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Molecular mechanisms for the conversion of zymogens to active proteolytic enzymesAn amino-terminal domain of the hepatitis C virus NS3 protease is essential for interaction with NS4AComplex formation between the NS3 serine-type proteinase of the hepatitis C virus and NS4A and its importance for polyprotein maturationBoth NS3 and NS4A are required for proteolytic processing of hepatitis C virus nonstructural proteinsStructural and mutational analysis of a monomeric and dimeric form of a single domain antibody with implications for protein misfoldingStructural evidence of intramolecular propeptide inhibition of the aspzincin metalloendopeptidase AsaP1Structure of alpha-lytic protease complexed with its pro regionThe ordered and compartment-specfific autoproteolytic removal of the furin intramolecular chaperone is required for enzyme activation.Thermodynamic propensities of amino acids in the native state ensemble: implications for fold recognition.Protein homeostasis disorders of key enzymes of amino acids metabolism: mutation-induced protein kinetic destabilization and new therapeutic strategies.Evolution, energy landscapes and the paradoxes of protein folding.Structure prediction for CASP8 with all-atom refinement using Rosetta.Refolding of barnase mutants and pro-barnase in the presence and absence of GroEL.Disabling the folding catalyst is the last critical step in alpha-lytic protease foldingStructural and energetic determinants of the S1-site specificity in serine proteases.Rubella virus nonstructural protein protease domains involved in trans- and cis-cleavage activities.Trafficking of the vasopressin and oxytocin prohormone through the regulated secretory pathway.A plant alternative to animal caspases: subtilisin-like proteasesDecoding the folding of Burkholderia glumae lipase: folding intermediates en route to kinetic stabilityFolding and assembly of phage P22 tailspike endorhamnosidase lacking the N-terminal, head-binding domain.Sequence-dependent denaturation energetics: A major determinant in amyloid disease diversity.Amino acid substitutions influencing intracellular protein folding pathways.Inhibition of cathepsin L-like proteases by cathepsin V propeptide.Aeropin from the extremophile Pyrobaculum aerophilum bypasses the serpin misfolding trap.The Kex2p proregion is essential for the biosynthesis of an active enzyme and requires a C-terminal basic residue for its function.Irreversible denaturation of maltodextrin glucosidase studied by differential scanning calorimetry, circular dichroism, and turbidity measurementsConformational control through translocational regulation: a new view of secretory and membrane protein folding.Insights from bacterial subtilases into the mechanisms of intramolecular chaperone-mediated activation of furinConserved prosegment residues stabilize a late-stage folding transition state of pepsin independently of ground states.Role of N-linked glycosylation in the secretion and enzymatic properties of Rhizopus chinensis lipase expressed in Pichia pastorisLipase-specific foldases.A molten globule-to-ordered structure transition of Drosophila melanogaster crammer is required for its ability to inhibit cathepsin.On the thermodynamic hypothesis of protein foldingCooperativity in protein-folding kinetics.Kinetic stability as a mechanism for protease longevity.Folding of the multidomain human immunodeficiency virus type-I integraseFolding pathway mediated by an intramolecular chaperone.The folding landscape of Streptomyces griseus protease B reveals the energetic costs and benefits associated with evolving kinetic stabilityYeast cytosine deaminase mutants with increased thermostability impart sensitivity to 5-fluorocytosineIndividual subunits of bacterial luciferase are molten globules and interact with molecular chaperones.
P2860
Q24673104-CFDF63E8-9365-4AEF-84B3-4B6E8E5DF906Q27478459-1A497801-5E24-4434-B543-BA6D7599B220Q27480317-FBCA5658-178C-4221-86A2-9F151031E345Q27485988-2D34099D-A297-434B-AED0-A7595FCA8462Q27694789-7759C849-0028-4BE4-9995-388D81C5D3CEQ27727696-A9E35D8B-D003-4893-B016-E0B249596851Q27765940-A15F0569-2653-471F-A13C-AEC4424592F8Q28941778-936F47DD-2092-4F74-B939-1B1CE76D0DBCQ30328135-67240EFA-00D6-4ED0-9C5B-72B927A02424Q30355120-7A67FF3F-AC50-4A70-897B-3BF06B42409EQ30370011-B48DF016-EC2A-4E03-AC5E-043C1C3DC69DQ30380039-3FD4832D-051B-4F8D-8382-36AFBE3FC628Q30419640-B927773E-5C56-4A5E-85A5-AB5C6D515454Q31037380-B6EF3E70-8503-494F-BAB1-284B533680D0Q33548213-B339E659-4F54-4897-887B-A5BCFCE43A3FQ33805356-6F865E48-1EC5-406C-AA94-5D5C1FE031B7Q33938177-0B866A3A-27C9-4122-A857-630684973B67Q34183085-FB73FEFA-449F-497F-BCE6-BE4CAFA62C03Q34277600-CB6BE50D-FADB-4AEB-B481-E332CE7B660FQ34353050-A85E3B37-AF10-4C16-AADE-1F1582A73222Q34443897-F15EDE8C-EABC-47DA-B6FF-980B9EE4FB13Q34481589-4CBAF653-B4CD-410F-8E04-225B17F01D78Q34630480-F3562BF3-E8AA-4493-9306-5F668255F04DQ34652212-0194026C-B24E-441D-AF25-827FEB1B31F7Q34719901-FC1803AA-8744-452C-B43B-F9FB68F32902Q34789967-82211D77-E178-4AA4-B598-2865ED6FCB12Q34811607-967B6F58-CC68-4DC8-A9B7-83BCE7D5FD1FQ34989002-3F92736C-40D3-43DC-8F6E-4F5B5AE4A29AQ35199297-F713F750-E477-44DB-AE77-98838DC152A5Q35563247-2246BE82-50F4-4EEF-B0CB-38DBDC26820EQ35648031-428B46D5-92DC-4C6A-A3BA-C3E7D0DAD6FAQ35778765-8496E4AB-AA07-49ED-84E9-78D6707B7951Q36091068-0AA1E325-3BD0-4F0B-92D3-1C629164DB0FQ36142260-EBA4B501-2A66-46BB-96D1-4632DC75C5FCQ36176625-D569EC39-4B92-4A17-8625-7D01486B7634Q36278761-676552F7-7AD8-4FE1-8307-FBEDA4AF1BC8Q36440336-52DAFD8B-F7B9-4499-95B3-F520DCDCC098Q36526421-D05EDF24-D896-4C28-90F4-868413117EFDQ36580716-CC7A498F-3137-4A15-B1E5-5980C0B83D80Q36675735-3EDFB56F-F84A-407F-BAB8-6539F7856CCA
P2860
description
1992 nî lūn-bûn
@nan
1992年の論文
@ja
1992年学术文章
@wuu
1992年学术文章
@zh
1992年学术文章
@zh-cn
1992年学术文章
@zh-hans
1992年学术文章
@zh-my
1992年学术文章
@zh-sg
1992年學術文章
@yue
1992年學術文章
@zh-hant
name
A protein-folding reaction under kinetic control.
@en
A protein-folding reaction under kinetic control.
@nl
type
label
A protein-folding reaction under kinetic control.
@en
A protein-folding reaction under kinetic control.
@nl
prefLabel
A protein-folding reaction under kinetic control.
@en
A protein-folding reaction under kinetic control.
@nl
P356
P1433
P1476
A protein-folding reaction under kinetic control.
@en
P2093
P2888
P304
P356
10.1038/356263A0
P407
P577
1992-03-01T00:00:00Z
P5875
P6179
1033610056