Works matching DE "MOLECULAR chaperones"
Results: 5000
Effect of Propolis Applied to Goat Kids at Weaning Period on Heat Shock Protein Genes.
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- Harran University Journal of the Faculty of Veterinary Medicine / Harran Üniversitesi Veteriner Fakültesi Dergisi, 2024, v. 13, n. 2, p. 84, doi. 10.31196/huvfd.1451671
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Transcutaneous electrical acustimulation promotes wound healing in mice by modulating signaling molecules and mitochondria function.
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- Archives of Dermatological Research, 2025, v. 317, n. 1, p. 1, doi. 10.1007/s00403-024-03754-y
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Bacteriophage Φ21's receptor-binding protein evolves new functions through destabilizing mutations that generate non-genetic phenotypic heterogeneity.
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- Virus Evolution, 2024, v. 10, n. 1, p. 1, doi. 10.1093/ve/veae049
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Heat shock protein 22: A new direction for cardiovascular disease (Review).
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- Molecular Medicine Reports, 2025, v. 31, n. 3, p. N.PAG, doi. 10.3892/mmr.2025.13447
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Crosstalk between heat shock proteins and other molecular co-chaperones in oil seed mustard to combat global warming.
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- Plant Biosystems, 2025, v. 159, n. 1, p. 142, doi. 10.1080/11263504.2025.2449926
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Disorders in brassinosteroids signal transduction triggers the profound molecular alterations in the crown tissue of barley under drought.
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- PLoS ONE, 2025, v. 20, n. 1, p. 1, doi. 10.1371/journal.pone.0318281
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Assessment of Hsp90β-selective inhibitor safety and on-target effects.
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- Scientific Reports, 2025, v. 15, n. 1, p. 1, doi. 10.1038/s41598-025-86647-y
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Epigenetically induced paucity of histone H2A.Z stabilizes fission-yeast ectopic centromeres.
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- Nature Structural & Molecular Biology, 2013, v. 20, n. 12, p. 1397, doi. 10.1038/nsmb.2697
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Conformation and dynamics of the periplasmic membrane-protein-chaperone complexes OmpX-Skp and tOmpA-Skp.
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- Nature Structural & Molecular Biology, 2013, v. 20, n. 11, p. 1265, doi. 10.1038/nsmb.2677
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Structure and function of Hip, an attenuator of the Hsp70 chaperone cycle.
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- Nature Structural & Molecular Biology, 2013, v. 20, n. 8, p. 929, doi. 10.1038/nsmb.2608
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Dynamic enzyme docking to the ribosome coordinates N-terminal processing with polypeptide folding.
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- Nature Structural & Molecular Biology, 2013, v. 20, n. 7, p. 843, doi. 10.1038/nsmb.2615
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NMR disentangles a dynamic disaggregase machinery.
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- Nature Structural & Molecular Biology, 2013, v. 20, n. 4, p. 409, doi. 10.1038/nsmb.2551
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Integration of the accelerator Aha1 in the Hsp90 co-chaperone cycle.
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- Nature Structural & Molecular Biology, 2013, v. 20, n. 3, p. 326, doi. 10.1038/nsmb.2502
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Histone chaperones in nucleosome assembly and human disease.
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- Nature Structural & Molecular Biology, 2013, v. 20, n. 1, p. 14, doi. 10.1038/nsmb.2461
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Structural characterization of a eukaryotic chaperone-the ribosome-associated complex.
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- Nature Structural & Molecular Biology, 2013, v. 20, n. 1, p. 23, doi. 10.1038/nsmb.2447
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Cryo-EM structure of the mature dengue virus at 3.5-Å resolution.
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- Nature Structural & Molecular Biology, 2013, v. 20, n. 1, p. 105, doi. 10.1038/nsmb.2463
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Hsp70 proteins bind Hsp100 regulatory M domains to activate AAA+ disaggregase at aggregate surfaces.
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- Nature Structural & Molecular Biology, 2012, v. 19, n. 12, p. 1347, doi. 10.1038/nsmb.2442
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Restoring order.
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- Nature Structural & Molecular Biology, 2012, v. 19, n. 3, p. 267, doi. 10.1038/nsmb.2265
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Newly folded substrates inside the molecular cage of the HtrA chaperone DegQ.
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- Nature Structural & Molecular Biology, 2012, v. 19, n. 2, p. 152, doi. 10.1038/nsmb.2210
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The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-?<sub>1?40</sub> peptide.
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- Nature Structural & Molecular Biology, 2012, v. 19, n. 1, p. 79, doi. 10.1038/nsmb.2191
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Crystal structure of a chaperone-bound assembly intermediate of form I Rubisco.
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- Nature Structural & Molecular Biology, 2011, v. 18, n. 8, p. 875, doi. 10.1038/nsmb.2090
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A conserved 20S proteasome assembly factor requires a C-terminal HbYX motif for proteasomal precursor binding.
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- Nature Structural & Molecular Biology, 2011, v. 18, n. 5, p. 622, doi. 10.1038/nsmb.2027
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Dominant prion mutants induce curing through pathways that promote chaperone-mediated disaggregation.
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- Nature Structural & Molecular Biology, 2011, v. 18, n. 4, p. 486, doi. 10.1038/nsmb.2031
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Genetic selection designed to stabilize proteins uncovers a chaperone called Spy.
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- Nature Structural & Molecular Biology, 2011, v. 18, n. 3, p. 262, doi. 10.1038/nsmb.2016
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Mechanics of Hsp70 chaperones enables differential interaction with client proteins.
