Relevant bibliographies by topics / Ubiquitin

Contents

  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'Ubiquitin'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 August 2024

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'Ubiquitin.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Journal articles on the topic "Ubiquitin"

1

Kama, Rachel, Galina Gabriely, Vydehi Kanneganti, and Jeffrey E. Gerst. "Cdc48 and ubiquilins confer selective anterograde protein sorting and entry into the multivesicular body in yeast." Molecular Biology of the Cell 29, no. 8 (April 15, 2018): 948–63. http://dx.doi.org/10.1091/mbc.e17-11-0652.

Full text
Abstract:
Cdc48/p97 is known primarily for the retrotranslocation of misfolded proteins in endoplasmic reticulum (ER)-associated protein degradation (ERAD). Here we uncover a novel function for both Cdc48 and the conserved ubiquitin-associated/ubiquitin-like ubiquitin receptor (ubiquilin) proteins in yeast (e.g., Ddi1, Dsk2, and Rad23), which deliver ubiquitinated proteins to the proteasome for degradation. We show that Cdc48, its core adaptors Npl4 and Ufd1, and the ubiquilins confer the constitutive anterograde delivery of carboxypeptidase S (Cps1), a membranal hydrolase, to the multivesicular body (MVB) and vacuolar lumen. Cdc48 and Ddi1 act downstream of Rsp5-dependent Cps1 ubiquitination to facilitate the disassembly of insoluble Cps1 oligomers and upstream of ESCRT-0 to facilitate the entry of soluble protein into the MVB. Consequentially, detergent-insoluble Cps1 accumulates in cells bearing mutations in CDC48, DDI1, and all three ubiquilins (ddi1Δ, dsk2Δ, rad23Δ). Thus, Cdc48 and the ubiquilins have ERAD- and proteasome-independent functions in the anterograde delivery of specific proteins to the yeast vacuole for proteolytic activation. As Cdc48/p97 and the ubiquilins are major linkage groups associated with the onset of human neurodegenerative disease (e.g., amytrophic lateral sclerosis, Alzheimer’s, and Paget’s disease of the bone), there may be a connection between their involvement in anterograde protein sorting and disease pathogenesis.
APA, Harvard, Vancouver, ISO, and other styles
2

Lee, Dong Yun, and Eric J. Brown. "Ubiquilins in the crosstalk among proteolytic pathways." Biological Chemistry 393, no. 6 (June 1, 2012): 441–47. http://dx.doi.org/10.1515/hsz-2012-0120.

Full text
Abstract:
Abstract Protein degradation occurs through several distinct proteolytic pathways for membrane and cytosolic proteins. There is evidence that these processes are linked and that crosstalk among these major protein degradation pathways occurs. Ubiquilins, a family of ubiquitin-binding proteins, are involved in all protein degradation pathways. This minireview provides an overview of ubiquilin function in protein degradation and contrasts it with sequestosome-1 (p62), a protein that also has been implicated in multiple proteolytic pathways.
APA, Harvard, Vancouver, ISO, and other styles
3

Jantrapirom, Salinee, Luca Lo Piccolo, Dumnoensun Pruksakorn, Saranyapin Potikanond, and Wutigri Nimlamool. "Ubiquilin Networking in Cancers." Cancers 12, no. 6 (June 15, 2020): 1586. http://dx.doi.org/10.3390/cancers12061586.

Full text
Abstract:
Ubiquilins or UBQLNs, members of the ubiquitin-like and ubiquitin-associated domain (UBL-UBA) protein family, serve as adaptors to coordinate the degradation of specific substrates via both proteasome and autophagy pathways. The UBQLN substrates reveal great diversity and impact a wide range of cellular functions. For decades, researchers have been attempting to uncover a puzzle and understand the role of UBQLNs in human cancers, particularly in the modulation of oncogene’s stability and nucleotide excision repair. In this review, we summarize the UBQLNs’ genetic variants that are associated with the most common cancers and also discuss their reliability as a prognostic marker. Moreover, we provide an overview of the UBQLNs networks that are relevant to cancers in different ways, including cell cycle, apoptosis, epithelial-mesenchymal transition, DNA repairs and miRNAs. Finally, we include a future prospective on novel ubiquilin-based cancer therapies.
APA, Harvard, Vancouver, ISO, and other styles
4

Hurtley, Stella M. "One Ubiquitin, Two Ubiquitin, Three Ubiquitin, Four." Science's STKE 2007, no. 369 (January 16, 2007): tw26. http://dx.doi.org/10.1126/stke.3692007tw26.

