A newly synthesized, ribosome-bound polypeptide chain adopts conformations dissimilar from early in vitro refolding intermediates.
about
A structural ensemble of a ribosome-nascent chain complex during cotranslational protein folding.Kinetic analysis of ribosome-bound fluorescent proteins reveals an early, stable, cotranslational folding intermediate.Protein folding by domain V of Escherichia coli 23S rRNA: specificity of RNA-protein interactionsMonitoring cotranslational protein folding in mammalian cells at codon resolutionRare codons cluster.Increased incidence of rare codon clusters at 5' and 3' gene termini: implications for function.Probing ribosome-nascent chain complexes produced in vivo by NMR spectroscopy.Cotranslational folding increases GFP folding yieldChaperone-mediated folding and maturation of the penicillin acylase precursor in the cytoplasm of Escherichia coli.Dynamic fluorescence depolarization: a powerful tool to explore protein folding on the ribosomeIn vivo translation rates can substantially delay the cotranslational folding of the Escherichia coli cytosolic proteomeAn elongated spine of buried core residues necessary for in vivo folding of the parallel beta-helix of P22 tailspike adhesin.The co-translational folding and interactions of nascent protein chains: a new approach using fluorescence resonance energy transfer.Dissociation of intermolecular disulfide bonds in P22 tailspike protein intermediates in the presence of SDSThe interdigitated beta-helix domain of the P22 tailspike protein acts as a molecular clamp in trimer stabilizationAutotransporters: The Cellular Environment Reshapes a Folding Mechanism to Promote Protein TransportQuality over quantity: optimizing co-translational protein folding with non-'optimal' synonymous codons.Protein folding on the ribosome studied using NMR spectroscopy.Direct imaging electron microscopy (EM) methods in modern structural biology: overview and comparison with X-ray crystallography and single-particle cryo-EM reconstruction in the studies of large macromolecules.Expanding Anfinsen's principle: contributions of synonymous codon selection to rational protein design.The ribosome in action: Tuning of translational efficiency and protein folding.The pathophysiology of defective proteostasis in the hypothalamus - from obesity to ageing.Folding of proteins with a flavodoxin-like architecture.The ribosome and its role in protein folding: looking through a magnifying glass.23S rRNA assisted folding of cytoplasmic malate dehydrogenase is distinctly different from its self-folding.Cotranslational folding promotes beta-helix formation and avoids aggregation in vivo.Chain dynamics of nascent polypeptides emerging from the ribosome.C-terminal hydrophobic interactions play a critical role in oligomeric assembly of the P22 tailspike trimer.Buried hydrophobic side-chains essential for the folding of the parallel beta-helix domains of the P22 tailspike.Ligand-driven vectorial folding of ribosome-bound human CFTR NBD1Evidence of evolutionary selection for cotranslational folding.Unraveling co-translational protein folding: Concepts and methods.Prediction of variable translation rate effects on cotranslational protein folding.Monoclonal antibody epitope mapping describes tailspike beta-helix folding and aggregation intermediates.Modeling the effect of codon translation rates on co-translational protein folding mechanisms of arbitrary complexity.Homogeneous stalled ribosome nascent chain complexes produced in vivo or in vitro.
P2860
Q27704200-56C526A0-FEDD-4A20-9AD2-E660F46322C1Q30155421-F409A5A6-CEE0-4231-AA50-F522396D89A9Q33321822-C079CAC5-6D8C-4E50-82ED-974258368D85Q33353919-C934092D-408B-4199-9738-1476FA9228D4Q33377033-20D52841-1C69-4C6C-AAF8-F88DE536F4A6Q33532304-FEA8B22C-29CF-4D94-BC68-159EC60C8058Q33564161-04BEE9EE-9C5A-4554-960A-7FA6154EDE68Q33767764-7F5711CF-C793-44E3-AACB-997339C62A0DQ34097904-1BE6E990-4AFB-4FF0-A17E-E275CB24D93FQ34108044-16784D42-E67E-4B7B-A1C5-39022A316AECQ34318728-1913EDEA-48A4-4F93-A878-669231C107E2Q34410800-E06B35CC-4932-4779-9FF1-64A31373869AQ36024278-D1DA508D-12B3-4F19-B21B-3AA8F020B527Q36088377-70BFC93A-713A-43DE-9671-92F5E2FA2706Q36639162-A3F3C90F-E8EE-4C53-AC07-E89C2CAA2F44Q36846535-EAD0208C-AB8C-44E0-849B-0A70EF40E98AQ37230401-8D84D9DF-EFA2-4EF7-947D-580C90DA8C91Q37710489-9B0DF145-B56C-4D8D-A472-736CFC78BA0FQ38231426-C3AA9CD9-D391-41F8-9A9C-8B27FDEA8F62Q38362696-A3435903-27E3-4705-A036-1955939EB331Q38838979-53E54678-CD1D-4C91-BDBD-3888581D5701Q38889413-78EF82F4-1069-465D-969C-8D985AC8B3EBQ39222310-C124747C-3EE6-4631-B5C1-219FC9734952Q39350724-D5E61B7E-EC3C-43BF-971D-B4937F3F8BE7Q39615665-25D7BF01-08CC-4DC5-94A5-A07E960729E3Q41140712-305727C1-0DF9-4619-A2A2-D4BCEAC92C65Q41810556-0753C694-F4F9-402C-8E37-F3F17512CC38Q41833119-416AE35D-D7FF-4D40-A4E5-656CA0A11498Q41862592-367611A6-BCC3-4FF4-ADF0-AAE7A7BC3555Q42093794-7AE6B769-A3BC-467B-9958-A66A1CD6C19DQ47111766-A696A1A8-A4B3-4EEA-A191-2914B4E7B957Q47314016-F4F3923C-E905-4E8A-8E8A-5D2742526EF2Q47696268-C31D0A22-611C-4C6C-9DE3-8324C4FB90E4Q50091591-F908CF6E-76B5-4B92-8540-AC48D1833E29Q51580383-B5A018B8-760E-4FC2-A03C-2466D56528B5Q54478521-442929E7-5B5F-49AF-A90B-3A5596210A25
P2860
A newly synthesized, ribosome-bound polypeptide chain adopts conformations dissimilar from early in vitro refolding intermediates.
description
2001 nî lūn-bûn
@nan
2001年の論文
@ja
2001年学术文章
@wuu
2001年学术文章
@zh-cn
2001年学术文章
@zh-hans
2001年学术文章
@zh-my
2001年学术文章
@zh-sg
2001年學術文章
@yue
2001年學術文章
@zh
2001年學術文章
@zh-hant
name
A newly synthesized, ribosome- ...... vitro refolding intermediates.
@en
A newly synthesized, ribosome- ...... vitro refolding intermediates.
@nl
type
label
A newly synthesized, ribosome- ...... vitro refolding intermediates.
@en
A newly synthesized, ribosome- ...... vitro refolding intermediates.
@nl
prefLabel
A newly synthesized, ribosome- ...... vitro refolding intermediates.
@en
A newly synthesized, ribosome- ...... vitro refolding intermediates.
@nl
P2860
P356
P1476
A newly synthesized, ribosome- ...... vitro refolding intermediates.
@en
P2860
P304
25411-25420
P356
10.1074/JBC.M008490200
P407
P577
2001-04-23T00:00:00Z