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- Nature Structural & Molecular Biology, 2011, v. 18, n. 3, p. 345, doi. 10.1038/nsmb.2006
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Substrate discrimination of the chaperone BiP by autonomous and cochaperone-regulated conformational transitions.
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- Nature Structural & Molecular Biology, 2011, v. 18, n. 2, p. 150, doi. 10.1038/nsmb.1970
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Mixed Hsp90-cochaperone complexes are important for the progression of the reaction cycle.
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- Nature Structural & Molecular Biology, 2011, v. 18, n. 1, p. 61, doi. 10.1038/nsmb.1965
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A portable RNA sequence whose recognition by a synthetic antibody facilitates structural determination.
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- Nature Structural & Molecular Biology, 2011, v. 18, n. 1, p. 100, doi. 10.1038/nsmb.1945
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Crystal structure of the open conformation of the mammalian chaperonin CCT in complex with tubulin.
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- Nature Structural & Molecular Biology, 2011, v. 18, n. 1, p. 14, doi. 10.1038/nsmb.1971
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Solid-state NMR and SAXS studies provide a structural basis for the activation of ?B-crystallin oligomers.
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- Nature Structural & Molecular Biology, 2010, v. 17, n. 9, p. 1037, doi. 10.1038/nsmb.1891
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A direct role for Hsp90 in pre-RISC formation in Drosophila.
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- Nature Structural & Molecular Biology, 2010, v. 17, n. 8, p. 1024, doi. 10.1038/nsmb.1875
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Determinants of structural and functional plasticity of a widely conserved protease chaperone complex.
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- Nature Structural & Molecular Biology, 2010, v. 17, n. 7, p. 837, doi. 10.1038/nsmb.1839
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ATP-independent reversal of a membrane protein aggregate by a chloroplast SRP subunit.
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- Nature Structural & Molecular Biology, 2010, v. 17, n. 6, p. 696, doi. 10.1038/nsmb.1836
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Alda-1 is an agonist and chemical chaperone for the common human aldehyde dehydrogenase 2 variant.
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- Nature Structural & Molecular Biology, 2010, v. 17, n. 2, p. 159, doi. 10.1038/nsmb.1737
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Crystal structure of an intramolecular chaperone mediating triple–β-helix folding.
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- Nature Structural & Molecular Biology, 2010, v. 17, n. 2, p. 210, doi. 10.1038/nsmb.1746
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Distinct passenger strand and mRNA cleavage activities of human Argonaute proteins.
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- Nature Structural & Molecular Biology, 2009, v. 16, n. 12, p. 1259, doi. 10.1038/nsmb.1712
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The chaperonin TRiC blocks a huntingtin sequence element that promotes the conformational switch to aggregation.
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- Nature Structural & Molecular Biology, 2009, v. 16, n. 12, p. 1279, doi. 10.1038/nsmb.1700
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Hsp90 charged-linker truncation reverses the functional consequences of weakened hydrophobic contacts in the N domain.
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- Nature Structural & Molecular Biology, 2009, v. 16, n. 11, p. 1141, doi. 10.1038/nsmb.1682
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Trigger factor finds new jobs and contacts.
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- Nature Structural & Molecular Biology, 2009, v. 16, n. 10, p. 1006, doi. 10.1038/nsmb1009-1006
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The Hsp82 molecular chaperone promotes a switch between unextendable and extendable telomere states.
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- Nature Structural & Molecular Biology, 2009, v. 16, n. 7, p. 711, doi. 10.1038/nsmb.1616
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Converging concepts of protein folding in vitro and in vivo.
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- Nature Structural & Molecular Biology, 2009, v. 16, n. 6, p. 574, doi. 10.1038/nsmb.1591
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The ribosome as a platform for co-translational processing, folding and targeting of newly synthesized proteins.
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- Nature Structural & Molecular Biology, 2009, v. 16, n. 6, p. 589, doi. 10.1038/nsmb.1614
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The large conformational changes of Hsp90 are only weakly coupled to ATP hydrolysis.
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- Nature Structural & Molecular Biology, 2009, v. 16, n. 3, p. 281, doi. 10.1038/nsmb.1557
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Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90.
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- Nature Structural & Molecular Biology, 2009, v. 16, n. 3, p. 287, doi. 10.1038/nsmb.1565
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Visualizing the twists and turns of a molecular chaperone.
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- Nature Structural & Molecular Biology, 2009, v. 16, n. 3, p. 235, doi. 10.1038/nsmb0309-235
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Defining the TRiC/CCT interactome links chaperonin function to stabilization of newly made proteins with complex topologies.
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- Nature Structural & Molecular Biology, 2008, v. 15, n. 12, p. 1255, doi. 10.1038/nsmb.1515
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Structural basis of nucleotide exchange and client binding by the Hsp70 cochaperone Bag2.
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- Nature Structural & Molecular Biology, 2008, v. 15, n. 12, p. 1309, doi. 10.1038/nsmb.1518
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The importance of presentation.
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- Nature Structural & Molecular Biology, 2008, v. 15, n. 12, p. 1234, doi. 10.1038/nsmb1208-1234
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Molecular functions of the histone acetyltransferase chaperone complex Rtt109–Vps75.
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- Nature Structural & Molecular Biology, 2008, v. 15, n. 9, p. 948, doi. 10.1038/nsmb.1459
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The structure of CCT–Hsc70<sub>NBD</sub> suggests a mechanism for Hsp70 delivery of substrates to the chaperonin.
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- Nature Structural & Molecular Biology, 2008, v. 15, n. 8, p. 858, doi. 10.1038/nsmb.1464
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