaction network, which are related to various processes such as immune response and photosynthesis. Transgenics also exhibited faster germination and longer roots than the control. Under heat stress, transgenic lines showed increased susceptibility to high temperature. These results suggest that Hsp90 has an important role in cellular physiology and development; in addition the levels of Hsp90 are critical for responses to stresses. The biophysical characterization of the mutant D456G Hop, a mutation in domain TPR2B showed that this protein is a mixture of monomers, dimers and higher oligomers, but the monomeric state is majoritary. The residue D456 may be involved in dimerization dynamics, and it is possible that Hop is regulated between monomeric and dimeric species, to enable its adaptor functions
Mestrado
Bioquimica
Mestre em Biologia Funcional e Molecular
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Zahn, Ralph. "Prion propagation and molecular chaperones." Zürich : Institut für Molekularbiologie und Biophysik, Eidgenössische Technische Hochschule Zürich, 2002. http://e-collection.ethbib.ethz.ch/show?type=habil&nr=4.

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Pemberton, Samantha. "Molecular chaperones in the assembly of α-Synuclein and Parkinson’s Disease." Thesis, Paris 11, 2011. http://www.theses.fr/2011PA114840/document.

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La formation et le dépôt de fibres d'α-Synucléine dans le cerveau humain sont à l‟origine de la maladie de Parkinson. Cette thèse documente le rôle de deux chaperons moléculaires dans l‟assemblage en fibres de l'α-Syn : Hsc70 (protéine de choc thermique constitutivement exprimée chez l‟Homme) et Ssa1p (son équivalent chez la levure). Le but était d'élargir le catalogue d'effets connus des chaperons moléculaires sur α-Syn, pour éventuellement ouvrir la voie à des applications thérapeutiques. Nous avons montré que Hsc70 inhibe l'assemblage de l'α-Syn en fibres, en se liant avec une forte affinité à la forme soluble de l'α-Syn. Hsc70 se lie préférentiellement aux fibres de l'α-Syn, et cette liaison a un effet cytoprotecteur puisqu'elle rend les fibres moins toxiques pour les cellules de mammifères en culture. Pareillement à Hsc70, Ssa1p inhibe l'assemblage de l'α-Syn en fibres, et a une plus forte affinité pour les fibres que pour la forme soluble de l'α-Syn. En revanche, la liaison de Ssa1p aux fibres de l'α-Syn n'a pas d'effet cytoprotecteur, sûrement due aux différences entre les séquences du site de liaison aux peptides des deux chaperons moléculaires, qui fait que Ssa1p a une affinité plus faible que Hsc70 pour les fibres d'α-Syn. Nous avons fixé le complexe entre Ssa1p et α-Syn avec des agents pontants, pour ensuite établir une carte du site d'interaction entre les deux protéines en utilisant la spectrométrie de masse. Ceci est indispensable si un « mini » Ssa1p, constitué des éléments nécessaires et suffisants sera utilisé comme agent thérapeutique pour réduire la toxicité des fibres d'α-Syn
The formation and deposition of α-Synuclein fibrils in the human brain is at the origin of Parkinson’s disease. The objective of my thesis was to document the role of two molecular chaperones on the assembly of α-Syn into fibrils: Hsc70, a constitutively expressed human heat shock protein, and Ssa1p, its yeast equivalent. The aim was to expand the catalogue of known effects of molecular chaperones on the PD implicated protein, which could have therapeutic significance. We showed that Hsc70 inhibits the assembly of α-Syn into fibrils, by binding with high affinity to the soluble form of α-Syn. We documented that Hsc70 binds preferentially to α-Syn fibrils and that this binding has a cytoprotective effect, as it renders the fibrils less toxic to cultured mammalian cells. Similarly to Hsc70, Ssa1p inhibits the assembly of α-Syn into fibrils, and has a higher affinity for fibrils than for the soluble form of α-Syn. On the other hand, binding of Ssa1p to α-Syn fibrils does not have a cytoprotective effect, almost certainly due to differences in the amino acid sequences of the peptide binding sites of the two molecular chaperones, which mean that Ssa1p has a lower affinity than Hsc70 for α-Syn fibrils. We stabilized the complex between Ssa1p and α-Syn using chemical cross-linkers, to then map the interaction site between the two proteins. This is indispensable if a “mini” Ssa1p, comprised of only what is necessary and sufficient of Ssa1p, is to be used as a therapeutic agent to decrease the toxicity of α-Syn fibrils. A therapeutic agent based on exogenous protein Ssa1p is less likely to trigger an autoimmune response than for example the endogenous protein Hsc70
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Beecham, Matthew Peter. "Supramolecular chaperones to assist protein folding." Thesis, University of Warwick, 2005. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.422081.

