Temperature-sensitive mutants blocked in the folding or subunit of the bacteriophage P22 tail spike protein. II. Active mutant proteins matured at 30 degrees C.
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Role for cysteine residues in the in vivo folding and assembly of the phage P22 tailspikeCircularly permuted dihydrofolate reductase possesses all the properties of the molten globule state, but can resume functional tertiary structure by interaction with its ligands.Folding of dimeric methionine adenosyltransferase III: identification of two folding intermediates.Intragenic suppressors of folding defects in the P22 tailspike protein.Suppressors of the ndc10-2 mutation: a role for the ubiquitin system in Saccharomyces cerevisiae kinetochore function.Mechanism of phage P22 tailspike protein folding mutations.Folding and assembly of phage P22 tailspike endorhamnosidase lacking the N-terminal, head-binding domain.Amino acid substitutions influencing intracellular protein folding pathways.Characterization in vitro of the defect in a temperature-sensitive mutant of the protein subunit of RNase P from Escherichia coliMultimeric intermediates in the pathway to the aggregated inclusion body state for P22 tailspike polypeptide chains.Temperature-sensitive Saccharomyces cerevisiae mutant defective in lipid biosynthesis.Trimeric intermediate in the in vivo folding and subunit assembly of the tail spike endorhamnosidase of bacteriophage P22.Genetic analysis of the folding pathway for the tail spike protein of phage P22.Single amino acid substitutions influencing the folding pathway of the phage P22 tail spike endorhamnosidase.Phage P22 tailspike protein: removal of head-binding domain unmasks effects of folding mutations on native-state thermal stability.Protein folding failure sets high-temperature limit on growth of phage P22 in Salmonella enterica serovar Typhimurium.Isolation of suppressors of temperature-sensitive folding mutationsCharacterization of Saccharomycopsis lipolytica mutants that express temperature-sensitive synthesis of isocitrate lyase.Three amino acids that are critical to formation and stability of the P22 tailspike trimer.Folding intermediates are involved in genetic diseases?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.Genetic properties of temperature-sensitive folding mutants of the coat protein of phage P22.Pressure dissociation studies provide insight into oligomerization competence of temperature-sensitive folding mutants of P22 tailspike.Alleviation of a defect in protein folding by increasing the rate of subunit assembly.Monoclonal antibody epitope mapping describes tailspike beta-helix folding and aggregation intermediates.Single amino acid substitutions globally suppress the folding defects of temperature-sensitive folding mutants of phage P22 coat protein.Unfolding of bacteriophage P22 tailspike protein: enhanced thermal stability of an N-terminal fusion mutant.Interaction of Salmonella phage P22 with its O-antigen receptor studied by X-ray crystallography.Folding of coliphage T4 short tail fiber in vitro. Analysing the role of a bacteriophage-encoded chaperone.The effects of mutations, deletions and insertions of single amino acids on the three-dimensional structure of globins
P2860
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P2860
Temperature-sensitive mutants blocked in the folding or subunit of the bacteriophage P22 tail spike protein. II. Active mutant proteins matured at 30 degrees C.
description
1981 nî lūn-bûn
@nan
1981年の論文
@ja
1981年学术文章
@wuu
1981年学术文章
@zh
1981年学术文章
@zh-cn
1981年学术文章
@zh-hans
1981年学术文章
@zh-my
1981年学术文章
@zh-sg
1981年學術文章
@yue
1981年學術文章
@zh-hant
name
Temperature-sensitive mutants ...... teins matured at 30 degrees C.
@en
Temperature-sensitive mutants ...... teins matured at 30 degrees C.
@nl
type
label
Temperature-sensitive mutants ...... teins matured at 30 degrees C.
@en
Temperature-sensitive mutants ...... teins matured at 30 degrees C.
@nl
prefLabel
Temperature-sensitive mutants ...... teins matured at 30 degrees C.
@en
Temperature-sensitive mutants ...... teins matured at 30 degrees C.
@nl
P1476
Temperature-sensitive mutants ...... teins matured at 30 degrees C.
@en
P2093
P304
P356
10.1016/0022-2836(81)90307-7
P407
P577
1981-02-01T00:00:00Z