Bibliographies thématiques / Protein oligomer

Littérature scientifique sur le sujet « Protein oligomer »

Auteur : Grafiati
Publié le 10 mars 2023

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Articles de revues sur le sujet "Protein oligomer"

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Schmid, J. A., H. Just et H. H. Sitte. « Impact of oligomerization on the function of the human serotonin transporter ». Biochemical Society Transactions 29, no 6 (1 novembre 2001) : 732–36. http://dx.doi.org/10.1042/bst0290732.

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The formation of oligomeric structures has been proposed for a large number of membrane proteins, including G-protein-coupled receptors and ion channels. Biochemical studies employing gel filtration, cross-linking or co-immunoprecipitation techniques showed that the serotonin [5-hydroxytryptamine (5-HT)] transporter is also capable of forming oligomers. We investigated whether the human serotonin transporter (hSERT) can be visualized as an oligomer in the plasma membrane of intact cells. To test this working hypothesis, we generated fusion proteins of hSERT and spectral variants of green fluorescent protein [cyan and yellow fluorescent proteins (CFP and YFP, respectively)]. When expressed in HeLa or HEK-293 cells, the resulting fusion proteins (CFP-hSERT and YFP-hSERT) were inserted into the plasma membrane and were indistinguishable from wild-type hSERT on functional testing (5-HT uptake assays, inhibition of 5-HT uptake by blockers such as imipramine). Oligomers were visualized by fluorescence resonance energy transfer (FRET) microscopy in living cells using complementary methods. Interestingly, oligomerization was not confined to hSERT; FRET was also observed between CFP-and YFP-labelled rat γ-aminobutyric acid transporter. Gel filtration experiments showed that most of the protein was recovered as higher molecular weight complexes; almost no monomeric form was detected. This indicates that the homo-oligomeric form is the favoured state of hSERT in living cells. The formation of oligomers was not significantly affected by co-incubation with transporter substrates or blockers. Based on our observations, oligomer formation might not be essential for the physiological function of the transporter protein, the re-uptake of substrates. Furthermore, we conclude that constitutive oligomer formation might be a general property of Na+/Cl−-dependent neurotransmitter transporters.
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Kreiser, Ryan P., Aidan K. Wright, Natalie R. Block, Jared E. Hollows, Lam T. Nguyen, Kathleen LeForte, Benedetta Mannini, Michele Vendruscolo et Ryan Limbocker. « Therapeutic Strategies to Reduce the Toxicity of Misfolded Protein Oligomers ». International Journal of Molecular Sciences 21, no 22 (17 novembre 2020) : 8651. http://dx.doi.org/10.3390/ijms21228651.

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The aberrant aggregation of proteins is implicated in the onset and pathogenesis of a wide range of neurodegenerative disorders, including Alzheimer’s and Parkinson’s diseases. Mounting evidence indicates that misfolded protein oligomers produced as intermediates in the aggregation process are potent neurotoxic agents in these diseases. Because of the transient and heterogeneous nature of these elusive aggregates, however, it has proven challenging to develop therapeutics that can effectively target them. Here, we review approaches aimed at reducing oligomer toxicity, including (1) modulating the oligomer populations (e.g., by altering the kinetics of aggregation by inhibiting, enhancing, or redirecting the process), (2) modulating the oligomer properties (e.g., through the size–hydrophobicity–toxicity relationship), (3) modulating the oligomer interactions (e.g., by protecting cell membranes by displacing oligomers), and (4) reducing oligomer toxicity by potentiating the protein homeostasis system. We analyze examples of these complementary approaches, which may lead to the development of compounds capable of preventing or treating neurodegenerative disorders associated with protein aggregation.
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Wako, Hiroshi, et Shigeru Endo. « ProMode-Oligomer : Database of Normal Mode Analysis in Dihedral Angle Space for a Full-Atom System of Oligomeric Proteins ». Open Bioinformatics Journal 6, no 1 (21 février 2012) : 9–19. http://dx.doi.org/10.2174/1875036201206010009.

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The database ProMode-Oligomer (http://promode.socs.waseda.ac.jp/promode_oligomer) was constructed by collecting normal-mode-analysis (NMA) results for oligomeric proteins including protein-protein complexes. As in the ProMode database developed earlier for monomers and individual subunits of oligomers (Bioinformatics vol. 20, pp. 2035–2043, 2004), NMA was performed for a full-atom system using dihedral angles as independent variables, and we released the results (fluctuations of atoms, fluctuations of dihedral angles, correlations between atomic fluctuations, etc.). The vibrating oligomer is visualized by animation in an interactive molecular viewer for each of the 20 lowest-frequency normal modes. In addition, displacement vectors of constituent atoms for each normal mode were decomposed into two characteristic motions in individual subunits, i.e., internal and external (deformation and rigid-body movements of the individual subunits, respectively), and then the mutual movements of the subunits and the movement of atoms around the interface regions were investigated. These results released in ProMode-Oligomer are useful for characterizing oligomeric proteins from a dynamic point of view. The analyses are illustrated with immunoglobulin light- and heavy-chain variable domains bound to lysozyme and to a 12-residue peptide.
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Eisenberg, David, Arthur Laganowsky, Cong Liu, Michael Sawaya, Julian Whitelegge, Minglei Zhao, Angela Soriaga et al. « Structural Studies of the Amyloid State of Proteins ». Acta Crystallographica Section A Foundations and Advances 70, a1 (5 août 2014) : C797. http://dx.doi.org/10.1107/s205327331409202x.

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Amyloid diseases, including Alzheimer's, Parkinson's, and the prion conditions, are each associated with a particular protein in fibrillar form. At the morphological level, these fibers appear similar and are termed "amyloid." We found that the adhesive segments of amyloid fibers are short protein sequences which form pairs of interdigitated, in-register beta sheets. These amyloid fibrils were long suspected to be the disease agents, but evidence suggests that in the neurodegenerative diseases, smaller, often transient and polymorphic oligomers are the toxic entities. We have identified a segment of the amyloid-forming protein, alphaB crystallin, which forms an oligomeric complex exhibiting properties of other amyloid oligomers: beta-sheet-rich structure, cytotoxicity, and recognition by an anti-oligomer antibody. The X-ray-derived atomic structure of the oligomer reveals a cylindrical barrel, formed from six anti-parallel, out-of-register protein strands, which we term a cylindrin. The cylindrin structure is compatible with sequence segments from the Abeta protein of Alzheimer's disease and from other amyloid proteins. Cylindrins offer models for the hitherto elusive structures of amyloid oligomers, and are distinct in structure from amyloid fibrils.
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de Klerk, G. J., et D. Engelen. « Assembly of Agrostemma githago (corn-cockle) storage proteins and their precursor proteins into oligomers ». Biochemical Journal 230, no 1 (15 août 1985) : 269–72. http://dx.doi.org/10.1042/bj2300269.

