Substrate protein folds while it is bound to the ATP-independent chaperone Spy
about
Engineering and Evolution of Molecular Chaperones and Protein Disaggregases with Enhanced ActivityCapturing a Dynamic Chaperone-Substrate Interaction Using NMR-Informed Molecular ModelingStructural model of dodecameric heat-shock protein Hsp21: Flexible N-terminal arms interact with client proteins while C-terminal tails maintain the dodecamer and chaperone activity.Biochemical characterization of functional domains of the chaperone CosmcMultifaceted anti-amyloidogenic and pro-amyloidogenic effects of C-reactive protein and serum amyloid P component in vitro.Visualizing chaperone-assisted protein folding.A molecular mechanism of chaperone-client recognition.A new general method for simultaneous fitting of temperature and concentration dependence of reaction rates yields kinetic and thermodynamic parameters for HIV reverse transcriptase specificity.Protein folding in the cell envelope of Escherichia coli.Chaperone-client interactions: Non-specificity engenders multifunctionality.Folding while bound to chaperones.The chloroplast-localized small heat shock protein Hsp21 associates with the thylakoid membranes in heat-stressed plants.Forces Driving Chaperone ActionHarnessing an RNA-mediated chaperone for the assembly of influenza hemagglutinin in an immunologically relevant conformation.Directed evolution to improve protein folding in vivo.Chaperone-client interactions between Hsp21 and client proteins monitored in solution by small angle X-ray scattering and captured by crosslinking mass spectrometry.Chaperone-substrate interactions monitored via a robust TEM-1 β-lactamase fragment complementation assay.Application of n-dodecane as an oxygen vector to enhance the activity of fumarase in recombinant Escherichia coli: role of intracellular microenvironment.Molecular chaperones: providing a safe place to weather a midlife protein-folding crisis.Conformational flexibility within the nascent polypeptide-associated complex enables its interactions with structurally diverse client proteins.Oligomerization of a molecular chaperone modulates its activity.
P2860
Q26750800-956A68B6-753E-4B1D-92DF-3031AB64459AQ28818853-404843F5-A443-46C5-853C-41EFE0CE5220Q30849020-C60A21B0-96E1-4073-96BC-FED98230DA6DQ33860182-74CFF78C-C2EB-449C-8D49-95108C1B8F71Q37067700-7DECCE1A-DF60-4178-87E3-C5A817BFE514Q37077645-72A2DAD8-6194-41BD-A53B-74D4B83BAD1DQ37603844-72B8619C-8FDA-4243-8597-EECC2E691B9AQ38932237-4D2A79AF-FD4E-42A5-A911-ADEF7CF9C3A2Q38940176-948D847E-4767-4221-BD13-B6B4FBCA2145Q39376939-5E99B5E0-E2B4-4FEC-8BCA-B324C9545067Q39451710-1F2C3572-2D6A-4113-9979-7CD1F206B666Q41461632-57C561F3-B27C-4BD9-B3FA-D847D88F69E5Q41832929-9C25DC4B-287E-4C03-B843-926D5F499D3BQ47236983-09E9668F-38AB-47EB-AAF5-7F59E9EC4951Q47253797-CD71572B-3270-449D-A262-62BA589CD630Q47589403-90947343-4C29-4F54-884C-E680A991C9FBQ48160549-0410F4C9-8D21-4DD3-A2EC-06956940D260Q50154659-420724DB-DBC0-4883-A8DF-36A2FF3FB266Q51263802-49EC174A-F5B4-42AA-8683-E1C433B1E929Q52323065-FBAC4D2D-5A22-4821-9472-DE002298BD24Q54203917-DB6C9196-EEED-4B4F-90A6-EA0E27244BED
P2860
Substrate protein folds while it is bound to the ATP-independent chaperone Spy
description
2015 nî lūn-bûn
@nan
2015年の論文
@ja
2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
@zh-tw
2015年论文
@wuu
2015年论文
@zh
2015年论文
@zh-cn
name
Substrate protein folds while it is bound to the ATP-independent chaperone Spy
@en
Substrate protein folds while it is bound to the ATP-independent chaperone Spy
@en-gb
type
label
Substrate protein folds while it is bound to the ATP-independent chaperone Spy
@en
Substrate protein folds while it is bound to the ATP-independent chaperone Spy
@en-gb
prefLabel
Substrate protein folds while it is bound to the ATP-independent chaperone Spy
@en
Substrate protein folds while it is bound to the ATP-independent chaperone Spy
@en-gb
P2860
P50
P356
P6366
P1154
2-s2.0-84954405061
P1476
Substrate protein folds while it is bound to the ATP-independent chaperone Spy
@en
P2093
James C A Bardwell
Philipp Koldewey
P2860
P2888
P356
10.1038/NSMB.3133
P5530
P577
2015-11-30T00:00:00Z
P6179
1012647701
P6366
2239241187