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Gokhale, Kavita Chandan. "Interactions between endogenous prions, chaperones and polyglutamine proteins in the yeast model." Diss., Available online, Georgia Institute of Technology, 2005, 2005. http://etd.gatech.edu/theses/available/etd-02272005-193343/unrestricted/gokhale%5Fkavita%5Fc%5F200505%5Fphd.pdf.

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Thesis (Ph. D.)--Biology, Georgia Institute of Technology, 2005.
Dr Yury Chernoff, Committee Member ; Dr Jung Choi, Committee Member ; Dr Nick Hud, Committee Member ; Dr Roger Wartell, Committee Member ; Dr Harish Radhakrishna, Committee Member. Vita. Includes bibliographical references.
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Amin-Wetzel, Niko. "Regulation of mammalian IRE1α : co-chaperones and their importance." Thesis, University of Cambridge, 2018. https://www.repository.cam.ac.uk/handle/1810/274869.

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When unfolded proteins accumulate in the endoplasmic reticulum (ER), the unfolded protein response (UPR) increases ER protein folding capacity to restore protein folding homeostasis. Unfolded proteins activate UPR signalling across the ER membrane to the nucleus by promoting oligomerisation of IRE1, a conserved transmembrane ER stress receptor. Despite significant research, the mechanism of coupling ER stress to IRE1 oligomerisation and activation has remained contested. There are two proposed mechanisms by which IRE1 may sense accumulating unfolded proteins. In the direct binding mechanism, unfolded proteins are able to bind directly to IRE1 to drive its oligomerisation. In the chaperone inhibition mechanism, unfolded proteins compete for the repressive BiP bound to IRE1 leaving IRE1 free to oligomerise. Currently, these two mechanisms respectively lack compelling in vivo and in vitro evidence required to assess their validity. The work presented here first describes in vivo experiments that identify a role of the ER co-chaperone ERdj4 as an IRE1 repressor that promotes a complex between the luminal Hsp70 BiP and the luminal stress-sensing domain of IRE1α (IRE1LD). This is then built on by a series of in vitro experiments showing that ERdj4 catalyses formation of a repressive BiP-IRE1LD complex and that this complex can be disrupted by the presence of competing unfolded protein substrates to restore IRE1LD to its default, dimeric, and active state. The identification of ERdj4 and the in vitro reconstitution of chaperone inhibition establish BiP and its J-domain co-chaperones as key regulators of the UPR. This thesis also utilises the power of Cas9-CRISPR technology to introduce specific mutations into the endogenous IRE1α locus and to screen for derepressing IRE1α mutations. Via this methodology, two predicted unstructured regions of IRE1 are found to be important for IRE1 repression. Finally, this thesis challenges recent in vitro findings concerning the direct binding mechanism.
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Seraphim, Thiago Vargas. "Estudos bioquímicos e biofísicos de proteínas de choque térmico da família Hsp40 de cana-de-açúcar e de levedura." [s.n.], 2011. http://repositorio.unicamp.br/jspui/handle/REPOSIP/314017.