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The major fraction of seed storage proteins of Agrostemma githago (corn-cockle), a non-leguminous dicot, occurs as material with S20,w values of approximately 11S and approximately 2S, and a minor fraction as oligomers with S20,w values of approximately 6.5S. The 11S proteins are of the legumin type and consist of disulphide-linked α- and β-subunits of Mr approximately 39 000 and approximately 23 000 respectively. The oligomeric assembly of the precursor polypeptides of the 11S proteins was examined. The approximately 65 000-Mr precursor polypeptides of two 11S proteins, which consist of 38 000-25 000-Mr subunits and 36 000-22 000-Mr subunits respectively, were assembled into oligomers of approximately 7S and subsequently cleaved. Thereafter the 11S oligomer was formed. The 88 000-Mr precursor of a third 11S protein, which consists of 41 000-23 000-Mr subunits, was assembled into an approximately 8S oligomer and then cleaved, yielding two disulphide-linked intermediates of Mr 59 000 and 24 000. Thereafter, the 11S oligomer was formed. Processing of the 59 000-Mr to the 41 000-Mr polypeptide occurred both in the 8S and in the 11S form.
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Burford, Neil T., Tom Wehrman, Daniel Bassoni, Jonathan O’Connell, Martyn Banks, Litao Zhang et Andrew Alt. « Identification of Selective Agonists and Positive Allosteric Modulators for µ- and δ-Opioid Receptors from a Single High-Throughput Screen ». Journal of Biomolecular Screening 19, no 9 (21 juillet 2014) : 1255–65. http://dx.doi.org/10.1177/1087057114542975.

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Hetero-oligomeric complexes of G protein–coupled receptors (GPCRs) may represent novel therapeutic targets exhibiting different pharmacology and tissue- or cell-specific site of action compared with receptor monomers or homo-oligomers. An ideal tool for validating this concept pharmacologically would be a hetero-oligomer selective ligand. We set out to develop and execute a 1536-well high-throughput screen of over 1 million compounds to detect potential hetero-oligomer selective ligands using a β-arrestin recruitment assay in U2OS cells coexpressing recombinant µ- and δ-opioid receptors. Hetero-oligomer selective ligands may bind to orthosteric or allosteric sites, and we might anticipate that the formation of hetero-oligomers may provide novel allosteric binding pockets for ligand binding. Therefore, our goal was to execute the screen in such a way as to identify positive allosteric modulators (PAMs) as well as agonists for µ, δ, and hetero-oligomeric receptors. While no hetero-oligomer selective ligands were identified (based on our selection criteria), this single screen did identify numerous µ- and δ-selective agonists and PAMs as well as nonselective agonists and PAMs. To our knowledge, these are the first µ- and δ-opioid receptor PAMs described in the literature.
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You, Young Suk, Jae-Hoon Kim, Jong-Soo Lee et Hyeseong Cho. « The mitochodnrial E3 ligase MARCH5 resolves RIG-I and MAVS aggregates in innate immunity ». Journal of Immunology 198, no 1_Supplement (1 mai 2017) : 222.13. http://dx.doi.org/10.4049/jimmunol.198.supp.222.13.

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Abstract Ubiquitin proteasome system (UPS) on the mitochondrial is one of quality control systems that works as a first line of defense barrier against aggregated or misfolded proteins. In innate immunity formation of the MAVS(Mitochondrial anti-viral signaling protein) oligomers elicits robust type-I interferon induction upon viral infection and however, persistent RIG-I and MAVS complex rather leads to host immunopathology. We recently reported that mitochondria-resident E3 ligase, MARCH5, recognizes the oligomeric form of RIG-I and MAVS complex. MARCH5+/− mice and MARCH5 deficient immune cells exhibited low viral replication and elevated type-I interferon response to viral infection. MARCH5 bound RIG-I and MAVS complex only during viral infection when MAVS forms oligomer. MARCH5 mediates Lys-48-linked poly-ubiquitination chain addition to RIG-I and MAVS oligomer and induces the RIG-I/MAVS monomer. Next, we studies have suggested that a novel function of MARCH5 in inflammation signaling. Together, these data demonstrates that MARCH5 regulates oligomeric RIG-I and MAVS complex.
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Weisz, OA, AM Swift et CE Machamer. « Oligomerization of a membrane protein correlates with its retention in the Golgi complex ». Journal of Cell Biology 122, no 6 (15 septembre 1993) : 1185–96. http://dx.doi.org/10.1083/jcb.122.6.1185.

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The first membrane-spanning domain (m1) of the M glycoprotein of avian coronavirus (formerly called E1) is sufficient to retain this protein in the cis-Golgi. When the membrane-spanning domain of a protein which is efficiently delivered to the plasma membrane (VSV G protein) is replaced with m1, the resulting chimera (Gm1) is retained in the Golgi (Swift, A. M., and C. E. Machamer. 1991. J. Cell Biol. 115:19-30). When assayed in sucrose gradients, we observed that Gm1 formed a large oligomer, and that much of this oligomer was SDS resistant and stayed near the top of the stacking gel of an SDS-polyacrylamide gel. The unusual stability of the oligomer allowed it to be detected easily. Gm1 mutants with single amino acid substitutions in the m1 domain that were retained in the Golgi complex formed SDS-resistant oligomers, whereas mutants that were rapidly released to the plasma membrane did not. Oligomerization was not detected immediately after synthesis of Gm1, but occurred gradually with a lag of approximately 10 min, suggesting that it is not merely aggregation of misfolded proteins. Furthermore, oligomerization did not occur under several conditions that block ER to Golgi transport. The lumenal domain was not required for oligomerization since another chimera (alpha m1G), where the lumenal domain of Gm1 was replaced by the alpha subunit of human chorionic gonadotropin, also formed an SDS-resistant oligomer, and was able to form hetero-oligomers with Gm1 as revealed by coprecipitation experiments. SDS resistance was conferred by the cytoplasmic tail of VSV G, because proteolytic digestion of the tail in microsomes containing Gm1 oligomers resulted in loss of SDS resistance, although the protease-treated material continued to migrate as a large oligomer on sucrose gradients. Interestingly, treatment of cells with cytochalasin D blocked formation of SDS-resistant (but not SDS-sensitive) oligomers. Our data suggest that SDS-resistant oligomers form as newly synthesized molecules of Gm1 arrive at the Golgi complex and may interact (directly or indirectly) with an actin-based cytoskeletal matrix. The oligomerization of Gm1 and other resident proteins could serve as a mechanism for their retention in the Golgi complex.
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Milošević, Jelica, Radivoje Prodanović et Natalija Polović. « On the Protein Fibrillation Pathway : Oligomer Intermediates Detection Using ATR-FTIR Spectroscopy ». Molecules 26, no 4 (12 février 2021) : 970. http://dx.doi.org/10.3390/molecules26040970.