Full text
Abstract:
The role of protein ubiquitination is well known in promoting regulated protein degradation. Mukhopadhyay and Riezman review what is known about the contribution of protein ubiquitination in other cellular pathways, including intracellular signaling, endocytosis, and protein sorting.D. Mukhopadhyay, H. Riezman, Proteasome-independent functions of ubiquitin in endocytosis and signaling. Science315, 201-205 (2007). [Abstract][Full Text]
APA, Harvard, Vancouver, ISO, and other styles
5

Hill, Spencer, Joseph S. Harrison, Steven M. Lewis, Brian Kuhlman, and Gary Kleiger. "Mechanism of Lysine 48 Selectivity during Polyubiquitin Chain Formation by the Ube2R1/2 Ubiquitin-Conjugating Enzyme." Molecular and Cellular Biology 36, no. 11 (April 4, 2016): 1720–32. http://dx.doi.org/10.1128/mcb.00097-16.

Full text
Abstract:
Lysine selectivity is of critical importance during polyubiquitin chain formation because the identity of the lysine controls the biological outcome. Ubiquitins are covalently linked in polyubiquitin chains through one of seven lysine residues on its surface and the C terminus of adjacent protomers. Lys 48-linked polyubiquitin chains signal for protein degradation; however, the structural basis for Lys 48 selectivity remains largely unknown. The ubiquitin-conjugating enzyme Ube2R1/2 has exquisite specificity for Lys 48, and computational docking of Ube2R1/2 and ubiquitin predicts that Lys 48 is guided to the active site through a key electrostatic interaction between Arg 54 on ubiquitin and Asp 143 on Ube2R1/2. The validity of this interaction was confirmed through biochemical experiments. Since structural examples involving Arg 54 in protein-ubiquitin complexes are exceedingly rare, these results provide additional insight into how ubiquitin-protein complexes can be stabilized. We discuss how these findings relate to how other ubiquitin-conjugating enzymes direct the lysine specificity of polyubiquitin chains.
APA, Harvard, Vancouver, ISO, and other styles
6

Ford, Diana L., and Mervyn J. Monteiro. "Dimerization of ubiquilin is dependent upon the central region of the protein: evidence that the monomer, but not the dimer, is involved in binding presenilins." Biochemical Journal 399, no. 3 (October 13, 2006): 397–404. http://dx.doi.org/10.1042/bj20060441.

Full text
Abstract:
Ubiquilin proteins have been shown to interact with a wide variety of other cellular proteins, often regulating the stability and degradation of the interacting protein. Ubiquilin contains a UBL (ubiquitin-like) domain at the N-terminus and a UBA (ubiquitin-associated) domain at the C-terminus, separated by a central region containing Sti1-like repeats. Little is known about regulation of the interaction of ubiquilin with other proteins. In the present study, we show that ubiquilin is capable of forming dimers, and that dimerization requires the central region of ubiquilin, but not its UBL or the UBA domains. Furthermore, we provide evidence suggesting that monomeric ubiquilin is likely to be the active form that is involved in binding presenilin proteins. Our results provide new insight into the regulatory mechanism underlying the interaction of ubiquilin with presenilins.
APA, Harvard, Vancouver, ISO, and other styles
7

Seok Ko, Han, Takashi Uehara, Kazuhiro Tsuruma, and Yasuyuki Nomura. "Ubiquilin interacts with ubiquitylated proteins and proteasome through its ubiquitin-associated and ubiquitin-like domains." FEBS Letters 566, no. 1-3 (April 28, 2004): 110–14. http://dx.doi.org/10.1016/j.febslet.2004.04.031.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

Chatrin, Chatrin, Mads Gabrielsen, Lori Buetow, Mark A. Nakasone, Syed F. Ahmed, David Sumpton, Gary J. Sibbet, Brian O. Smith, and Danny T. Huang. "Structural insights into ADP-ribosylation of ubiquitin by Deltex family E3 ubiquitin ligases." Science Advances 6, no. 38 (September 2020): eabc0418. http://dx.doi.org/10.1126/sciadv.abc0418.

Full text
Abstract:
Cellular cross-talk between ubiquitination and other posttranslational modifications contributes to the regulation of numerous processes. One example is ADP-ribosylation of the carboxyl terminus of ubiquitin by the E3 DTX3L/ADP-ribosyltransferase PARP9 heterodimer, but the mechanism remains elusive. Here, we show that independently of PARP9, the conserved carboxyl-terminal RING and DTC (Deltex carboxyl-terminal) domains of DTX3L and other human Deltex proteins (DTX1 to DTX4) catalyze ADP-ribosylation of ubiquitin’s Gly76. Structural studies reveal a hitherto unknown function of the DTC domain in binding NAD+. Deltex RING domain recruits E2 thioesterified with ubiquitin and juxtaposes it with NAD+ bound to the DTC domain to facilitate ADP-ribosylation of ubiquitin. This ubiquitin modification prevents its activation but is reversed by the linkage nonspecific deubiquitinases. Our study provides mechanistic insights into ADP-ribosylation of ubiquitin by Deltex E3s and will enable future studies directed at understanding the increasingly complex network of ubiquitin cross-talk.
APA, Harvard, Vancouver, ISO, and other styles
9

Morgan, Rachel E., Vijay Chudasama, Paul Moody, Mark E. B. Smith, and Stephen Caddick. "A novel synthetic chemistry approach to linkage-specific ubiquitin conjugation." Organic & Biomolecular Chemistry 13, no. 14 (2015): 4165–68. http://dx.doi.org/10.1039/c5ob00130g.