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Orientador: Carlos Henrique Inacio Ramos
Dissertação (mestrado) - Universidade Estadual de Campinas, Instituto de Biologia
Made available in DSpace on 2018-08-17T21:47:21Z (GMT). No. of bitstreams: 1 Seraphim_ThiagoVargas_M.pdf: 4293116 bytes, checksum: bd401fff62b6ce29029ac35de3bc753a (MD5) Previous issue date: 2011
Resumo: O enovelamento protéico é essencial para a correta função biológica das proteínas. A existência de um ambiente com alta concentração dos mais diferentes tipos de moléculas, dentro da célula, e de diversos tipos de situações de estresse, podem agir induzindo a formação de espécies improdutivas na via de enovelamento, como proteínas mal enoveladas e/ou até mesmo agregados protéicos. Para controlar estes eventos, há a maquinaria de chaperonas moleculares, que tem por objetivo garantir a homeostase protéica celular. As chaperonas moleculares são capazes de ligar e estabilizar um polipeptídio, mas sem contribuir com informações para a sua conformação final. Dentro desta maquinaria, o sistema Hsp70 tem um papel central, sendo responsável por receber proteínas desenoveladas ou mal enoveladas de outras chaperonas, podendo auxiliar no reenovelamento e direcionamento para outras chaperonas moleculares ou para degradação. A Hsp70 é regulada por co-chaperonas, como a Hsp40, que é responsável pela entrega de proteínas clientes à Hsp70 e pelo estímulo da atividade ATPase, essencial para a funcionalidade da Hsp70. Este trabalho apresenta a caracterização de uma Hsp40 tipo I de cana-de-açúcar, nomeada SHsp40, e o estudo de uma Hsp40 tipo II de levedura e seus mutantes, a fim de entender a relação estrutura-função destas proteínas. A SHsp40 foi expressa em E. coli, purificada e obtida enovelada, como verificado por dicroísmo circular. Além disso, a SHsp40 apresentou atividade chaperona em experimentos de proteção ao substrato desenovelado e se comportou como um dímero alongado em solução, como mostrado por SEC-MALS e pela determinação do fator de Perrin. Experimentos de desenovelamento térmico monitorado pelo sinal de CD a 222 nm revelaram que a SHsp40 possui pelo menos um intermediário, e a fluorescência de tioflavina T e bis-ANS mostraram que este intermediário é rico em folhas ? e parcialmente desenovelado, características de espécies na via de formação de fibrilas. A SHsp40 agregada foi examinada por microscopia eletrônica de varredura, que comprovou sua capacidade de formar de fibrilas. Este trabalho também contribuiu para o estudo de uma Hsp40 tipo II de levedura, Sis1, e seus mutantes de deleção, Sis1?124-174 e Sis1?121-257. Ensaios de fluorescência estática do triptofano, fotoapagamento e anisotropia mostraram que a deleção do domínio G/M não afetou a estrutura e hidrodinâmica de Sis1?124-174 em relação à proteína selvagem. Estudos de estabilidade destas proteínas, realizado anteriormente em nosso grupo de pesquisa e complementado neste trabalho pelo uso da técnica de SEC-MALS, mostrou que Sis1 e Sis1?124-174 foram mais estáveis que Sis1?121-257, mutante que o domínio G/M e subdomínio CTDI estão ausentes
Abstract: Correct protein folding is essential for proper protein biological function. There is a crowded environment and many types of molecules inside the cell and a variety of external stresses can act inducing unproductive species, as unfolded and/or misfolded proteins and even protein aggregates. To control these undesired events and ensures the protein homeostasis there is a molecular chaperone machinery. Molecular chaperones are able to bind and stabilize polypeptides but with no contributions for their final conformations. Inside this machinery, the Hsp70 system has a central role and is responsible to receive unfolded or misfolded proteins from other chaperones, helping in protein refolding and delivering the clients to other chaperones and even protein targeting for degradation. Hsp70 is regulated by its co-chaperones, such as Hsp40, which is responsible to client proteins deliver to Hsp70 and stimulation of its ATPase activity, essential processes for Hsp70 function. This work presents a sugarcane type I Hsp40 characterization, named SHsp40, and studies of an yeast type II Hsp40 and its mutants in order to understand the structure-function relationship of these proteins. The SHsp40 was expressed in E. coli, purified and obtained folded, as verified by circular dichroism. Furthermore, SHsp40 presented chaperone activity in unfolded substrate protection experiments and behaved as an elongated dimer in solution, as shown by SEC-MALS and estimated by Perrin factor. Thermal-induced unfolding experiments monitored by CD signal at 222 nm revealed that SHsp40 has at least one intermediate which is populated and tioflavin T and bis-ANS fluorescence showed that this intermediate is ? sheet-rich and partially folded, such as intermediate species in the fibril formation pathway. The aggregated SHsp40 was examined by scanning electron microscopy, wich proved its ability to fibril formation. This work also contributed for the study of an yeast type II Hsp40, Sis1, and its deletion mutants, Sis1?124-174 and Sis1?121-257. Steady-state tryptophan fluorescence, quenching and anisotropy assays showed that the G/M domain deletion did not affect the structure and hydrodynamic properties of Sis1?124-174 in relation to the wild type protein. Stability studies of these proteins, previously performed in our research group and complemented in this work by using the SEC-MALS technique, showed that Sis1 and Sis1?124-174 were more stable than Sis1?121-257, a mutant with the G/M domain and CTDI subdomain absents
Mestrado
Bioquimica
Mestre em Biologia Funcional e Molecular
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Coto, Amanda Laís de Souza. "Estudo estrutural e funcional da co-chaperona SGT de Leishmania braziliensis." Universidade de São Paulo, 2016. http://www.teses.usp.br/teses/disponiveis/75/75133/tde-17112016-135653/.