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Oligomeric intermediates on the pathway of amyloid fibrillation are suspected as the main cytotoxins responsible for amyloid-related pathogenicity. As they appear to be a part of the lag phase of amyloid fibrillation when analyzed using standard methods such as Thioflavin T (ThT) fluorescence, a more sensitive method is needed for their detection. Here we apply Fourier transform infrared spectroscopy (FTIR) in attenuated total reflectance (ATR) mode for fast and cheap analysis of destabilized hen-egg-white lysozyme solution and detection of oligomer intermediates of amyloid fibrillation. Standard methods of protein aggregation analysis— Thioflavin T (ThT) fluorescence, atomic force microscopy (AFM), and 8-anilinonaphthalene-1-sulphonic acid (ANS) fluorescence were applied and compared to FTIR spectroscopy data. Results show the great potential of FTIR for both, qualitative and quantitative monitoring of oligomer formation based on the secondary structure changes. While oligomer intermediates do not induce significant changes in ThT fluorescence, their secondary structure changes were very prominent. Normalization of specific Amide I region peak intensities by using Amide II peak intensity as an internal standard provides an opportunity to use FTIR spectroscopy for both qualitative and quantitative analysis of biological samples and detection of potentially toxic oligomers, as well as for screening of efficiency of fibrillation procedures.
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Eghiaian, Frederic, Thorsten Daubenfeld, Yann Quenet, Marieke van Audenhaege, Anne-Pascale Bouin, Guillaume van der Rest, Jeanne Grosclaude et Human Rezaei. « Diversity in prion protein oligomerization pathways results from domain expansion as revealed by hydrogen/deuterium exchange and disulfide linkage ». Proceedings of the National Academy of Sciences 104, no 18 (18 avril 2007) : 7414–19. http://dx.doi.org/10.1073/pnas.0607745104.

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The prion protein (PrP) propensity to adopt different structures is a clue to its biological role. PrP oligomers have been previously reported to bear prion infectivity or toxicity and were also found along the pathway of in vitro amyloid formation. In the present report, kinetic and structural analysis of ovine PrP (OvPrP) oligomerization showed that three distinct oligomeric species were formed in parallel, independent kinetic pathways. Only the largest oligomer gave rise to fibrillar structures at high concentration. The refolding of OvPrP into these different oligomers was investigated by analysis of hydrogen/deuterium exchange and introduction of disulfide bonds. These experiments revealed that, before oligomerization, separation of contacts in the globular part (residues 127–234) occurred between the S1–H1–S2 domain (residues 132–167) and the H2–H3 bundle (residues 174–230), implying a conformational change of the S2–H2 loop (residues 168–173). The type of oligomer to be formed depended on the site where the expansion of the OvPrP monomer was initiated. Our data bring a detailed insight into the earlier conformational changes during PrP oligomerization and account for the diversity of oligomeric entities. The kinetic and structural mechanisms proposed here might constitute a physicochemical basis of prion strain genesis.
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Thèses sur le sujet "Protein oligomer"

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Phan, Jamie. « Investigating protein folding by the de novo design of an α-helix oligomer ». Scholarly Commons, 2013. https://scholarlycommons.pacific.edu/uop_etds/859.

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Proteins are composed of a unique sequence of amino acids, whose order guides a protein to adopt its particular fold and perform a specific function. It has been shown that a protein's 3-dimensional structure is embedded within its primary sequence. The problem that remains elusive to biochemists is how a protein's primary sequence directs the folding to adopt such a specific conformation. In an attempt to gain a better understanding of protein folding, my research tests a novel model of protein packing using protein design. The model defines the knob-socket construct as the fundamental unit of packing within protein structure. The knob-socket model characterizes packing specificity in terms of amino acid preferences for sockets in different environments: sockets filled with a knob are involved in inter-helical interactions and free sockets are involved in intra-helical interactions. Equipped with this knowledge, I sought to design a unique protein, Ksα1.1, completely de novo. The sequence was selected to induce helix formation with a predefined tertiary packing interface. Circular dichroism showed that Ksα1.1 formed α-helical secondary structure as intended. The nuclear magnetic resonance studies demonstrated formation of a high order oligomer with increased protein concentration. These results and analysis prove that the knob-socket model is a predictive model for all α-helical protein packing. More importantly, the knob-socket model introduces a new protein design method that can potentially hold a solution to the folding problem.
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Phan, Jamie. « Investigating protein folding by the de novo design of an α-helix oligomer : a thesis ». Scholarly Commons, 2001. https://scholarlycommons.pacific.edu/uop_etds/859.

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Proteins are composed of a unique sequence of amino acids, whose order guides a protein to adopt its particular fold and perform a specific function. It has been shown that a protein's 3-dimensional structure is embedded within its primary sequence. The problem that remains elusive to biochemists is how a protein's primary sequence directs the folding to adopt such a specific conformation. In an attempt to gain a better understanding of protein folding, my research tests a novel model of protein packing using protein design. The model defines the knob-socket construct as the fundamental unit of packing within protein structure. The knob-socket model characterizes packing specificity in terms of amino acid preferences for sockets in different environments: sockets filled with a knob are involved in inter-helical interactions and free sockets are involved in intra-helical interactions. Equipped with this knowledge, I sought to design a unique protein, Ksα1.1, completely de novo. The sequence was selected to induce helix formation with a predefined tertiary packing interface. Circular dichroism showed that Ksα1.1 formed α-helical secondary structure as intended. The nuclear magnetic resonance studies demonstrated formation of a high order oligomer with increased protein concentration. These results and analysis prove that the knob-socket model is a predictive model for all α-helical protein packing. More importantly, the knob-socket model introduces a new protein design method that can potentially hold a solution to the folding problem.
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Ryazanov, Sergey. « Oligomer modulator anle138b and related compounds in neurodegeneration and beyond ». Doctoral thesis, Niedersächsische Staats- und Universitätsbibliothek Göttingen, 2020. http://hdl.handle.net/21.11130/00-1735-0000-0005-1519-8.

