E-64c-hydrazide: a lead structure for the development of irreversible cathepsin C inhibitors.

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Cathepsins mediate tumor metastasis.IL-1 Family Cytokine Pathways Underlying NAFLD: Towards New Treatment Strategies.

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E-64c-hydrazide: a lead structure for the development of irreversible cathepsin C inhibitors.

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http://www.wikidata.org/entity/Q50895934

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2013 nî lūn-bûn

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2013年の論文

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2013年学术文章

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E-64c-hydrazide: a lead struct ...... rsible cathepsin C inhibitors.

@en

E-64c-hydrazide: a lead struct ...... rsible cathepsin C inhibitors.

@nl

type

Item

label

E-64c-hydrazide: a lead struct ...... rsible cathepsin C inhibitors.

@en

E-64c-hydrazide: a lead struct ...... rsible cathepsin C inhibitors.

@nl

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E-64c-hydrazide: a lead struct ...... rsible cathepsin C inhibitors.

@en

E-64c-hydrazide: a lead struct ...... rsible cathepsin C inhibitors.

@nl

P1476

E-64c-hydrazide: a lead struct ...... rsible cathepsin C inhibitors.

@en

P2093

Christian P Sommerhoff

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

Dennis Klimpel

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

Hanna Radzey

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

Maresa Grundhuber

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

Markus Rethmeier

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

Norbert Schaschke

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

P2860

The Primary Structure and Tissue Distribution of Cathepsin

L-trans-Epoxysuccinyl-leucylamido(4-guanidino)butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B, H and L

Haim-Munk syndrome and Papillon-Lefèvre syndrome are allelic mutations in cathepsin C

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

Structural basis for development of cathepsin B-specific noncovalent-type inhibitor: crystal structure of cathepsin B-E64c complex

Irreversible inhibitors of serine, cysteine, and threonine proteases

Efficient parallel synthesis of privileged benzopyranylpyrazoles via regioselective condensation of beta-keto aldehydes with hydrazines.

Novel semicarbazide-derived inhibitors of human dipeptidyl peptidase I (hDPPI).

Dipeptidyl peptidase I is required for the processing and activation of granzymes A and B in vivo.

Critical role of dipeptidyl peptidase I in neutrophil recruitment during the development of experimental abdominal aortic aneurysms.

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1314-1321

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scholarly article

P356

10.1002/CMDC.201300093

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

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2013-06-18T00:00:00Z

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23780739

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E-64c-hydrazide: a lead structure for the development of irreversible cathepsin C inhibitors.

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P2860

P2860

E-64c-hydrazide: a lead structure for the development of irreversible cathepsin C inhibitors.

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P1433

P1476

P2093

P2860

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P433

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P698

P356

P1433

P1476

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P433

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P577

P698