Full text
APA, Harvard, Vancouver, ISO, and other styles
10

Ikeda, Hiromi, and Tom K. Kerppola. "Lysosomal Localization of Ubiquitinated Jun Requires Multiple Determinants in a Lysine-27–Linked Polyubiquitin Conjugate." Molecular Biology of the Cell 19, no. 11 (November 2008): 4588–601. http://dx.doi.org/10.1091/mbc.e08-05-0496.

Full text
Abstract:
Ubiquitination regulates many cellular functions, including protein localization and degradation. Each function is specified by unique determinants in the conjugate. Ubiquitinated Jun is localized to lysosomes for degradation. Here, we characterized determinants of Jun ubiquitination and lysosomal localization by using ubiquitin-mediated fluorescence complementation (UbFC) in living cells and analysis of the stoichiometry of ubiquitin linked to Jun extracted from cells. The δ region of Jun and isoleucine-44 in ubiquitin were required for lysosomal localization of the conjugate. Ubiquitin containing only lysine-27, but no other single-lysine ubiquitin, mediated Jun ubiquitination, albeit at lower stoichiometry than wild-type ubiquitin. These conjugates were predominantly nuclear, but coexpression of lysine-27 and lysine-less ubiquitins enhanced the mean stoichiometry of Jun ubiquitination and lysosomal localization of the conjugate. Hepatocyte growth factor-regulated tyrosine kinase substrate (HRS) and tumor susceptibility gene 101 (TSG101) colocalized with ubiquitinated Jun. Knockdown of HRS or TSG101 inhibited lysosomal localization of ubiquitinated Jun and reduced Jun turnover. Ubiquitination of other Fos and Jun family proteins had distinct effects on their localization. Our results indicate that Jun is polyubiquitinated by E3 ligases that produce lysine-27–linked chains. Lysosomal localization of the conjugate requires determinants in Jun and in ubiquitin that are recognized in part by TSG101 and HRS, facilitating selective translocation and degradation of ubiquitinated Jun.
APA, Harvard, Vancouver, ISO, and other styles
More sources

Dissertations / Theses on the topic "Ubiquitin"

1

Sekiyama, Naotaka. "STRUCTURAL ANALYSIS OF UBIQUITIN AND UBIQUITIN-LIKE PROTEIN RECEPTORS." 京都大学 (Kyoto University), 2010. http://hdl.handle.net/2433/120884.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Braxton, Courtney N. "The progress on mapping ubiquitin signaling using photocrosslinking mono and di-ubiquitin probes and other ubiquitin moieties." VCU Scholars Compass, 2018. https://scholarscompass.vcu.edu/etd/5382.

Full text
Abstract:
Ubiquitin (Ub) is a small, 76 amino acid, and post-translational modification (PTM) protein in eukaryotes. Modification of a substrate protein via the covalent attachment of the C-terminal glycine of Ub to the ε-amino group of lysine residues in a substrate is termed ubiquitination. Unlike, other PTM proteins, Ub can form polyUb chains at one or more of its seven lysine residues. (K6, K11, K27, K29, K33, K48, and K68). The consequence of these different polymerization sites is altered biological response with different polyUb linkages conferring different fates to target proteins. Unfortunately, the study of these chains have been limited by the inability to generate homogeneous polyUbs chains linked at known lysine residues. Furthermore, a three step enzymatic cascade consisting of activating-enzymes (E1s), conjugating enzymes (E2s), and ligase enzymes (E3s) tightly controls this modification. In response, our laboratory has developed a system that creates polyUb chains through bacterial expression and "synthetic" building blocks. Now, the main questions are what do these chains interact with in the cell and how do these interactions mediate biological responses? In an attempt to answer these questions, this dissertation looks at different molecular techniques created to capture the transient interactions of monoUb and diUb probes with Ub substrates, such as, ubiquitin binding domains (UBDs) and conjugating E2 enzymes. One molecular technique focuses on the use of incorporating a genetically encoded, photo-crosslinker, p-Benzoyl-L-phenylalanine (pBpa) into diUb probes to capture their interaction with UBDs. This sets the foundation for understanding Ub’s cellular signaling recognition of UBDs. Another technique is creating diUb probes that contain lysine derivatives, Nε-L-Thiaprolyl-L-lysine (ThzK) or Nε-L-Cysteinyl-L-lysine (CysK), and can form a disulfide bonds with E2 enzymes to capture their complex, opening an opportunity to understand mechanistically the role E2 enzymes have with polyUb chain formation. Herein, these techniques are established to help unravel the complexity of Ub signaling.
APA, Harvard, Vancouver, ISO, and other styles
3

Haririnia, Aydin. "Molecular interactions of ubiquitin and polyubiquitin with ubiquitin binding domains." College Park, Md. : University of Maryland, 2007. http://hdl.handle.net/1903/7627.