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Halabelian, L. C. « DECIPHERING THE AGGREGATION MECHANISMS IN HUMAN B2-MICROGLOBULIN ». Doctoral thesis, Università degli Studi di Milano, 2014. http://hdl.handle.net/2434/243399.

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Beta2-microglobulin (β2m) is a 99-residue globular protein that represents the light chain of the major histocompatibility complex class I (MHCI). β2m is responsible for two types of human amyloid diseases: dialysis-related amyloidosis (DRA) caused by wt β2m, and hereditary systemic amyloidosis due to the D76N β2m mutant. Two independent projects were carried out during my PhD studies addressing both types of β2m-related amyloidosis: (i) The human cells adopt a sophisticated unfolded protein response (UPR) system for targeting misfolded/aggregated polypeptides. However, the D76N variant, which is unstable and aggregation prone, bypasses the UPR system and reaches the extracellular space forming amyloids. To understand the mechanism(s) that allow the D76N variant to escape the UPR system and to characterize its effect on MHCI, we performed a complete structural and biophysical study on a MHCI bearing the D76N variant. Our results show that MHCI acts as a chaperone that stabilize and hide the amyloidogenic variant from the UPR system, and transfers it to cell membrane, where during its normal turnover, the D76N β2m variant dissociates into blood serum and aggregates causing human pathologies. (ii) The early oligomeric species are responsible for cellular cytotoxicity in amyloidosis. Previous data showed a favourable association interface (between two facing D β-strands) that may involve in β2m oligomerization. To further elucidate its role in aggregation, we created a S-S linked dimer of β2m (DimC33) that interacts via the DD interface. Our data show that DimC33 is highly amyloidogenic compared to wt β2m, suggesting that dimerization through DD interface is instrumental for enhancing its aggregation propensity. Furthermore, DimC33 was co-crystallized in complex with Thioflavin-T (ThT), a well-known amyloid-specific dye, showing unique ThT binding site that may indicate a second key interface involved in β2m oligomerization.
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Kabulski, Jarod L. « Development of Au-immobilized P450 platform for exploring the effect of oligomer formation on P450-mediated metabolism for In vitro to In vivo drug metabolism predictions ». Morgantown, W. Va. : [West Virginia University Libraries], 2010. http://hdl.handle.net/10450/10892.

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Thesis (Ph. D.)--West Virginia University, 2010.
Title from document title page. Document formatted into pages; contains xiv, 180 p. : ill. (some col.). Includes abstract. Includes bibliographical references.
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Chandupatla, Ram Reddy [Verfasser]. « Development of oligomer-specific antibodies against tau protein and testing of therapeutic potential in a cell model of tau pathology / Ram Reddy Chandupatla ». Bonn : Universitäts- und Landesbibliothek Bonn, 2020. http://d-nb.info/1208765094/34.

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Kleckner, Ian Robert. « Thermodynamic, Kinetic, and Dynamics Studies of the Allosteric Ligand-Responsive Regulatory Protein TRAP ». The Ohio State University, 2011. http://rave.ohiolink.edu/etdc/view?acc_num=osu1313460041.

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New, Christopher Paul. « Analysis of Tha4 Function and Organization in Chloroplast Twin Arginine Transport ». Miami University / OhioLINK, 2020. http://rave.ohiolink.edu/etdc/view?acc_num=miami1586878527570538.

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Solé, i. Codina Laura. « Role of KCN E4 on the voltage gated potassium channel Kv1.3 = Paper de KCNE4 en el canal de potassi dependent de voltage Kv1.3 ». Doctoral thesis, Universitat de Barcelona, 2013. http://hdl.handle.net/10803/129685.

