A concerted mechanism for the suppression of a folding defect through interactions with chaperones.
about
'Let the phage do the work': using the phage P22 coat protein structures as a framework to understand its folding and assembly mutantsThe C-terminal cysteine annulus participates in auto-chaperone function for Salmonella phage P22 tailspike folding and assembly.GroEL/S substrate specificity based on substrate unfolding propensity.
P2860
A concerted mechanism for the suppression of a folding defect through interactions with chaperones.
description
2004 nî lūn-bûn
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name
A concerted mechanism for the ...... interactions with chaperones.
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A concerted mechanism for the ...... interactions with chaperones.
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type
label
A concerted mechanism for the ...... interactions with chaperones.
@en
A concerted mechanism for the ...... interactions with chaperones.
@nl
prefLabel
A concerted mechanism for the ...... interactions with chaperones.
@en
A concerted mechanism for the ...... interactions with chaperones.
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P2093
P2860
P356
P1476
A concerted mechanism for the ...... interactions with chaperones.
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P2093
Carolyn M Teschke
Eric Anderson
Kristin N Parent
Shannon M Doyle
P2860
P304
17473-17482
P356
10.1074/JBC.M400467200
P407
P577
2004-02-04T00:00:00Z