Vito Turk--30 years of research on cysteine proteases and their inhibitors.

about

Vito Turk--30 years of research on cysteine proteases and their inhibitors.

Item

http://www.wikidata.org/entity/Q44529747

description

2003 nî lūn-bûn

@nan

2003年の論文

@ja

2003年学术文章

@wuu

2003年学术文章

@zh

2003年学术文章

@zh-cn

2003年学术文章

@zh-hans

2003年学术文章

@zh-my

2003年学术文章

@zh-sg

2003年學術文章

@yue

2003年學術文章

@zh-hant

name

Vito Turk--30 years of research on cysteine proteases and their inhibitors.

@en

Vito Turk--30 years of research on cysteine proteases and their inhibitors.

@nl

type

Item

label

Vito Turk--30 years of research on cysteine proteases and their inhibitors.

@en

Vito Turk--30 years of research on cysteine proteases and their inhibitors.

@nl

prefLabel

Vito Turk--30 years of research on cysteine proteases and their inhibitors.

@en

Vito Turk--30 years of research on cysteine proteases and their inhibitors.

@nl

P1476

Vito Turk--30 years of research on cysteine proteases and their inhibitors

@en

P2093

Hans Fritz

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

P2860

Cloning a synthetic gene for human stefin B and its expression in E. coli

Major histocompatibility complex class II-associated p41 invariant chain fragment is a strong inhibitor of lysosomal cathepsin L

Crystal structure of MHC class II-associated p41 Ii fragment bound to cathepsin L reveals the structural basis for differentiation between cathepsins L and S.

Inhibition mechanism of cathepsin L-specific inhibitors based on the crystal structure of papain-CLIK148 complex

Structure of human dipeptidyl peptidase I (cathepsin C): exclusion domain added to an endopeptidase framework creates the machine for activation of granular serine proteases

Crystal structure of cathepsin B inhibited with CA030 at 2.0-A resolution: A basis for the design of specific epoxysuccinyl inhibitors

Crystal structures of human procathepsin B at 3.2 and 3.3 Angstroms resolution reveal an interaction motif between a papain-like cysteine protease and its propeptide

Molecular cloning and sequence analysis of human preprocathepsin C

Amino acid sequences of the human kidney cathepsins H and L

Human plasma kininogens are identical with alpha-cysteine proteinase inhibitors. Evidence from immunological, enzymological and sequence data.

P304

833-836

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

P31

scholarly article

P356

10.1515/BC.2003.093

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

P433

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

P478

384

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

P50

Boris Turk

P577

2003-06-01T00:00:00Z

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

P698

12887049

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