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Voltage gated potassium channels (Kv) play important roles in different biological process such as generation and propagation of the nerve pulse and the cardiac action potential, promotion of insulin secretion, cell volume control, induction of cell proliferation, apoptosis, migration and initiation of many signaling pathways. Kv channels can homo- or hetero- tetramerize. The composition of the channel modulates their surface expression and serves as a mechanism for regulating channel activity. Kv channel interaction with accessory subunits provides mechanisms for channels to respond to stimuli beyond changes in membrane potential. The present dissertation is focused in the analysis of the effect of one regulatory subunits family (KCNEs) on different Kv channels. The first channel analyzed is Kv7.1, which is one of the most well-known channels to interact with all the KCNE family members. In fact KCNE1-Kv7.1 complex is focus of a huge number of studies, due to its important role in heart. Most of the studies though are focused to their electrophysiological properties and molecular determinants involved in the interaction. We performed traffic analysis experiments of Kv7.1 in the present of KCNE1-5 and demonstrated that Kv7.1 membrane surface localization is modified by some of them. Next, analysis was expanded to another channel from the same family, less characterized: Kv7.5. We demonstrated that from the five KCNEs members, only KCNE1 and KCNE3 modulate Kv7.5 activity. Furthermore, we demonstrated that Kv7.5 association to KCNE3 modifies the targeting of the regulatory subunit. Next, we moved to a non-related Kv channel such as Kv1.3, which plays a crucial role in the immune system. We first focused into characterizing the modulation of Kv1.3. We demonstrated that KCNE4, but not KCNE2, functions as an inhibitory Kv1.3 partner. Kv1.3 trafficking, targeting and activity are altered by the presence of KCNE4. Furthermore, by the combination of a plethora of approaches such as electrophysiological experiments from chimeric proteins and GFP single bleaching counting steps methodology we deciphered the stoichiometry of the Kv1.3-KCNE4 complex. Next, by immunoprecipitation experiments, traffic analysis and electrophysiological experiments, we analyzed the molecular determinants involved in the association between Kv1.3 and KCNE4. We have map a domain of Kv1.3 and a specific motif of KCNE4 involved in the formation of Kv1.3-KCNE4 complex, but not in the modulation of the channel. We also proposed a 3D docking model of Kv1.3 and KCNE4. Finally, due to the importance of Kv1.3 in the immune system, the expression of all the KCNE family has been analyzed in several cell lines of leukocytes. We have demonstrated that all KCNEs suffer a differential regulation among proliferation of leukocytes. Furthermore, a different regulation can be observed, depend on the mode of leukocytes’ activation. Our results further suggest a new and yet unidentified physiological role for KCNE subunits in the immune system. Putative associations of these ancillary proteins with Kv channels would yield a wide variety of biophysically and pharmacologically distinct channels that fine-tune the immunological response.
Els canals de potassi dependents de voltatge (Kv) juguen un paper molt important tant en cèl•lules excitables com no excitables. La possibilitat de formar hetero-oligomers i la d’associació amb subunitats reguladores són uns dels mecanismes que existeixen per tal de proveir de diferents mecanismes per a respondre de manera diferent enfront a canvis en el potencial de membrana. La composició del canalosoma modula tant la seva expressió a superfície com l’activitat d’aquests. Aquesta tesi es centra en l’estudi de l’efecte del la família de les subunitats reguladores KCNE sobre diferents Kv. Primerament s’estudià l’efecte que causaven en el tràfic del canal Kv7.1 (canal model per a l’estudi dels KCNEs) i posteriorment s’amplià l’estudi a un altre membre de la mateixa família, Kv7.5. A continuació s’estudià un canal d’elevada importància per a l’activació i proliferació leucocitària: Kv1.3, centrant-nos sobretot en l’efecte causat per un dels KCNEs: KCNE4. Aquesta subunitat no només inhibeix dràsticament el corrent del canal Kv1.3, sinó que a més a més, modifica el seu tràfic i localització. Aquests canvis són deguts a una interacció directa entre ambdues proteïnes. A continuació s’estudià en detall el complex Kv1.3-KCNE4. Mitjançant la combinació d’experiments d’electrofisiologia i monitorització de fluorescència de molècules individuals en la membrana, es va poder establir l’estequiometria d’aquest complex. Posteriorment, mitjançant l’anàlisi de diverses proteïnes quimèriques i mutants, tant del canal com de la subunitat reguladora, es van cercar els determinants moleculars implicats en l’associació entre ambdues proteïnes. S’han pogut determinar els motius claus en KCNE4 i Kv1.3 implicats en la formació del complex, però no en la modulació del canal. Finalment, degut a la importància de Kv1.3 en el sistema immunitari, s’han analitzat els nivells d’expressió dels KCNEs en diferents línies leucocitàries. S’ha observat que aquestes subunitats pateixen una regulació diferencial en funció de la manera d’activació i al llarg de la proliferació del leucòcits, suggerint un possible paper en la regulació precisa de la resposta immunològica.
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Jimenez, Jeffy Pilar. « Effects of Monoclonal Anti-Abeta Antibodies on the Amyloid Beta Peptide Fibrillogenesis and their Involvement in the Clearance of Alzheimer's Disease Plaques ». Scholar Commons, 2010. http://scholarcommons.usf.edu/etd/3445.

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Alzheimer’s disease (AD) is the most common cause of senile dementia worldwide. AD is a neurodegenerative disorder characterized by the loss of memory and language skill, collapse of the cognitive function, and distortion of social behavior. As of today, the onset mechanisms of AD and cure are unknown; however, three hallmarks are commonly encountered: extra and intracellular accumulation of amyloid beta (A!) peptide plaques, formation of intracellular neurofibrillary tangles, and inevitable neuronal death. Hypothetically, a possible scenario provoking or involved in the onset of AD is a cascade effect that starts with an imbalance in the production and clearance of Aß peptide that consequently leads to its accumulation, formation of tau protein tangles and neuronal death. This work studied and characterized the mechanisms governing A! peptide aggregation and the effects of using anti-Aß monoclonal antibodies to modify this process. These mechanisms play an important role in the formation of AD plaques and are critical in the search for therapies involving Aß peptide plaque clearance. Yet, antibody-based therapies for plaque clearance are not well understood, adding to the existing concerns about side effects in humans, hence there is a necessity of knowledge in this matter. In this work different Nterminus, C-terminus, and Mid-domain antibodies were used against Aß peptide species (monomers, oligomers, and fibrils) to probe peptide aggregates modification and disruption. Additionally, construction of a soft supported lipid bilayer membrane was proposed to study the adhesion mechanisms of Aß peptide and interactions with antibodies, mimicking the neuronal cell surface. The main characterization techniques used in this work were: atomic force microscopy (AFM) and transmission electron microscopy that allowed the physical exploration and visualization of the different processes of aggregation in terms of adhesion, size evolution, and distribution of the peptide; and attenuated total reflectance Fourier spectroscopy (ATR/FTIR) which allowed monitoring the change of secondary structures for the peptide during the processes studied. It is endeavored that this work will help to elucidate the effects attributed to the molecular interactions between A! peptide species and antibodies to target Aß plaque’s clearance in the brain of AD patients. Ultimately, this study provides novel information critical for the formulation of effective therapies to prevent and treat AD with less collateral effects. It also represents a contribution to the basic scientific knowledge regarding peptide-antibody interactions with application to other diseases related to protein misfolding.
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Livres sur le sujet "Protein oligomer"

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Nakamura, Tomohiro, et Stuart A. Lipton. Neurodegenerative Diseases as Protein Misfolding Disorders. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780190233563.003.0002.

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Neurodegenerative diseases (NDDs) often represent disorders of protein folding. Rather than large aggregates, recent evidence suggests that soluble oligomers of misfolded proteins are the most neurotoxic species. Emerging evidence points to small, soluble oligomers of misfolded proteins as the cause of synaptic dysfunction and loss, the major pathological correlate to disease progression in many NDDs including Alzheimer’s disease. The protein quality control machinery of the cell, which includes molecular chaperones as found in the endoplasmic reticulum (ER), the ubiquitin-proteasome system (UPS), and various forms of autophagy, can counterbalance the accumulation of misfolded proteins to some extent. Their ability to eliminate the neurotoxic effects of misfolded proteins, however, declines with age. A plausible explanation for the age-dependent deterioration of the quality control machinery involves compromise of these systems by excessive generation of reactive oxygen species (ROS), such as superoxide anion (O2-), and reactive nitrogen species (RNS), such as nitric oxide (NO). The resulting redox stress contributes to the accumulation of misfolded proteins. Here, we focus on aberrantly increased generation of NO-related species since this process appears to accelerate the manifestation of key neuropathological features, including protein misfolding. We review the chemical mechanisms of posttranslational modification by RNS such as protein S-nitrosylation of critical cysteine thiol groups and nitration of tyrosine residues, showing how they contribute to the pathogenesis of NDDs.
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Moloshok, Thomas David. Oligogalacturonides as signals for plant defensive genes : Structure-activity relationships of oligomers for induction of proteinase inhibitors and for enhancement of plasma membrane protein phosphorylation. 1989.