Full text
Abstract:
Thesis (Ph. D.)--University of Maryland, College Park, 2007.
Thesis research directed by: Dept. of Chemistry and Biochemistry. Title from t.p. of PDF. Includes bibliographical references. Published by UMI Dissertation Services, Ann Arbor, Mich. Also available in paper.
APA, Harvard, Vancouver, ISO, and other styles
4

Lange, Anja. "Structural characterization of the interaction of the Stam2's ubiquitin binding domains with ubiquitin chains by NMR : Cooperativity or not, that is the question !" Thesis, Lyon 1, 2010. http://www.theses.fr/2010LYO10308.

Full text
Abstract:
Résumé en anglais uniquement
From the discovery of ubiquitin and its function as signal for proteasomal degradation over 20 years ago to this days, it became evident that ubiquitin is a universal signal in eukaryotic cells. Ubiquitin in its different forms is involved in many versatile cellular processes. Knowing that the ubiquitin signal is differently translated, depending on its occurrences as mono-ubiquitin or poly-ubiquitin, raises the question: how do cells distinguish between the different occurrences of ubiquitin and translate it into the proper response? Proteins interacting with ubiquitin contain so called ubiquitin binding domains (UBDs), whereas the affinities to ubiquitin vary from a few _M to mM. So far only three (K63, K48 and linear chains) out of the eight possible chain-linkages can be produced in sufficient amounts to characterize their interaction with UBDs. K48- and K63- linked ubiquitin chains regulate different cellular events and need to be recognized by different proteins. Thus, it is of prime importance to characterize the binding of different UBDs to these two kinds of ubiquitin chains, as it can give important clues related to the general mechanism of chain discrimination by ubiquitin adapter proteins. Some isolated UBDs exhibit a preference for one chain linkage type over the other, whereas others do not discriminate between mono-ubiquitin or K63- and K48-linked chains. Interestingly, many ubiquitin adapter proteins harbor more than one UBD. STAM2 is a ubiquitin adapter protein, that is involved in endosomal receptor sorting and supposed to preferentially bind mono-ubiquitin and K63- over K48-linked ubiquitin. STAM2 contains two UBDs (a VHS and UIM domain) that were shown to bind to ubiquitin . The current manuscript shows that STAM2’s SH3 domain binds ubiquitin as well. To understand the function of the sequential arrangement of three UBDs in one protein, first binding of the individual VHS and UIM domains to monoubiquitin as well as K48- and K63-linked di-ubiquitin was investigated. This work shows, that the VHS domain displays a different mode of binding for K63- and K48-linked diubiquitin. In spite of the fact, that the apparent Kd for both chains is the same, only one VHS domain can bind to K48-linked di-ubiquitin chains (with a preference for the distal domain), whereas K63-linked di-ubiquitin can accommodate two VHS domains at a time. Since no conclusion can be drawn with respect to the apparent Kds, the different binding modes might gain more impact in consideration of the ensemble of three UBDs. Results presented in this manuscript, based on a construct containing the VHS and UIM domain, show that binding to K63- but not K48-linked di-ubiquitin is cooperative
APA, Harvard, Vancouver, ISO, and other styles
5

Pirim, Ibrahim. "Ubiquitin and neurogenerative diseases." Thesis, University of Nottingham, 1993. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.335277.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

Deschutter, Julie. "Identification de la monoubiquitination de la protéine SHIP2 et caractérisation des mécanismes régulateurs associés." Doctoral thesis, Universite Libre de Bruxelles, 2009. http://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/241308.

Full text
APA, Harvard, Vancouver, ISO, and other styles
7

Depaux, Arnaud. "Régulation des complexes d'ubiquitinylation et de sumoylation par la ligase E3 hSIAH2." Paris 7, 2006. http://www.theses.fr/2006PA077094.

