A Fluorescent-Labeled Phosphono Bisbenzguanidine As an Activity-Based Probe for Matriptase.

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A BODIPY-Tagged Phosphono Peptide as Activity-Based Probe for Human Leukocyte Elastase.A Short Peptide Inhibitor as an Activity-Based Probe for Matriptase-2.

P2860

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A Fluorescent-Labeled Phosphono Bisbenzguanidine As an Activity-Based Probe for Matriptase.

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http://www.wikidata.org/entity/Q50754826

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2017 nî lūn-bûn

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2017年の論文

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2017年学术文章

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2017年学术文章

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2017年学术文章

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A Fluorescent-Labeled Phosphon ...... ty-Based Probe for Matriptase.

@en

A Fluorescent-Labeled Phosphon ...... ty-Based Probe for Matriptase.

@nl

type

Item

label

A Fluorescent-Labeled Phosphon ...... ty-Based Probe for Matriptase.

@en

A Fluorescent-Labeled Phosphon ...... ty-Based Probe for Matriptase.

@nl

prefLabel

A Fluorescent-Labeled Phosphon ...... ty-Based Probe for Matriptase.

@en

A Fluorescent-Labeled Phosphon ...... ty-Based Probe for Matriptase.

@nl

P1476

A Fluorescent-Labeled Phosphon ...... ty-Based Probe for Matriptase.

@en

P2093

Aline Keils

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

Anna-Christina Schulz-Fincke

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

Anna-Madeleine Beckmann

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

Daniela Häußler

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

Erik Gilberg

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

Marit Stirnberg

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

Martin Mangold

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

Michael Gütschow

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

Torsten Steinmetzer

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

P2860

Peptide Length and Leaving-Group Sterics Influence Potency of Peptide Phosphonate Protease Inhibitors

Development and binding characteristics of phosphonate inhibitors of SplA protease from Staphylococcus aureus

Discovery of Pyridyl Bis(oxy)dibenzimidamide Derivatives as Selective Matriptase Inhibitors

Inhibition of trypsin and thrombin by amino(4-amidinophenyl)methanephosphonate diphenyl ester derivatives: X-ray structures and molecular models

Type II transmembrane serine proteases. Insights into an emerging class of cell surface proteolytic enzymes

The activation of matriptase requires its noncatalytic domains, serine protease domain, and its cognate inhibitor

Matriptase and its putative role in cancer

Inhibition of Matriptase Activity Results in Decreased Intestinal Epithelial Monolayer Integrity In Vitro

Matriptase, HAT, and TMPRSS2 activate the hemagglutinin of H9N2 influenza A viruses.

Matriptase proteolytically activates influenza virus and promotes multicycle replication in the human airway epithelium.

P304

5205-5209

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scholarly article

P356

10.1002/CHEM.201700319

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English

P433

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

P478

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

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Jürgen Bajorath

P577

2017-03-28T00:00:00Z

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

P698

28370501

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

A Fluorescent-Labeled Phosphono Bisbenzguanidine As an Activity-Based Probe for Matriptase.

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P2860

P2860

A Fluorescent-Labeled Phosphono Bisbenzguanidine As an Activity-Based Probe for Matriptase.

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P1433

P1476

P2093

P2860

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P356

P407

P433

P478

P50

P577

P698

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698