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As chaperonas moleculares são ativas em muitos processos celulares envolvendo o enovelamento e a homeostase de proteínas. Essas características fazem das chaperonas alvos potenciais para o tratamento de diversas doenças. As Hsp70 e as Hsp90, em especial, são proteínas ubíquas altamente conservadas biologicamente que atuam no enovelamento de proteínas nascentes, prevenção da agregação proteica, recuperação de proteínas de agregados, sinalização e crescimento celular, dentre outros. Contudo, para que essas proteínas cumpram eficientemente suas funções, elas devem ser moduladas por co-chaperonas moleculares. A SGT é uma co-chaperona que pode ser dividida em três regiões: domínio N-terminal, domínio TPR e domínio C-terminal, sendo que a região do domínio TPR é a responsável pela interação com o motivo EEVD no C-terminal das Hsp90 e Hsp70 citoplasmáticas. A SGT é encontrada em vários organismos, dentre eles os protozoários do gênero Leishmania spp.. Estes organismos são responsáveis pela leishmaniose, uma doença negligenciada que afeta milhares de pessoas todos os anos, principalmente em países subdesenvolvidos. Evidências indicam que a SGT em protozoários é essencial para o crescimento e viabilidade da forma promastigota. Diante disso, nesse trabalho foi feito o estudo estrutural e funcional da co-chaperona SGT de Leishmania braziliensis (LbSGT). A LbSGT recombinante foi produzida e purificada. A caracterização estrutural indica que a LbSGT é uma proteína rica em estrutura secundária do tipo hélice α que se comporta como um dímero alongado em solução. Dados de estabilidade térmica e química indicam que a LbSGT é uma proteína formada por domínios com diferentes estabilidades. A LbSGT foi identificada in vivo e o western blotting indicou sua presença cognata nas formas promastigotas do protozoário. Os ensaios de interação indicam que as interações entre a LbSGT e a Hsp90 de L. braziliensis (LbHsp90) e a LbSGT e Hsp70-1A humana (usada como proteína modelo) são diferentes da interação da LbSGT com o peptídeo MEEVD. Sendo assim, esses dados sugerem que a interação da LbSGT com a Hsp70-1A e LbHsp90 envolvem mais regiões das proteínas do que somente o motivo de interação da Hsp70-1A e da LbHsp90 com o domínio TPR da LbSGT. Em conjunto, as propriedades estruturais e funcionais da LbSGT observadas estão de acordo com a possível função da SGT como proteína adaptadora entre os sistemas Hsp70 e Hsp90 no foldossoma.
The molecular chaperones are active in many cellular processes involving protein folding and homeostasis. These characteristics make the chaperones potential targets to the treatment of many diseases. Hsp70 and Hsp90, in special, are highly conserved ubiquitous proteins that act in the folding of nascent proteins, protein aggregation prevention, aggregate recovering, signaling and cellular growth, among others. However, for these proteins to effectively fulfill their function, they must be modulated by molecular co-chaperones. SGT is a co-chaperone that can be divided into three domains: a N-terminal domain, a TPR domain and a C-terminal domain, being the TPR domain responsible for the interaction with the EEVD motif at the C-terminus of cytoplasmic Hsp90 and Hsp70. SGT is found in various organisms; among they are the protozoans of Leishmania spp.. These organisms are responsible for leishmaniasis, a neglected disease that affects thousands people every year, mainly at underdeveloped countries. Evidences indicate that SGT in protozoans are essential to the growth and viability of promastigote form. Therefore, the structural and functional study of the Leishmania braziliensis SGT (LbSGT) is presented. Recombinant LbSGT was produced and purified. The structural characterization points that LbSGT is rich in α-helix secondary structure and behaves as an elongated dimer in solution. Chemical and thermal stability data suggest that LbSGT is formed by domains of different stabilities. LbSGT was identified in vivo and the western blotting indicates its cognate presence in the protozoan promastigote forms. The interaction assays show that the interaction between LbSGT and Hsp90 of L. braziliensis (LbHsp90) or human Hsp70-1A (used as model protein) were different from the interaction between LbSGT with MEEVD peptide. Moreover, these data suggests that the interaction between LbSGT and Hsp70-1A and LbHsp90 involves additional protein regions besides the Hsp70-1A and LbHsp90 interaction motif. Altogether, the observed functional and structural proprieties of LbSGT accord to the SGT possible function as an adapter protein between the Hsp70 and Hsp90 systems in the foldossome.
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Books on the topic "Chaperones"

