Single amino acid substitutions globally suppress the folding defects of temperature-sensitive folding mutants of phage P22 coat protein.
about
Nature's favorite building block: Deciphering folding and capsid assembly of proteins with the HK97-foldStepwise molecular display utilizing icosahedral and helical complexes of phage coat and decoration proteins in the development of robust nanoscale display vehicles'Let the phage do the work': using the phage P22 coat protein structures as a framework to understand its folding and assembly mutantsOmpA and OmpC are critical host factors for bacteriophage Sf6 entry in Shigella.Unraveling the role of the C-terminal helix turn helix of the coat-binding domain of bacteriophage P22 scaffolding protein.Characterization of the Prophage Repertoire of African Salmonella Typhimurium ST313 Reveals High Levels of Spontaneous Induction of Novel Phage BTP1.SHV-129: A Gateway to Global Suppressors in the SHV β-Lactamase Family?An intramolecular chaperone inserted in bacteriophage P22 coat protein mediates its chaperonin-independent folding.Bacteriophage P22 capsid size determination: roles for the coat protein telokin-like domain and the scaffolding protein amino-terminus.Polyhead formation in phage P22 pinpoints a region in coat protein required for conformational switching.Determinants of bacteriophage P22 polyhead formation: the role of coat protein flexibility in conformational switching.GroEL/S substrate specificity based on substrate unfolding propensity.Phage P22 procapsids equilibrate with free coat protein subunits.Alleviation of a defect in protein folding by increasing the rate of subunit assembly.A concerted mechanism for the suppression of a folding defect through interactions with chaperones.Coat Protein Mutations That Alter the Flux of Morphogenetic Intermediates through the ϕX174 Early Assembly Pathway.
P2860
Q28647860-4E443E48-B072-4006-BDAF-5E0BDC20F8FFQ30417846-94412B5D-DA97-4B44-913E-D91D0C8A643FQ30494291-D0A321C2-E407-4F7A-80FE-5AA35FD190B0Q30578890-D8E988D9-8CE9-46F9-BF24-E4C29E71C04EQ36286184-1397CC92-CB70-4ECA-9ECC-BD7CEF159041Q36303585-C4BF25D4-96B9-41B9-87B9-E65AB080C90FQ37007861-EB5B250E-2761-4039-AD08-F31627EBDC80Q37333736-3C4BDC21-3C01-4FC5-8AFC-02609C2FCF0EQ38270659-65C8A8D0-D215-426B-A82E-F3D18A583153Q39080227-F8F49C0D-DA21-42A6-81C9-DF16526D249DQ41618323-58BF9301-474F-4A93-9261-E7752D884647Q42104362-EAA7FCDB-4B3C-4423-B6BA-F717B074B8A4Q42279715-AAB20833-9AAC-4B91-9E4D-DA773271C80EQ43576570-FABE334E-177A-431A-A8F3-11B617DD9DBAQ44756926-5233219C-4234-4A2F-ABBB-4444B33EEE5AQ47623034-3D2A4CCB-7027-4C8E-A0D1-B59BED2EA0BC
P2860
Single amino acid substitutions globally suppress the folding defects of temperature-sensitive folding mutants of phage P22 coat protein.
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
1999年學術文章
@zh-hant
name
Single amino acid substitution ...... nts of phage P22 coat protein.
@en
Single amino acid substitution ...... nts of phage P22 coat protein.
@nl
type
label
Single amino acid substitution ...... nts of phage P22 coat protein.
@en
Single amino acid substitution ...... nts of phage P22 coat protein.
@nl
prefLabel
Single amino acid substitution ...... nts of phage P22 coat protein.
@en
Single amino acid substitution ...... nts of phage P22 coat protein.
@nl
P2860
P356
P1476
Single amino acid substitution ...... nts of phage P22 coat protein.
@en
P2093
P2860
P304
22217-22224
P356
10.1074/JBC.274.32.22217
P407
P577
1999-08-01T00:00:00Z