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Wetzel, Ronald, et Rakesh Mishra. Structural Biology. Oxford University Press, 2014. http://dx.doi.org/10.1093/med/9780199929146.003.0012.

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The 3,144–amino acid huntingtin protein (HTT) folds in water into a structure consisting of compact, organized domains interspersed with intrinsically disordered protein (IDP) elements. The IDPs function as sites of post-translational modifications and proteolysis as well as in targeting, binding, and aggregation. Although the dominant structural motif of HTT is the α‎-helix–rich HEAT repeat, the expanded polyglutamine (polyQ) toxicity responsible for Huntington’s disease is most likely played out within intrinsically disordered HTT exon 1–like fragments consisting of the 16– to 17–amino acid N-terminal HTTNT segment, the polyQ segment, and a proline-rich segment. The physical behavior of HTT exon 1 fragments is dominated by interactive, polyQ repeat length–dependent structural transitions responsible for membrane and protein–protein interactions and the formation of tetramers, higher oligomers, amyloid fibrils, and inclusions. Understanding the basis of this solution behavior may be the key to disease mechanisms and molecular therapeutic strategies.
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Safar, Jiri G. Prion Paradigm of Human Neurodegenerative Diseases Caused by Protein Misfolding. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780190233563.003.0005.

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Data accumulated from different laboratories argue that a growing number of proteins causing neurodegeneration share certain characteristics with prions. Prion-like particles were produced from synthetic amyloid beta (Aβ‎) peptides of Alzheimer’s disease (AD), from recombinant α‎-synuclein linked to Parkinson’s disease (PD), and from recombinant tau associated with frontotemporal dementias (FTD). Evidence from human prions reveals that variable disease phenotypes, rates of propagation, and targeting of different brain structures are determined by distinct conformers (strains) of pathogenic prion protein. Recent progress in the development of advanced biophysical tools identified the structural characteristics of Aβ‎ in the brain cortex of phenotypically diverse AD patients and thus allowed an investigation of the prion paradigm of AD. The findings of distinctly structured strains of human brain Aβ‎, forming a unique spectrum of oligomeric particles in the cortex of rapidly progressive cases, implicates these structures in variable rates of propagation in the brain.
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Lattman, Eaton E., Thomas D. Grant et Edward H. Snell. Shape Reconstructions from Small Angle Scattering Data. Oxford University Press, 2018. http://dx.doi.org/10.1093/oso/9780199670871.003.0004.

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This chapter discusses recovering shape or structural information from SAXS data. Key to any such process is the ability to generate a calculated intensity from a model, and to compare this curve with the experimental one. Models for the particle scattering density can be approximated as pure homogenenous geometric shapes. More complex particle surfaces can be represented by spherical harmonics or by a set of close-packed beads. Sometimes structural information is known for components of a particle. Rigid body modeling attempts to rotate and translate structures relative to one another, such that the resulting scattering profile calculated from the model agrees with the experimental SAXS data. More advanced hybrid modelling procedures aim to incorporate as much structural information as is available, including modelling protein dynamics. Solutions may not always contain a homogeneous set of particles. A common case is the presence of two or more conformations of a single particle or a mixture of oligomeric species. The method of singular value decomposition can extract scattering for conformationally distinct species.
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Chapitres de livres sur le sujet "Protein oligomer"

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Baek, Minkyung, Taeyong Park, Lim Heo et Chaok Seok. « Modeling Protein Homo-Oligomer Structures with GalaxyHomomer Web Server ». Dans Methods in Molecular Biology, 127–37. New York, NY : Springer US, 2020. http://dx.doi.org/10.1007/978-1-0716-0708-4_7.

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Palacio-Castañeda, Valentina, Roland Brock et Wouter P. R. Verdurmen. « Generation of Protein-Phosphorodiamidate Morpholino Oligomer Conjugates for Efficient Cellular Delivery via Anthrax Protective Antigen ». Dans Methods in Molecular Biology, 129–41. New York, NY : Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2010-6_8.

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AbstractPhosphorodiamidate morpholino oligomers (PMOs) offer great promise as therapeutic agents for translation blocking or splice modulation due to their high stability and affinity for target sequences. However, in spite of their neutral charge as compared to natural oligonucleotides or phosphorothioate analogs, they still show little permeability for cellular membranes, highlighting the need for effective cytosolic delivery strategies. In addition, the implementation of strategies for efficient cellular targeting is highly desirable to minimize side effects and maximize the drug dose at its site of action. Anthrax toxin is a three-protein toxin of which the pore-forming protein anthrax protective antigen (PA) can be redirected to a receptor of choice and lethal factor (LF), one of the two substrate proteins, can be coupled to various cargoes for efficient cytosolic cargo delivery. In this protocol, we describe the steps to produce the proteins and protein conjugates required for cytosolic delivery of PMOs through the cation-selective pore generated by anthrax protective antigen. The method relies on the introduction of a unique cysteine at the C-terminal end of a truncated LF (aa 1–254), high-yield expression of the (truncated) toxin proteins in E. coli, functionalization of a PMO with a maleimide group and coupling of the maleimide-functionalized PMO to the unique cysteine on LF by maleimide-thiol conjugation chemistry. Through co-administration of PA with LF-PMO conjugates, an efficient cytosolic delivery of PMOs can be obtained.
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Heuninck, Joyce, Candide Hounsou, Elodie Dupuis, Eric Trinquet, Bernard Mouillac, Jean-Philippe Pin, Dominique Bonnet et Thierry Durroux. « Time-Resolved FRET-Based Assays to Characterize G Protein-Coupled Receptor Hetero-oligomer Pharmacology ». Dans Methods in Molecular Biology, 151–68. New York, NY : Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9121-1_8.

