Characterization of the active site thiol group of rhinovirus 2A proteinase.

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A norovirus protease structure provides insights into active and substrate binding site integrity Structure and dynamics of coxsackievirus B4 2A proteinase, an enyzme involved in the etiology of heart disease Enzymatic activity of the SARS coronavirus main proteinase dimer.

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P2860

Characterization of the active site thiol group of rhinovirus 2A proteinase.

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http://www.wikidata.org/entity/Q44823260

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2000 nî lūn-bûn

@nan

2000年の論文

@ja

2000年学术文章

@wuu

2000年学术文章

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2000年学术文章

@zh-cn

2000年学术文章

@zh-hans

2000年学术文章

@zh-my

2000年学术文章

@zh-sg

2000年學術文章

@yue

2000年學術文章

@zh-hant

name

Characterization of the active site thiol group of rhinovirus 2A proteinase.

@en

Characterization of the active site thiol group of rhinovirus 2A proteinase.

@nl

type

Item

label

Characterization of the active site thiol group of rhinovirus 2A proteinase.

@en

Characterization of the active site thiol group of rhinovirus 2A proteinase.

@nl

prefLabel

Characterization of the active site thiol group of rhinovirus 2A proteinase.

@en

Characterization of the active site thiol group of rhinovirus 2A proteinase.

@nl

P1476

Characterization of the active site thiol group of rhinovirus 2A proteinase

@en

P2093

L Polgár

http://www.w3.org/2001/XMLSchema#string

P2860

Tissue sulfhydryl groups

The structure of the 2A proteinase from a common cold virus: a proteinase responsible for the shut-off of host-cell protein synthesis

Refined X-ray crystallographic structure of the poliovirus 3C gene product

Deuterium isotope effects on papain acylation. Evidence for lack of general base catalysis and for enzyme--leaving-group interaction

Consequences of molecular recognition in the S1-S2 intersubsite region of papain for catalytic-site chemistry. Change in pH-dependence characteristics and generation of an inverse solvent kinetic isotope effect by introduction of a P1-P2 amide bond

Structure of human rhinovirus 3C protease reveals a trypsin-like polypeptide fold, RNA-binding site, and means for cleaving precursor polyprotein.

Viral proteinases.

Picornaviral 3C cysteine proteinases have a fold similar to chymotrypsin-like serine proteinases.

Identification of the active site of legumain links it to caspases, clostripain and gingipains in a new clan of cysteine endopeptidases.

Polypeptide 2A of human rhinovirus type 2: identification as a protease and characterization by mutational analysis.

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289-292

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scholarly article

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10.1016/S0014-5793(00)02024-X

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English

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P478

481

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Tim Skern

Z Sárkány

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2000-09-01T00:00:00Z

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12315578

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11007981

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Characterization of the active site thiol group of rhinovirus 2A proteinase.

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P2860

P2860

Characterization of the active site thiol group of rhinovirus 2A proteinase.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P5875

P698

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P5875

P698