Full text
Abstract:
Les modifications post-traductionnelles des protéines (phosphorylation, l'acétylation ou l'ubiquitinylation) permettent de réguler leur activité, stabilité, localisation ou interactions avec d'autres facteurs. Les complexes permettant la modification par l'ubiquitine ou Sumo bien que d'organisation similaire sont composés de protéines différentes : une ligase El qui active le résidu, une ligase E2 permettant le transfert de l'ubiquitine sur le substrat et une ligase E3 qui assure la spécificité de reconnaissance du substrat. Plusieurs familles de ligases E3 ont été décrites mais seule la famille de protéines à domaine RING Finger présente des membres impliqués dans les complexes de la sumoylation et de l'ubiquitinylation. Afin de caractériser de nouveaux partenaires des ligases à domaine RING Finger hSIAHl et hSIAH2 (human Seven In Absentia homolog), nous avons développé une expérience de double-hybride chez la levure en utilisant hSIAH2 pour appât. La caractérisation des partenaires ainsi isolés a fait l'objet de mon projet de thèse. J'ai mis en évidence des protéines impliquées dans l'ubiquitinylation (Ubiquitine, Ubc5 ou hSIAH) et la sumoylation (PIAS, SUMO et Ubc9). J'ai ainsi démontré que hSIAH2 est capable de former des homodimères et des hétérodimères avec hSIAH et que cette dimérisation permet de réguler la propre stabilité des deux protéines. D'autre part, j'ai montré que hSIAH2 catalyse l'ubiquitinylation de PIAS et sa dégradation par le protéasome. L'ensemble de ce travail a mis en évidence le rôle spécifique de hSIAH2 dans la régulation de la stabilité d'intermédiaires essentiels, à la fois, aux complexes d'ubiquitinylation et de sumoylation
After synthesis, proteins are targeted to post-translational modifications such as acetylation, phosphorylation or ubiquitination. These mechanisms regulate their function, stability, localization or interaction with partners. Modification process by ubiquitin or sumo named ubiquitination or sumoylation respectively involve complexes with similar organization but compose of different enzymes. Their organization relies on Sumo or ubiquitin activating El enzyme, transferring E2-ligase and E3-ligase or sub-complex conferring the substrate specific récognition. El-ligase is unique for each complex, whereas E2 and E3-ligases are multiple. Among E3-ligase families, RING Finger protein family only has been involved in both modifications complexes. Two human homologs of Drosophila Seven In Absentia (hSIAHl et hSIAH2), belong to RING Finger E3-ligase family. In a yeast two hybrid assay, we have identified new SIAH interacting proteins. Their characterization has been the purpose of my PhD project. We have characterized partners implicated in both ubiquitination (ubiquitin, Ubc5 or hSIAH) and sumoylation (Sumo, Ubc9 and PIAS) pathways. In a first attempt, I have demonstrated that hSIAH proteins can form homo- or hetero-dimers. Dimerization régulates their stability via a proteasome dependent degradation. I have also demonstrated that hSIAH2 catalyzes the proteasome dependent degradation of PIAS1, a sumo E3-ligase. Altogether this study evidences an important rôle for hSIAH2 in the regulation of the stability of ubiquitination and sumolation complexes
APA, Harvard, Vancouver, ISO, and other styles
8

Bazirgan, Omar Al-Kasim. "Functional analysis of the ubiquitin ligase Hrd1p with the ubiquitin-conjugating enzyme Ubc7p." Diss., Connect to a 24 p. preview or request complete full text in PDF format. Access restricted to UC campuses, 2007. http://wwwlib.umi.com/cr/ucsd/fullcit?p3246079.

Full text
Abstract:
Thesis (Ph. D.)--University of California, San Diego, 2007.
Title from first page of PDF file (viewed March 9, 2007). Available via ProQuest Digital Dissertations. Vita. Includes bibliographical references.
APA, Harvard, Vancouver, ISO, and other styles
9

Rumsby, Ellen Louise. "Regulation of the cell division cycle by ubiquitin and ubiquitin-like modifications in yeast." Thesis, University of Newcastle upon Tyne, 2015. http://hdl.handle.net/10443/2938.

Full text
Abstract:
The ability of a cell to regulate its cell cycle in response to external stimuli, such as oxidative stress, is important to maintain viability by preventing damage and allowing time for repair. However, the underlying sensing and signalling mechanisms behind cell cycle regulation in response to oxidative stress remain largely unclear. Ubiquitin and ubiquitin-like (Ubl) proteins are a family of highly conserved protein modifiers with a role in many cellular processes including cell cycle regulation. The use of catalytic cysteine residues in the conjugation pathways of ubiquitin and Ubls suggest a mechanism by which these modifiers can be redox-regulated. Thus the aim of this project was to investigate the regulation of the cell division cycle by ubiquitin and Ubls in response to two conditions previously observed to lead to G1 phase cell cycle arrest in S. cerevisiae, treatment with the oxidising agent diamide and glutathione depletion. We find that in response to diamide the ubiquitin E2, Cdc34 is particularly sensitive to oxidation compared to the other E2s examined. Oxidation of Cdc34 was shown to lead to an increase in the stability of the Cdc34 substrate Sic1, coincident with G1 phase arrest. We also find that the Rub1 Ubl modifier is essential for regulation of the cell cycle in response to diamide. Interestingly, we find that Rub1 is also required to prevent budding in response to glutathione depletion. Importantly, here we reveal that SIC1 is essential to maintain viability by preventing replication-induced DNA damage following glutathione depletion. Our studies demonstrate that G1 phase cell cycle arrest in response to diamide and glutathione depletion is multifaceted, involving many of the same proteins but that these proteins are regulated differently in response to the two conditions.
APA, Harvard, Vancouver, ISO, and other styles
10

Souza, Letícia Martins Ignácio de 1987. "Sistema ubiquitina-proteassoma no hipotálamo : implicações para a gênese da obesidade." [s.n.], 2013. http://repositorio.unicamp.br/jspui/handle/REPOSIP/310374.

