The peptidases from fungi and viruses. - Wikidata - awgldk - TriplyDB

The peptidases from fungi and viruses.

The peptidases from fungi and viruses.

http://www.wikidata.org/entity/Q36559710

about

New families of carboxyl peptidases: serine-carboxyl peptidases and glutamic peptidases.Studies on the catalytic mechanism of a glutamic peptidase.

P2860

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P2860

The peptidases from fungi and viruses.

http://www.wikidata.org/entity/Q36559710

description

2006 nî lūn-bûn

@nan

2006年の論文

@ja

2006年論文

@yue

2006年論文

@zh-hant

2006年論文

@zh-hk

2006年論文

@zh-mo

2006年論文

@zh-tw

2006年论文

@wuu

2006年论文

@zh

2006年论文

@zh-cn

name

The peptidases from fungi and viruses.

@ast

The peptidases from fungi and viruses.

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type

label

The peptidases from fungi and viruses.

@ast

The peptidases from fungi and viruses.

@en

prefLabel

The peptidases from fungi and viruses.

@ast

The peptidases from fungi and viruses.

@en

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P1433

Biological Chemistry

P1476

The peptidases from fungi and viruses.

@en

P2093

Michael N G James

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

P2860

Crystal structure of an inhibitor complex of the 3C proteinase from hepatitis A virus (HAV) and implications for the polyprotein processing in HAV

Structure and refinement of penicillopepsin at 1.8 A resolution

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

MEROPS: the peptidase database.

Beta-lactones as a new class of cysteine proteinase inhibitors: inhibition of hepatitis A virus 3C proteinase by N-Cbz-serine beta-lactone.

The molecular structure and catalytic mechanism of a novel carboxyl peptidase from Scytalidium lignicolum.

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

Catalytic residues and substrate specificity of scytalidoglutamic peptidase, the first member of the eqolisin in family (G1) of peptidases.

Dual modes of modification of hepatitis A virus 3C protease by a serine-derived beta-lactone: selective crystallization and formation of a functional catalytic triad in the active site.

Functional dissection of a poliovirus cis-acting replication element [PV-cre(2C)]: analysis of single- and dual-cre viral genomes and proteins that bind specifically to PV-cre RNA

P304

1023-1029

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P31

scholarly article

P356

10.1515/BC.2006.126

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P433

8

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P478

387

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P577

2006-08-01T00:00:00Z

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P698

16895471

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