Subtleties among subtilases. The structural biology of Kex2 and furin-related prohormone convertases.

about

Differential P1 arginine and lysine recognition in the prototypical proprotein convertase Kex2 Processing of predicted substrates of fungal Kex2 proteinases from Candida albicans, C. glabrata, Saccharomyces cerevisiae and Pichia pastoris.

P2860

Q27644405-9D0C6D44-24B3-45E1-9900-98F00C8F69A4 Q33351525-6BA07D65-2023-49B0-8175-0AED1E52143D

P2860

Subtleties among subtilases. The structural biology of Kex2 and furin-related prohormone convertases.

Item

http://www.wikidata.org/entity/Q41011167

description

2003 nî lūn-bûn

@nan

2003年の論文

@ja

2003年論文

@yue

2003年論文

@zh-hant

2003年論文

@zh-hk

2003年論文

@zh-mo

2003年論文

@zh-tw

2003年论文

@wuu

2003年论文

@zh

2003年论文

@zh-cn

name

Subtleties among subtilases. T ...... elated prohormone convertases.

@en

type

Item

label

Subtleties among subtilases. T ...... elated prohormone convertases.

@en

prefLabel

Subtleties among subtilases. T ...... elated prohormone convertases.

@en

P1476

Subtleties among subtilases. T ...... elated prohormone convertases.

@en

P2860

Structural and enzymatic characterization of a purified prohormone-processing enzyme: secreted, soluble Kex2 protease

Furin at the cutting edge: from protein traffic to embryogenesis and disease

Solution structure of the pro-hormone convertase 1 pro-domain from Mus musculus

2.4 A resolution crystal structure of the prototypical hormone-processing protease Kex2 in complex with an Ala-Lys-Arg boronic acid inhibitor

The crystal structure of the proprotein processing proteinase furin explains its stringent specificity

Yeast alpha factor is processed from a larger precursor polypeptide: the essential role of a membrane-bound dipeptidyl aminopeptidase.

Isolation of the putative structural gene for the lysine-arginine-cleaving endopeptidase required for processing of yeast prepro-alpha-factor

Human furin is a calcium-dependent serine endoprotease that recognizes the sequence Arg-X-X-Arg and efficiently cleaves anthrax toxin protective antigen

The ordered and compartment-specfific autoproteolytic removal of the furin intramolecular chaperone is required for enzyme activation.

Proteolytic processing in the secretory pathway.

P304

937-938

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

P31

scholarly article

P356

10.1038/SJ.EMBOR.EMBOR946

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

P433

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

P478

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

P50

Charles Brenner

P577

2003-10-01T00:00:00Z

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

P5875

9064482

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

P698

14528262

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

P932

1326404

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

Subtleties among subtilases. The structural biology of Kex2 and furin-related prohormone convertases.

about

P2860

P2860

Subtleties among subtilases. The structural biology of Kex2 and furin-related prohormone convertases.

description

name

type

label

prefLabel

P1433

P1476

P2860

P304

P31

P356

P433

P478

P50

P577

P5875

P698

P932

P356

P1433

P1476

P2860

P304

P31

P356

P433

P478

P50

P577

P5875

P698

P932