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Braakman, Ineke, ed. Chaperones. Berlin, Heidelberg: Springer Berlin Heidelberg, 2006. http://dx.doi.org/10.1007/b100697.

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Calderwood, Stuart K., and Thomas L. Prince, eds. Chaperones. New York, NY: Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-7477-1.

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Calderwood, Stuart K., and Thomas L. Prince, eds. Chaperones. New York, NY: Springer US, 2023. http://dx.doi.org/10.1007/978-1-0716-3342-7.

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Blatch, Gregory L. Networking of Chaperones by Co-Chaperones. New York, NY: Springer New York, 2007. http://dx.doi.org/10.1007/978-0-387-49310-7.

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L, Blatch Gregory, ed. Networking of chaperones by co-chaperones. Austin, Tex: Landes Bioscience/Eurekah.com, 2007.

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Blatch, Gregory Lloyd, and Adrienne Lesley Edkins, eds. The Networking of Chaperones by Co-chaperones. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-11731-7.

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Edkins, Adrienne L., and Gregory L. Blatch, eds. The Networking of Chaperones by Co-Chaperones. Cham: Springer International Publishing, 2023. http://dx.doi.org/10.1007/978-3-031-14740-1.

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Heise, Tilman, ed. RNA Chaperones. New York, NY: Springer US, 2020. http://dx.doi.org/10.1007/978-1-0716-0231-7.

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Ellis, R. J., R. A. Laskey, and G. H. Lorimer, eds. Molecular Chaperones. Dordrecht: Springer Netherlands, 1993. http://dx.doi.org/10.1007/978-94-011-2108-8.

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Calderwood, Stuart K., and Thomas L. Prince, eds. Molecular Chaperones. Totowa, NJ: Humana Press, 2011. http://dx.doi.org/10.1007/978-1-61779-295-3.

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Book chapters on the topic "Chaperones"

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de Jonge, Wim, Henk F. Tabak, and Ineke Braakman. "Chaperone proteins and peroxisomal protein import." In Chaperones, 149–83. Berlin, Heidelberg: Springer Berlin Heidelberg, 2005. http://dx.doi.org/10.1007/b136669.

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Bousset, Luc, Nicolas Fay, and Ronald Melki. "Template-induced protein misfolding underlying prion diseases." In Chaperones, 221–50. Berlin, Heidelberg: Springer Berlin Heidelberg, 2005. http://dx.doi.org/10.1007/4735_107.

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Fasman, Gerald D. "Chaperones." In Circular Dichroism and the Conformational Analysis of Biomolecules, 531–54. Boston, MA: Springer US, 1996. http://dx.doi.org/10.1007/978-1-4757-2508-7_15.

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Zimmermann, Richard. "Chaperones." In Encyclopedia of Molecular Pharmacology, 1–5. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-21573-6_238-1.

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Zimmermann, Richard. "Chaperones." In Encyclopedia of Molecular Pharmacology, 439–44. Cham: Springer International Publishing, 2021. http://dx.doi.org/10.1007/978-3-030-57401-7_238.

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Cohen, G. N. "The Ribosomes, Translation, Chaperones and Chaperonins." In Microbial Biochemistry, 235–45. Dordrecht: Springer Netherlands, 2014. http://dx.doi.org/10.1007/978-94-017-8908-0_19.

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Dods, Richard. "Chaperones/Chaperonins, Tertiary, and Quaternary Structure." In Concepts in Bioscience Engineering, 127–50. Cham: Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-28303-2_4.