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Yekkirala, Ajay S. « Novel Mechanisms of G Protein-Coupled Receptor Oligomer and Ion Channel Interactions in Nociception ». Dans Methods in Pharmacology and Toxicology, 347–64. Totowa, NJ : Humana Press, 2013. http://dx.doi.org/10.1007/978-1-62703-779-2_19.

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Kaufman, Adam C., et Stephen M. Strittmatter. « Role of Cellular Prion Protein in the Amyloid-β Oligomer Pathophysiology of Alzheimer’s Disease ». Dans Prions and Diseases, 35–48. New York, NY : Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4614-5305-5_3.

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Li, QiPeng, Shao Wu Zhang et Quan Pan. « Using Multi-scale Glide Zoom Window Feature Extraction Approach to Predict Protein Homo-oligomer Types ». Dans Pattern Recognition in Bioinformatics, 78–86. Berlin, Heidelberg : Springer Berlin Heidelberg, 2008. http://dx.doi.org/10.1007/978-3-540-88436-1_7.

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Li, Qi-Peng, Shao-Wu Zhang et Quan Pan. « Prediction of Protein Homo-oligomer Types with a Novel Approach of Glide Zoom Window Feature Extraction ». Dans Lecture Notes in Computer Science, 71–78. Berlin, Heidelberg : Springer Berlin Heidelberg, 2008. http://dx.doi.org/10.1007/978-3-540-87442-3_10.

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Garratt, Richard C., Napoleão Fonseca Valadares et José Fernando Ruggiero Bachega. « Oligomeric Proteins ». Dans Encyclopedia of Biophysics, 1781–89. Berlin, Heidelberg : Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-16712-6_416.

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Petty, Howard R. « Lipids, Oligomers, and Proteins ». Dans Molecular Biology of Membranes, 7–49. Boston, MA : Springer US, 1993. http://dx.doi.org/10.1007/978-1-4899-1146-9_2.

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Ferré, Sergi. « Allosterism Within GPCR Oligomers : Back to Symmetry ». Dans G-Protein-Coupled Receptor Dimers, 433–50. Cham : Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-60174-8_17.

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Actes de conférences sur le sujet "Protein oligomer"

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Su, Tianxiang, et Prashant K. Purohit. « Mechanics of Heterogeneous Fluctuating Elastic Rods ». Dans ASME 2009 International Design Engineering Technical Conferences and Computers and Information in Engineering Conference. ASMEDC, 2009. http://dx.doi.org/10.1115/detc2009-86364.

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Biofilaments, such as actin and DNA, have for long been modeled as thermally fluctuating elastic rods with homogeneous material properties. Such models are adequate if the length scale of the filaments being studied is much larger than the scale of the heterogeneity. However, advanced single molecule experimental techniques have now made it possible to probe the properties of biomolecules at the scale of a few nanometers. The data emerging from these experiments ought to be greeted with appropriately detailed models. In this paper we study the mechanics of a thermally fluctuating elastic rod whose moduli are a function of position. Such a rod can be used as a model for DNA whose sequence specific properties are known or for a protein oligomer in an AFM where some of the monomers might be unfolded. The mechanics of these rods is understood by first evaluating a partition function through path integral techniques. We develop a computational technique to efficiently evaluate the partition function and use it to obtain the force-extension relation of a fluctuating rod with two different bending moduli as would be the case for a partially unfolded protein oligomer stretched in an AFM. The variance of the transverse fluctuations of the protein oligomer is also evaluated and are found to agree with the results of a Monte Carlo simulation.
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Xiao, Xuan, et Pu Wang. « Application of Function Domain and Pseudo Amino Acid Composition to Predict Hetero-Oligomer Protein Structural Types ». Dans 2010 4th International Conference on Bioinformatics and Biomedical Engineering (iCBBE). IEEE, 2010. http://dx.doi.org/10.1109/icbbe.2010.5515624.

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Abakumets, V. Y., et K. Ya Bulanava. « THE INFLUENCE OF INSULIN FIBRILLATION ». Dans SAKHAROV READINGS 2021 : ENVIRONMENTAL PROBLEMS OF THE XXI CENTURY. International Sakharov Environmental Institute of Belarusian State University, 2021. http://dx.doi.org/10.46646/sakh-2021-2-7-10.

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Violation of protein folding leads to the development of a number of systemic and neurodegenerative diseases-proteinopathy. In these pathologies, proteins acquire an incorrect conformation that differs from the native one, become functionally inactive, toxic, and prone to aggregation and deposition in various organs and tissues. There is a widespread hypothesis that the primary cytotoxic agents in the development of proteinopathies are protein oligomers that are prone to aggregation. These diseases include Parkinson’s disease, Creutzfeldt-Jakob disease, type 2 diabetes, and many others.
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Shibatay, N., K. Tanaka, K. Okamoto et T. Onji. « REORGANIZATION OF ACTIN AND MYOSIN IN THE ACTIVATED PLATELETS ». Dans XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643539.

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This study was done to clarify the intracellular dynamic arrangements of myosin(My) and actin(Ac) in activation process of human platelets (PLs) from unactivated to activated stage (clot retraction) in electron microscopy. The observation of unactivated PLs was done either in the fresh whole blood fixed directly with 0.1 % glutaraldehyde or in PLs isolated by gel filtration of platelet rich plasma(PRP) containing prostaglandin I2 (10 ng/ml). The isolated PLs mounted on a glass cover slip were used as activated PLs (adrerent ones). The contracted PLs were prepared in PRP incubated with thrombin (0.5 u/ml) and 20 mM CaCl- for 10-60 min. Treating PLs with 0.15 % Triton X-100 containing 0.05 % glutaraldehyde produced cytoskeleton. My and F-Ac were identified by an indirect immuno-cytochemical method using the specific antibody (rabbit IgG) against PL-My and protein A-gold and by demonstration of in “arrow-head” decoration by Ishikawa's method using skeletal meromyosin (HMM), respectively. [Results] (1) Unactivated PLs. Mys in monomer or oligomer distributed homogenously in scare association with cytoskeleton. Cytoskeletons were exclusively composed of F-Ac networks of crossolinked short filaments which were thinly distributed in the cytoplasm with partial connection to the cell membrance. (2) Surface activated spreading PLs. PLs adhered to the glass cover slip in dendritic forms. Mys were densely located around granulomere and formed linear arrays associated with F-Ac filaments of the cytoskeleton surrounding the granulomere and running straightly in cytoplasm. (3) Contracted PLs. Activated PLs protruded several filopodia in which networks or bundles of F-Ac filaments were found connecting to extracellular fibrin strand through cell membrene. Microfilaments formed arrow-head decoration with HMM pointing toward the cell body. The cytoskeleton in contracted PLs contained thick filaments of My-polymers attaching to F-Ac filaments end by end. It is concluded that the reorganization of Ac-My is the basis for the shape change, secretion and clot retraction of activated PLs.
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Ide, J. P., D. R. Klug, W. Kuhlbrandt et G. Porter. « Detergent effects upon the picosecond dynamics of higher plant light harvesting chlorophyll complex (LHC). » Dans International Conference on Ultrafast Phenomena. Washington, D.C. : Optica Publishing Group, 1986. http://dx.doi.org/10.1364/up.1986.mf1.