Full text
Abstract:
Orientadores: Lício Augusto Velloso, Marciane Milanski Ferreira
Tese (Doutorado) - Universidade Estadual de Campinas, Faculdade de Ciências Médicas
Made available in DSpace on 2018-08-22T00:15:51Z (GMT). No. of bitstreams: 1 Souza_LeticiaMartinsIgnaciode_D.pdf: 4083691 bytes, checksum: 4627dc93519577a00d2747b36d1a406f (MD5) Previous issue date: 2013
Resumo: Dentre os fatores ambientais que contribuem para o desenvolvimento de obesidade, o consumo de dietas ricas em ácidos graxos saturados desempenha o papel mais importante. Estudos recentes realizados por vários grupos, inclusive o nosso, revelam que ácidos graxos saturados presentes na dieta levam ao desenvolvimento de resistência hipotalâmica à ação dos hormônios leptina e insulina, fenômeno este fundamental para que ocorra a quebra no equilíbrio entre ingestão e gasto calórico. Até o momento caracterizaram-se dois mecanismos moleculares potencialmente envolvidos na iniciação do processo que resulta na disfunção hipotalâmica na obesidade, a ativação de TLR4 e a indução de estresse de retículo endoplasmático, ambos levando a uma resposta inflamatória local e, eventualmente, a apoptose neuronal. Estudos recentes têm revelado que frente a situações que oferecem risco de dano celular, ativa-se um mecanismo de controle de tráfico e degradação protéica chamado sistema ubiquitina-proteassoma (UPS). O acúmulo de agregados protéicos positivos para ubiquitina pode gerar toxicidade celular e regular a plasticidade neuronal. Também a modulação de componentes do UPS pode gerar neurodegeneração hipotalâmica e fenótipo obeso em animais experimentais. Neste estudo aventamos a hipótese que durante períodos prolongados de obesidade a ativação anômala do UPS contribuiria para a perpetuação do quadro de obesidade. De fato, os resultados obtidos revelam que roedores com predisposição para a obesidade induzida por dieta mantém, a princípio, a capacidade de regular adequadamente a UPS no hipotálamo. Com o passar do tempo esta capacidade é perdida resultando numa maior dificuldade para perda de peso frente à redução do aporte calórico. Roedores com mutações que os protegem da inflamação, não apresentam distúrbio funcional do UPS quando expostos a dieta rica em ácidos graxos e, são também protegidos da obesidade. Portanto, o defeito funcional do UPS no hipotálamo no curso de obesidade prolongada, constitui-se num fator importante contribuindo para a refratariedade ao tratamento e perpetuação da doença
Abstract: The consumption of high-fat diets, especially those rich in saturated fatty acids, plays the most important role in the development of obesity. Recent studies by several groups, including ours, have shown that dietary long-chain saturated fatty acids lead to the development of hypothalamic resistance to leptin and insulin, an important condition contributing for breaking of the balance between caloric intake and energy expenditure. Two molecular mechanisms are currently known to play a triggering role in this process; activation of TLR4 and endoplasmic reticulum stress, both leading to local inflammation and eventually apoptosis of neurons. The ubiquitin-proteasome system (UPS) plays an important role in the control of protein recycling in the cell. The accumulation of ubiquitin-positive protein aggregates can cause cell toxicity and regulate neuronal plasticity. Also the modulation or differential activation of UPS can produce hypothalamic neurodegeneration and obese phenotype in experimental animals. Here, we hypothesized that under prolonged diet-induced obesity, a defect in the UPS in the hypothalamus could contribute for the defective control of energy homeostasis leading to the refractoriness of obesity to caloric restriction. In fact in an obesity-prone rodent strain, prolonged, but not short-term obesity was accompanied by functional abnormality of the UPS in the hypothalamus. In mutants protected from inflammation, resistance to diet-induced obesity was accompanied by stability of the UPS in the hypothalamus. Thus, defect of the UPS in the hypothalamus, during prolonged obesity is an important factor contributing the refractoriness of obesity to caloric restriction
Doutorado
Biologia Estrutural, Celular, Molecular e do Desenvolvimento
Doutora em Fisiopatologia Médica
APA, Harvard, Vancouver, ISO, and other styles
More sources

Books on the topic "Ubiquitin"

1

Conaway, Joan, and Ray DeShaies. Abstracts of papers presented at the 2005 meeting on the ubiquitin family: April 27-May 1, 2005. Cold Spring Harbor, N.Y: Cold Spring Harbor Laboratory, 2005.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
2

Rechsteiner, Martin, ed. Ubiquitin. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4899-2049-2.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Martin, Rechsteiner, ed. Ubiquitin. New York: Plenum Press, 1988.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
4

1961-, Deshaies Raymond Joseph, ed. Ubiquitin and protein degradation. Amsterdam: Elsevier Academic Press, 2005.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
5

S, Jentsch, and Haendler B, eds. The ubiquitin system in health and disease. Berlin: Springer, 2009.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
6

Patterson, Cam, and Douglas M. Cyr. Ubiquitin-Proteasome Protocols. New Jersey: Humana Press, 2005. http://dx.doi.org/10.1385/1592598951.