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Ellis, R. J. "The general concept of molecular chaperones." In Molecular Chaperones, 1–5. Dordrecht: Springer Netherlands, 1993. http://dx.doi.org/10.1007/978-94-011-2108-8_1.

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Dierks, T., P. Klappa, H. Wiech, and R. Zimmerman. "The role of molecular chaperones in protein transport into the endoplasmic reticulum." In Molecular Chaperones, 79–85. Dordrecht: Springer Netherlands, 1993. http://dx.doi.org/10.1007/978-94-011-2108-8_10.

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Hardy, S. J. S., and L. L. Randall. "Recognition of ligands by SecB, a molecular chaperone involved in bacterial protein export." In Molecular Chaperones, 87–98. Dordrecht: Springer Netherlands, 1993. http://dx.doi.org/10.1007/978-94-011-2108-8_11.

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Conference papers on the topic "Chaperones"

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Strickland, T. Stephen, Sam Tobin-Hochstadt, Robert Bruce Findler, and Matthew Flatt. "Chaperones and impersonators." In the ACM international conference. New York, New York, USA: ACM Press, 2012. http://dx.doi.org/10.1145/2384616.2384685.

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Abakumets, V., N. Bogdanova, R. Baranovskiy, and K. Bulanava. "THE ROLE OF CHAPERONES IN DIABETES MELLITUS." In SAKHAROV READINGS 2020: ENVIRONMENTAL PROBLEMS OF THE XXI CENTURY. Minsk, ICC of Minfin, 2020. http://dx.doi.org/10.46646/sakh-2020-2-10-14.

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Kumar, A., D. Souza De Lima, Z. Mark, and V. Anathy. "Lung Epithelial Redox Chaperones in Human Coronavirus Propagation." In American Thoracic Society 2023 International Conference, May 19-24, 2023 - Washington, DC. American Thoracic Society, 2023. http://dx.doi.org/10.1164/ajrccm-conference.2023.207.1_meetingabstracts.a5663.

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Massaeli, Hamid, Divya Viswanathan, Dhanya Pillai, and Nasrin Mesaeli. "Regulation Of Caveolin-dependent Endocytosis By Endoplasmic Reticulum Chaperones." In Qatar Foundation Annual Research Conference Proceedings. Hamad bin Khalifa University Press (HBKU Press), 2014. http://dx.doi.org/10.5339/qfarc.2014.hbpp1034.

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Workman, P. "Abstract BSF2-1: Molecular Chaperones: Cancer Dependence and Druggability." In Abstracts: Thirty-Third Annual CTRC‐AACR San Antonio Breast Cancer Symposium‐‐ Dec 8‐12, 2010; San Antonio, TX. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/0008-5472.sabcs10-bsf2-1.

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Gounari, Eleni, Romanie Hannah, and Frances Howsham. "697 Chaperones in paediatrics – are we thinking about it?" In Royal College of Paediatrics and Child Health, Abstracts of the RCPCH Conference–Online, 15 June 2021–17 June 2021. BMJ Publishing Group Ltd and Royal College of Paediatrics and Child Health, 2021. http://dx.doi.org/10.1136/archdischild-2021-rcpch.148.

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Takami, Tomohide, Jun-ichi Uewaki, Hiroshi Ochiai, Masato Koyama, Yoshihide Ogawa, Mikako Saito, Hideaki Matsuoka, and Shin-ichi Tate. "Live Dynamics on Femtoinjection of GFP-Tagged Nucleosome Chaperones into HeLa Cell." In JSAP-OSA Joint Symposia. Washington, D.C.: OSA, 2014. http://dx.doi.org/10.1364/jsap.2014.18p_c4_12.

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Truskett, Thomas M. "How Concentration and Crowding Impact Protein Stability: Insights From a Coarse-Grained Model." In ASME 2008 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2008. http://dx.doi.org/10.1115/sbc2008-192239.

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Much of the current understanding of the protein folding problem derives from studies of proteins in dilute solutions. However, in many systems of scientific and engineering interest, proteins must fold in concentrated, heterogeneous environments. Cells are crowded with many molecular species, and chaperones often sequester proteins and promote rapid folding. Proteins are also present in high concentrations in the manufacture, storage, and delivery of biotherapeutics. How does crowding generally affect the stability of the native state? Are all crowding agents created equal? If not, can generic structural or chemical features forecast their effects on protein stability?
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Suckling, Lorna AB, Marissa Powers, Swee Sharp, and Paul Workman. "Abstract 4772: Addiction to chaperones: Investigating the role of HSP70 isoforms in cancer." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-4772.