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The light-harvesting chlorophyll a/b protein complex (LHC) has been shown to form crystalline arrays in vitro. These arrays have P321 symmetry. The unit cell is composed of trimeric protein oligomers arranged with a 3-fold symmetry axis running centrally through each complex[1]. Each polypeptide has an apparent molecular weight of 25–27kd within which are bound 6-11 chlorophyll molecules.
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Intze, A., M. E. Temperini, R. Polito, E. Zacco, G. G. Tartaglia, A. Pastore, M. Ortolani et V. Giliberti. « Mid-infrared nanospectroscopy of individual DNA-binding protein oligomers ». Dans 2022 47th International Conference on Infrared, Millimeter and Terahertz Waves (IRMMW-THz). IEEE, 2022. http://dx.doi.org/10.1109/irmmw-thz50927.2022.9895918.

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Temirov, Jamshid, James H. Werner, Peter M. Goodwin et Andrew R. M. Bradbury. « "Sizing" the oligomers of Azami Green fluorescent protein with FCS and antibunching ». Dans SPIE BiOS, sous la direction de Jörg Enderlein, Zygmunt K. Gryczynski, Rainer Erdmann, Felix Koberling et Ingo Gregor. SPIE, 2012. http://dx.doi.org/10.1117/12.906843.

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Nikulina, N., et Sergey Nikulin. « PROTECTIVE WOOD TREATMENT WITH AN OLIGOMER CONTAINING STYRENE UNITS ». Dans Modern machines, equipment and IT solutions for industrial complex : theory and practice. FSBE Institution of Higher Education Voronezh State University of Forestry and Technologies named after G.F. Morozov, 2021. http://dx.doi.org/10.34220/mmeitsic2021_261-265.

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Currently, much attention is paid to the protective treatment of wood materials. This allows you to protect wood from adverse factors and extend the service life of products based on it. At the same time, not a little, an important criterion is the ratio of the price of the protective composition and its quality. The article discusses the possibility of using an oligomer for the protective treatment of natural wood, obtained on the basis of by-products of the production of polybutadiene and modified with secondary polystyrene. Considering the fact that this waste has not found its application, its use makes it possible to obtain not only valuable and affordable compositions based on it, but also to solve a number of environmental problems. For the modification, an oligomer with a bound styrene content of about 50% was used. The process was carried out at 200°C in the presence of a desiccant. At high temperatures and in the presence of atmospheric oxygen, destruction of both oligomer and secondary polystyrene occurs. The resulting destruction products interact with each other with the formation of new macromolecules containing an increased amount of styrene groups and the appearance of functional groups containing oxygen in the polymer chains. Protective treatment of natural wood with the obtained impregnating compounds allows to reduce water absorption and swelling of birch samples. This treatment allows you to extend the life of wood products.
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Strandberg, L., D. Lawrence et T. Ny. « ISOLATION OF THE GENOMIC REGION CODING FOR TYPE-1 PLASMINOGEN ACTIVATOR INHIBITOR ». Dans XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644439.

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The type-1 Plasminogen Activator Inhibitor (PAI-1) has recently been identified as a member of the Serine Protease Inhibitor family (SERPINS). This family of proteins contain many serine protease inhibitors but also functionally unrelated proteins like ovalbumin and anginotensinogen. PAI-1 inhibits both u-PA and t-PA and might therefore be an important regulator of the fibrinolytic system.In order to study the evolution of the Serpin family as well as PAI-1 gene expression we have isolated the genomic region carrying the PAI-1 gene. A cDNA sequence for PAI-1 was used as probe to screen a human genomic library. When 2 million independent phages were screened, 13 positive clones were isolated. Characterisation of these clones showed that they could be divided into 3 overlapping groups covering a genomic region of approximately 30 kb. The gene was localized and characterized by restriction enzyme analysis, southern blotting using cDNA and oligomer probes, and DNA sequencing.
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Vuga, LJ, A. Ben-Yehudah, K. Pandit, Y. Zheng, J. Sciurba, J. Milosevic, LJ Chensny, K. Konishi, KF Gibson et N. Kaminski. « Cartilage Oligomeric Matrix Protein Is a Potential Biomarker for Idiopathic Pulmonary Fibrosis. » Dans American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a3487.

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Rapports d'organisations sur le sujet "Protein oligomer"

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Garcia, A. E., et G. Hummer. Theoretical studies of the interaction of water with DNA oligomers and proteins. Office of Scientific and Technical Information (OSTI), avril 1996. http://dx.doi.org/10.2172/212500.

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Sierks, Michael. Oligomeric Neuronal Protein Aggregates as Biomarkers for Traumatic Brain Injury (TBI) and Alzheimer Disease (AD). Fort Belvoir, VA : Defense Technical Information Center, octobre 2013. http://dx.doi.org/10.21236/ada591179.

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Azem, Abdussalam, George Lorimer et Adina Breiman. Molecular and in vivo Functions of the Chloroplast Chaperonins. United States Department of Agriculture, juin 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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Fleming, Karen G. Energetics and Structure Prediction of the Network of Homo- and Hetero-Oligomers Formed by the Transmembrane Domains of the ErbReceptor Family of Proteins. Fort Belvoir, VA : Defense Technical Information Center, juin 2006. http://dx.doi.org/10.21236/ada456142.

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Valente, Pedro, Luis Rama, Hugo Sarmento et Ana Teixeira. Cartilage Oligomeric Matrix Protein (COMP), a potential cartilage destruction biomarker in active and healthy individuals or athletes from different sports. A systematic review. INPLASY - International Platform of Registered Systematic Review and Meta-analysis Protocols, février 2021. http://dx.doi.org/10.37766/inplasy2021.2.0032.

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