Full text
APA, Harvard, Vancouver, ISO, and other styles
7

Rodriguez, Manuel S., and Rosa Barrio, eds. The Ubiquitin Code. New York, NY: Springer US, 2023. http://dx.doi.org/10.1007/978-1-0716-2859-1.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

Cam, Patterson, and Cyr Douglas M, eds. Ubiquitin-proteasome protocols. Totowa, N.J: Humana Press, 2005.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
9

Argilés, Josep M. Ubiquitin and disease. Austin, Tex., U.S.A: R.G. Landes, 1998.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
10

J, Schlesinger Milton, Hershko Avram, and Cold Spring Harbor Laboratory, eds. The Ubiquitin system. Cold Spring Harbor, N.Y: Cold Spring Harbor Laboratory, 1988.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
More sources

Book chapters on the topic "Ubiquitin"

1

Rechsteiner, Martin. "Introduction." In Ubiquitin, 1–4. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4899-2049-2_1.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Siegelman, Mark, and Irving L. Weissman. "Lymphocyte Homing Receptors, Ubiquitin, and Cell Surface Proteins." In Ubiquitin, 239–69. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4899-2049-2_10.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Ciechanover, Aaron. "Role of Transfer RNA in the Degradation of Selective Substrates of the Ubiquitin- and ATP-Dependent Proteolytic System." In Ubiquitin, 271–86. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4899-2049-2_11.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Varshavsky, Alexander, Andreas Bachmair, Daniel Finley, David Gonda, and Ingrid Wünning. "The N-End Rule of Selective Protein Turnover." In Ubiquitin, 287–324. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4899-2049-2_12.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Hershko, Avram. "Selectivity of Ubiquitin-Mediated Protein Breakdown." In Ubiquitin, 325–32. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4899-2049-2_13.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

Wilkinson, Keith D. "Purification and Structural Properties of Ubiquitin." In Ubiquitin, 5–38. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4899-2049-2_2.

Full text
APA, Harvard, Vancouver, ISO, and other styles
7

Finley, Daniel, Engin Özkaynak, Stefan Jentsch, John P. McGrath, Bonnie Bartel, Michael Pazin, Robert M. Snapka, and Alexander Varshavsky. "Molecular Genetics of the Ubiquitin System." In Ubiquitin, 39–75. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4899-2049-2_3.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

Pickart, Cecile M. "Ubiquitin Activation and Ligation." In Ubiquitin, 77–99. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4899-2049-2_4.

Full text
APA, Harvard, Vancouver, ISO, and other styles
9

Hough, Ronald F., Gregory W. Pratt, and Martin Rechsteiner. "Ubiquitin/ATP-Dependent Protease." In Ubiquitin, 101–34. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4899-2049-2_5.

Full text
APA, Harvard, Vancouver, ISO, and other styles
10

Rose, Irwin A. "Ubiquitin Carboxyl-Terminal Hydrolases." In Ubiquitin, 135–55. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4899-2049-2_6.

Full text
APA, Harvard, Vancouver, ISO, and other styles

Conference papers on the topic "Ubiquitin"

1

Zhi, Xu, Dong Zhao, Zhongmei Zhou, and Ceshi Chen. "Abstract 213: RNF126 E3 ubiquitin ligase targets p21cipfor ubiquitin-mediated degradation." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-213.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Song, Chengcheng, Vyacheslav Akimov, Peter Foote, Xiaolong Lu, Blagoy Blagoev, and Rajesh Singh. "Abstract B074: Ubiquitin proteomics: profiling the landscape of ubiquitin modification by ubisite-omics." In Abstracts: AACR-NCI-EORTC International Conference: Molecular Targets and Cancer Therapeutics; October 26-30, 2017; Philadelphia, PA. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1535-7163.targ-17-b074.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Qin, Haoran, Yilin Zhong, and Shuning Liu. "Ubiquitin-proteasome pathway in disease." In Third International Conference on Biological Engineering and Medical Science (ICBioMed2023), edited by Alan Wang. SPIE, 2024. http://dx.doi.org/10.1117/12.3021667.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Yao, Eric, Shenshen Lai, and Jun Yan. "Abstract 3862: Empowering research on ubiquitin and ubiquitin-like protein modification cascade using recombinant enzyme systems." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-3862.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Hong, Huang Chun, Hu Tian, Wu Xin Yin, Jie Ke Ming, Yan Nian long, and Ying Mu Ying. "Structure and function of ubiquitin-conjugating enzymes." In International conference on Human Health and Medical Engineering. Southampton, UK: WIT Press, 2014. http://dx.doi.org/10.2495/hhme130411.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

Wang, Zehua, Arun Seth, and Ceshi Chen. "Abstract 509: RNF115/BCA2 E3 ubiquitin ligase promotes breast cancer cell proliferation through targeting p21Waf1/Cip1for ubiquitin-mediated degradation ." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-509.