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Sarkar, Saugata, and Marissa Nichole Rylander. "Treatment Planning Model for Nanotube-Mediated Laser Cancer Therapy." In ASME 2008 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2008. http://dx.doi.org/10.1115/sbc2008-192997.

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The goal of the project is to develop an effective treatment planning computational tool for nanotube-mediated laser therapy that maximizes tumor destruction and minimizes tumor recurrence. Laser therapies can provide a minimally invasive treatment alternative to surgical resection of tumors. However, the effectiveness of these therapies is limited due to nonspecific heating of target tissue and diffusion limited thermal deposition which often leads to healthy tissue injury and extended treatment durations. These therapies can be further compromised due to induction of molecular chaperones called heat shock protein (HSP) in tumor regions where non-lethal temperature elevation occurs causing enhanced tumor cell viability and imparting resistance to chemotherapy and radiation treatments which are generally employed in conjunction with hyperthermia.
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Reports on the topic "Chaperones"

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Robb, Frank T. Mechanisms of Stability of Robust Chaperones from Hyperthermophiles. Fort Belvoir, VA: Defense Technical Information Center, February 2009. http://dx.doi.org/10.21236/ada586573.

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Takayama, Shin-ichi. BAG Family Proteins: Regulators of Cancer Cell Growth Through Molecular Chaperones. Fort Belvoir, VA: Defense Technical Information Center, June 2001. http://dx.doi.org/10.21236/ada398188.

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Takayama, Shinichi. BAG Family Proteins: Regulators of Cancer Cell Growth Through Molecular Chaperones. Fort Belvoir, VA: Defense Technical Information Center, June 2002. http://dx.doi.org/10.21236/ada407556.

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Azem, Abdussalam, George Lorimer, and Adina Breiman. Molecular and in vivo Functions of the Chloroplast Chaperonins. United States Department of Agriculture, June 2011. http://dx.doi.org/10.32747/2011.7697111.bard.

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We present here the final report for our research project entitled "The molecular and in vivo functions of the chloroplast chaperonins”. Over the past few decades, intensive investigation of the bacterial GroELS system has led to a basic understanding of how chaperonins refold denatured proteins. However, the parallel is limited in its relevance to plant chaperonins, since the plant system differs from GroEL in genetic complexity, physiological roles of the chaperonins and precise molecular structure. Due to the importance of plant chaperonins for chloroplast biogenesis and Rubisco assembly, research on this topic will have implications for many vital applicative fields such as crop hardiness and efficiency of plant growth as well as the production of alternative energy sources. In this study, we set out to investigate the structure and function of chloroplast chaperonins from A. thaliana. Most plants harbor multiple genes for chaperonin proteins, making analysis of plant chaperonin systems more complicated than the GroEL-GroES system. We decided to focus on the chaperonins from A. thaliana since the genome of this plant has been well defined and many materials are available which can help facilitate studies using this system. Our proposal put forward a number of goals including cloning, purification, and characterization of the chloroplast cpn60 subunits, antibody preparation, gene expression patterns, in vivo analysis of oligomer composition, preparation and characterization of plant deletion mutants, identification of substrate proteins and biophysical studies. In this report, we describe the progress we have made in understanding the structure and function of chloroplast chaperonins in each of these categories.
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van Wijk, Klaas. Proteolysis in Plastids of Arabidopsis Thaliana: Functional Analysis of ClpS1,2,T and their Physical and Genetic Interactions with the ClpPR Protease Core Complex and Clp Chaperones. Office of Scientific and Technical Information (OSTI), January 2009. http://dx.doi.org/10.2172/971250.

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Tzfira, Tzvi, Michael Elbaum, and Sharon Wolf. DNA transfer by Agrobacterium: a cooperative interaction of ssDNA, virulence proteins, and plant host factors. United States Department of Agriculture, December 2005. http://dx.doi.org/10.32747/2005.7695881.bard.

