Processing of human protryptase in mast cells involves cathepsins L, B, and C. - Wikidata - awgldk - TriplyDB

Processing of human protryptase in mast cells involves cathepsins L, B, and C.

Processing of human protryptase in mast cells involves cathepsins L, B, and C.

http://www.wikidata.org/entity/Q35147673

about

Biomarkers of the involvement of mast cells, basophils and eosinophils in asthma and allergic diseases Mutational tail loss is an evolutionary mechanism for liberating marapsins and other type I serine proteases from transmembrane anchors.Mast cell proteases as pharmacological targets Mast cell secretory granules: armed for battle.Sexual dimorphism in the mast cell transcriptome and the pathophysiological responses to immunological and psychological stress.Tryptase inhibitors: a patent review.A Role for Human Skin Mast Cells in Dengue Virus Infection and Systemic Spread.Platelets Induce Thymic Stromal Lymphopoietin Production by Endothelial Cells: Contribution to Fibrosis in Human Systemic Sclerosis.

P2860

Q26767423-0C479AF2-BC11-499D-8FBD-4CC6820EDCC5 Q28709095-099609B5-602B-4345-B8D1-617A1E24503E Q34475790-CCE04C58-955B-429A-893D-6E8C1EBC9F3B Q35182662-0A95814F-BF13-42F0-831B-AFE89A42233F Q37431685-3F53D50B-B018-432E-8695-184E0EDDE865 Q38692832-A7319798-402D-4502-95A7-13036CB0C62E Q40082082-6142AD92-04F9-4CE7-98B7-EA44A41D252C Q47651642-0A4D773E-0BE6-4B42-B62C-36753C54ED43

P2860

Processing of human protryptase in mast cells involves cathepsins L, B, and C.

http://www.wikidata.org/entity/Q35147673

description

2011 nî lūn-bûn

@nan

2011 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի հուլիսին հրատարակված գիտական հոդված

@hy

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

name

Processing of human protryptase in mast cells involves cathepsins L, B, and C.

@ast

Processing of human protryptase in mast cells involves cathepsins L, B, and C.

@en

type

label

Processing of human protryptase in mast cells involves cathepsins L, B, and C.

@ast

Processing of human protryptase in mast cells involves cathepsins L, B, and C.

@en

prefLabel

Processing of human protryptase in mast cells involves cathepsins L, B, and C.

@ast

Processing of human protryptase in mast cells involves cathepsins L, B, and C.

@en

P1433

Q35147673-32A23B1C-6DE5-4584-9A92-CD500B6C9E52

P1476

Q35147673-CC1B7D01-6BE0-4DD6-A112-243DC06F26C8

P2093

Q35147673-0B1A3879-4BB9-4052-B420-6B750FEBC46E

Q35147673-1E11B16D-FA48-47A2-83D8-F6E42C9F745F

Q35147673-2264752A-A4C4-4DA5-94FA-F5713323D851

Q35147673-557B2F8A-E648-4DDD-9051-3A71162891C9

Q35147673-BC7E03B8-F39A-4834-A0B7-457837FA6FB6

Q35147673-CB0EE0FB-C9E3-4B56-8EDB-4067B05B869D

Q35147673-DBFB4E11-3574-4B6E-973D-E8CD331AE1F4

Q35147673-EFFF14AF-654F-4FD0-950B-760550FAB2AD

P2860

Q35147673-00F9D08A-AC88-4511-BDF7-FDCD5EA96517

Q35147673-096B54A9-AD63-4A63-8685-9DB58BF6527E

Q35147673-09930984-0FC6-4A3D-81F3-ABBCACBC940A

Q35147673-0DC6AB60-3C1A-4F7A-A650-E47B3D809410

Q35147673-1A56243B-FD31-4E3D-B8AE-2BDAB45755D3

Q35147673-20BC0E64-5264-40B3-98F2-03E0319C98C4

Q35147673-296FE902-3712-4E70-9818-76A1A51117CB

Q35147673-33848F37-7036-4133-8B89-ECB2DD06F1DF

Q35147673-47EA0EC6-B4EA-4503-A086-47D418754C3C

Q35147673-4F0A13DA-B738-4835-BBEF-A6AB0CA9541F

P304

Q35147673-6D85C6FF-3A63-4AF1-97B4-292DB7A75279

P31

Q35147673-1D714D21-A43B-40F6-AB14-BDBF2AEF67ED

P356

Q35147673-E76C2641-BAFE-4C48-9160-02E2D0ABEDF3

P407

Q35147673-B5C0CC5F-57BB-42C0-BE06-A7B0D3EAD5CE

P433

Q35147673-7CF9A599-9176-4F4D-92A0-17637B22F8F4

P478

Q35147673-952FB88E-C4EE-453F-80D3-D831B3715470

P577

Q35147673-FB654E56-C556-4519-8A00-25A8AF536816

P5875

Q35147673-9678C766-78BC-4464-8209-0938D52C539F

P698

Q35147673-934D6626-AADC-4841-9406-36C8C0973041

P921

Q35147673-4ED63013-7397-44D5-8C48-1752C1A4E51F

P932

Q35147673-2A3C7689-CA90-4ED9-907A-FF74BD6A82AA

P356

JIMMUNOL.1001806

P1433

Journal of Immunology

P1476

Processing of human protryptase in mast cells involves cathepsins L, B, and C.

@en

P2093

Gregorio Gomez

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

Han-Zhang Xia

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

Jiang Hu

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

Lawrence B Schwartz

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

Nobuhiko Katunuma

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

Quang T Le

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

Wei Zhao

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

Yoshihiro Fukuoka

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

P2860

The B12 anti-tryptase monoclonal antibody disrupts the tetrameric structure of heparin-stabilized beta-tryptase to form monomers that are inactive at neutral pH and active at acidic pH

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.

Purification and characterization of dipeptidyl peptidase I from human spleen

Cathepsin B, Cathepsin H, and cathepsin L

Cathepsin L: critical role in Ii degradation and CD4 T cell selection in the thymus

Promiscuous processing of human alphabeta-protryptases by cathepsins L, B, and C

Cathepsin L is essential for onset of autoimmune diabetes in NOD mice.

Acid hydrolases and tryptase from secretory granules of dispersed human lung mast cells.

Cathepsin L in secretory vesicles functions as a prohormone-processing enzyme for production of the enkephalin peptide neurotransmitter.

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

P304

1912-1918

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

P31

scholarly article

P356

10.4049/JIMMUNOL.1001806

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

P407

P433

4

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

P478

187

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

P577

2011-07-08T00:00:00Z

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

P5875

51480527

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

P698

21742978

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

P921

P932

3150348

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