Full text
APA, Harvard, Vancouver, ISO, and other styles
7

Ruiz-Agudo, Cristina, Lutz Joachim, King Michael, Marx Andreas, and Gebauer Denis. "Designer Ubiquitin Proteins Towards Controlling Calcium Carbonate Crystallization." In Goldschmidt2020. Geochemical Society, 2020. http://dx.doi.org/10.46427/gold2020.2242.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

Yoshida, Yukiko, Koji Matsuoka, Tomoki Chiba, Toshiaki Suzuki, Keiji Tanaka, and Tadashi Tai. "N-GLYCANS ARE RECOGNIZED BY E3 UBIQUITIN-LIGASE." In XXIst International Carbohydrate Symposium 2002. TheScientificWorld Ltd, 2002. http://dx.doi.org/10.1100/tsw.2002.430.

Full text
APA, Harvard, Vancouver, ISO, and other styles
9

Ma, Ke, Philip Ryan, Rachel Klevit, and Stanley Lipkowitz. "Abstract 4965: Multiple ubiquitin-conjugating enzymes modulate the ubiquitination and downregulation of the EGFR by the Cbl RING finger ubiquitin ligase." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-4965.

Full text
APA, Harvard, Vancouver, ISO, and other styles
10

Driscoll, James J., and Sajjeev Jagannathan. "Abstract 1708: Metabolic regulation of the ubiquitin+proteasome system." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-1708.

Full text
APA, Harvard, Vancouver, ISO, and other styles

Reports on the topic "Ubiquitin"

1

Royer, Lacey. Cul3 Ubiquitin Ligase and Ctb73 Protein Interactions. Portland State University Library, January 2014. http://dx.doi.org/10.15760/honors.48.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Whitehead, Ian P. A Role for Ubiquitin Binding in Bcr-Abl Transformation. Fort Belvoir, VA: Defense Technical Information Center, June 2008. http://dx.doi.org/10.21236/ada487390.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Vierstra, R. D. Mechanism for the selective conjugation of ubiquitin to phytochrome. Office of Scientific and Technical Information (OSTI), January 1990. http://dx.doi.org/10.2172/5229610.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Whitehead, Ian P. A Role for Ubiquitin Binding in Bcr-Abl Transformation. Fort Belvoir, VA: Defense Technical Information Center, June 2009. http://dx.doi.org/10.21236/ada510762.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Zhang, Hui. The Role of Ubiquitin E3 Ligase SCFSKP2 in Prostate Cancer Development. Fort Belvoir, VA: Defense Technical Information Center, February 2005. http://dx.doi.org/10.21236/ada435854.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

Spruck, Charles H. Identification of Substances for Ubiquitin-Dependent Proteolysis During Breast Tumor Progression. Fort Belvoir, VA: Defense Technical Information Center, October 2008. http://dx.doi.org/10.21236/ada510763.

Full text
APA, Harvard, Vancouver, ISO, and other styles
7

Schultz, David C. Analysis BAP-1 as a Ubiquitin Hydrolase in the BRCA1 Pathway. Fort Belvoir, VA: Defense Technical Information Center, October 1999. http://dx.doi.org/10.21236/ada392104.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

Schultz, David C. Analysis BAP-1 as a Ubiquitin Hydrolase in the BRCA1 Pathway. Fort Belvoir, VA: Defense Technical Information Center, October 2000. http://dx.doi.org/10.21236/ada392881.

Full text
APA, Harvard, Vancouver, ISO, and other styles
9

Davidge, Brittney. The Cul3 Ubiquitin Ligase: An Essential Regulator of Diverse Cellular Processes. Portland State University Library, January 2000. http://dx.doi.org/10.15760/etd.5666.

Full text
APA, Harvard, Vancouver, ISO, and other styles
10

Srikanth, Appikonda. The Role of Ubiquitin-Mediated Proteolysis of Cyclin D in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, April 2005. http://dx.doi.org/10.21236/ada455151.

Full text
APA, Harvard, Vancouver, ISO, and other styles
You might also be interested in the extended bibliographies on the topic 'Ubiquitin' for particular source types:
Journal articles Dissertations / Theses Books
We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!

To the bibliography