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Agrobacteriumtumefaciensmediates genetic transformation of plants. The possibility of exchanging the natural genes for other DNA has led to Agrobacterium’s emergence as the primary vector for genetic modification of plants. The similarity among eukaryotic mechanisms of nuclear import also suggests use of its active elements as media for non-viral genetic therapy in animals. These considerations motivate the present study of the process that carries DNA of bacterial origin into the host nucleus. The infective pathway of Agrobacterium involves excision of a single-stranded DNA molecule (T-strand) from the bacterial tumor-inducing plasmid. This transferred DNA (T-DNA) travels to the host cell cytoplasm along with two virulence proteins, VirD2 and VirE2, through a specific bacteriumplant channel(s). Little is known about the precise structure and composition of the resulting complex within the host cell and even less is known about the mechanism of its nuclear import and integration into the host cell genome. In the present proposal we combined the expertise of the US and Israeli labs and revealed many of the biophysical and biological properties of the genetic transformation process, thus enhancing our understanding of the processes leading to nuclear import and integration of the Agrobacterium T-DNA. Specifically, we sought to: I. Elucidate the interaction of the T-strand with its chaperones. II. Analyzing the three-dimensional structure of the T-complex and its chaperones in vitro. III. Analyze kinetics of T-complex formation and T-complex nuclear import. During the past three years we accomplished our goals and made the following major discoveries: (1) Resolved the VirE2-ssDNA three-dimensional structure. (2) Characterized VirE2-ssDNA assembly and aggregation, along with regulation by VirE1. (3) Studied VirE2-ssDNA nuclear import by electron tomography. (4) Showed that T-DNA integrates via double-stranded (ds) intermediates. (5) Identified that Arabidopsis Ku80 interacts with dsT-DNA intermediates and is essential for T-DNA integration. (6) Found a role of targeted proteolysis in T-DNA uncoating. Our research provide significant physical, molecular, and structural insights into the Tcomplex structure and composition, the effect of host receptors on its nuclear import, the mechanism of T-DNA nuclear import, proteolysis and integration in host cells. Understanding the mechanical and molecular basis for T-DNA nuclear import and integration is an essential key for the development of new strategies for genetic transformation of recalcitrant plant species. Thus, the knowledge gained in this study can potentially be applied to enhance the transformation process by interfering with key steps of the transformation process (i.e. nuclear import, proteolysis and integration). Finally, in addition to the study of Agrobacterium-host interaction, our research also revealed some fundamental insights into basic cellular mechanisms of nuclear import, targeted proteolysis, protein-DNA interactions and DNA repair.
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Nelson, Nathan, and Randy Schekman. Functional Biogenesis of V-ATPase in the Vacuolar System of Plants and Fungi. United States Department of Agriculture, September 1996. http://dx.doi.org/10.32747/1996.7574342.bard.

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The vacuolar H+-ATPase (V-ATPase) is one of the most fundamental enzymes in nature. It pumps protons into the vacuolar system of eukaryotic cells and provides the energy for numerous transport systems. Through our BARD grant we discovered a novel family of membrane chaperones that modulate the amount of membrane proteins. We also elucidated the mechanism by which assembly factors guide the membrane sector of V-ATPase from the endoplasmic reticulum to the Golgi apparatus. The major goal of the research was to understand the mechanism of action and biogenesis of V-ATPase in higher plants and fungi. The fundamental question of the extent of acidification in organelles of the vacuolar system was addressed by studying the V-ATPase of lemon fruit, constructing lemon cDNAs libraries and study their expression in mutant yeast cells. The biogenesis of the enzyme and its function in the Golgi apparatus was studied in yeast utilizing a gallery of secretory mutants available in our laboratories. One of the goals of this project is to determine biochemically and genetically how V-ATPase is assembled into the different membranes of a wide variety of organelles and what is the mechanism of its action.The results of this project advanced out knowledge along these lines.
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Muga, Arturo. Asociaciones funcionales de chaperonas. Sociedad Española de Bioquímica y Biología Molecular (SEBBM), January 2012. http://dx.doi.org/10.18567/sebbmdiv_anc.2012.01.1.

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Vierling, Elizabeth. Hsp100/ClpB Chaperone Function and Mechanism. Office of Scientific and Technical Information (OSTI), January 2015. http://dx.doi.org/10.2172/1168677.

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Paschal, Bryce M. Chaperone Function in Androgen-Independent Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, May 2010. http://dx.doi.org/10.21236/ada542323.

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