Contribution of cotranslational folding to the rate of formation of native protein structure.
about
The refolding activity of the yeast heat shock proteins Ssa1 and Ssa2 defines their role in protein translocationStructural features of the precursor to mitochondrial aspartate aminotransferase responsible for binding to hsp70Kinetic analysis of ribosome-bound fluorescent proteins reveals an early, stable, cotranslational folding intermediate.Directionality in protein fold prediction.Competition between folding and glycosylation in the endoplasmic reticulum.Characterization of GE82832, a peptide inhibitor of translocation interacting with bacterial 30S ribosomal subunitsAntibody-ribosome-mRNA (ARM) complexes as efficient selection particles for in vitro display and evolution of antibody combining sites.Probing ribosome-nascent chain complexes produced in vivo by NMR spectroscopy.Specific, efficient, and selective inhibition of prokaryotic translation initiation by a novel peptide antibiotic.Characterization of membrane protein non-native states. 1. Extent of unfolding and aggregation of rhodopsin in the presence of chemical denaturantsDiversity and selectivity in mRNA translation on the endoplasmic reticulumTritium planigraphy: from the accessible surface to the spatial structure of a protein.Selection of Recombinant Human Antibodies.Protein folding on the ribosome studied using NMR spectroscopy.Free luciferase may acquire a more favorable conformation than ribosome-associated luciferase for its activity expression.Reactivation of denatured proteins by domain V of bacterial 23S rRNA.The path of the growing peptide chain through the 23S rRNA in the 50S ribosomal subunit; a comparative cross-linking study with three different peptide families.A ribosome-associated peptidyl-prolyl cis/trans isomerase identified as the trigger factor.Cotranslational folding of nascent proteins on Escherichia coli ribosomes.Co-translational trimerization of the reovirus cell attachment protein.Genetic Code Optimization for Cotranslational Protein Folding: Codon Directional Asymmetry Correlates with Antiparallel Betasheets, tRNA Synthetase ClassesCotranslational protein folding.Structure of the beta 2 homodimer of bacterial luciferase from Vibrio harveyi: X-ray analysis of a kinetic protein folding trap.Unraveling co-translational protein folding: Concepts and methods.The ribosome destabilizes native and non-native structures in a nascent multidomain protein.Binding of an N-terminal rhodanese peptide to DnaJ and to ribosomes.Dihydrofolate reductase synthesis in the presence of immobilized methotrexate. An approach to a continuous cell-free protein synthesis system.Co-translational Folding of an Eukaryotic Multidomain Protein in a Prokaryotic Translation System
P2860
Q27933070-35BA2894-EA3A-467D-9B2D-8C75D9B2577EQ28289511-FB38C820-ED31-449F-AD86-7B7F35D0CC1FQ30155421-9E72AF36-767D-4FEC-A0AC-6544DD346159Q30387760-C95E87C9-6FFE-4187-8FFE-BB996CE8AE21Q30424056-1AF9A30D-485C-4E9E-AB24-7D59EF310F18Q30815114-0450BFC6-F16E-4C7B-947E-19CB7E1BE68EQ32182653-CFCCE05B-8EDA-4F45-9654-A9892A04F377Q33564161-7652AB09-70A8-4C13-A44E-2DFE11CFCE5EQ34248263-69E4E864-F8AF-4748-B95D-0CEF61BD5A19Q35626549-218B7EE6-D847-4CBB-8C73-F7FAFA27E246Q35827837-5EE1B7D7-92FD-4160-8568-54988C3F2356Q35971283-11DE2DE9-44BC-46D6-ACC5-474252A71584Q36033281-8E212406-AD2B-43B0-9757-CBD2AB5A7E9DQ37710489-69BF3F6E-7E1A-4146-9548-37F7B67626BEQ38554352-EC826B56-EE69-433B-850C-1B095E627B67Q39721940-C7A95207-AB26-4368-A522-8B9B3A501B43Q39722844-0DAEF5AF-4A21-48DA-83F2-F953CB01D164Q40789637-697144AC-9FCE-49F6-AE8B-C009D0A412D1Q41043864-FAE47B4F-2D29-4B81-93CD-94C9201DF87CQ41065185-7BB89ADF-3233-4E18-A35E-62FACBCF7E13Q41472888-ACD7449E-653C-4314-A171-441BDBAAA15BQ41667140-40524CF7-52B8-40A0-B021-72971CB09295Q42039270-554BAF98-0B6B-4A23-B035-FC40E58604B1Q47314016-98066F97-6067-4C1E-964D-D315FF8D638FQ50439464-EFBB9BB7-3DD3-4625-9238-8ADA288CB84FQ54575498-46258D65-416B-44B4-81BF-2E02DEF45CAFQ54581192-26191B3F-4810-4729-840E-5243E0D4ED81Q57202161-221F1AEB-ECF0-4E59-BF32-615538FDE444
P2860
Contribution of cotranslational folding to the rate of formation of native protein structure.
description
1995 nî lūn-bûn
@nan
1995 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
Contribution of cotranslationa ...... n of native protein structure.
@ast
Contribution of cotranslationa ...... n of native protein structure.
@en
type
label
Contribution of cotranslationa ...... n of native protein structure.
@ast
Contribution of cotranslationa ...... n of native protein structure.
@en
prefLabel
Contribution of cotranslationa ...... n of native protein structure.
@ast
Contribution of cotranslationa ...... n of native protein structure.
@en
P2860
P356
P1476
Contribution of cotranslationa ...... n of native protein structure.
@en
P2093
Baldwin TO
Fedorov AN
P2860
P304
P356
10.1073/PNAS.92.4.1227
P407
P577
1995-02-01T00:00:00Z