Inhibition of tumor invasion by genomic down-regulation of matriptase through suppression of activation of receptor-bound pro-urokinase - Wikidata - wikimedia - TriplyDB

Inhibition of tumor invasion by genomic down-regulation of matriptase through suppression of activation of receptor-bound pro-urokinase

Inhibition of tumor invasion by genomic down-regulation of matriptase through suppression of activation of receptor-bound pro-urokinase

http://www.wikidata.org/entity/Q28241119

about

Chronic exposure to carbon nanotubes induces invasion of human mesothelial cells through matrix metalloproteinase-2 Role of H-Ras/ERK signaling in carbon nanotube-induced neoplastic-like transformation of human mesothelial cells Regulation of feto-maternal barrier by matriptase- and PAR-2-mediated signaling is required for placental morphogenesis and mouse embryonic survival A Reverse Binding Motif That Contributes to Specific Protease Inhibition by Antibodies Discovery of Pyridyl Bis(oxy)dibenzimidamide Derivatives as Selective Matriptase Inhibitors Inhibition of human matriptase by eglin c variants.Text mining of full-text journal articles combined with gene expression analysis reveals a relationship between sphingosine-1-phosphate and invasiveness of a glioblastoma cell line.Matriptase activation, an early cellular response to acidosis.Deregulated matriptase causes ras-independent multistage carcinogenesis and promotes ras-mediated malignant transformation.Matriptase is involved in ErbB-2-induced prostate cancer cell invasion Matriptase: potent proteolysis on the cell surface.Regulation of cancer cell migration and invasion by sphingosine-1-phosphate Combinatorial optimization of cystine-knot peptides towards high-affinity inhibitors of human matriptase-1 Delineation of matriptase protein expression by enzymatic gene trapping suggests diverging roles in barrier function, hair formation, and squamous cell carcinogenesis Suppression of Tumorigenicity-14, encoding matriptase, is a critical suppressor of colitis and colitis-associated colon carcinogenesis Protein kinase C alpha-CARMA3 signaling axis links Ras to NF-kappa B for lysophosphatidic acid-induced urokinase plasminogen activator expression in ovarian cancer cells Matriptase: a culprit in cancer?ECRG2 regulates cell migration/invasion through urokinase-type plasmin activator receptor (uPAR)/beta1 integrin pathway.Characteristics of the level-of-evidence-1 disease forecast cancer biomarkers uPA and its inhibitor PAI-1.Decreasing the ratio of matriptase/HAI‑1 by downregulation of matriptase as a potential adjuvant therapy in ovarian cancer.The role of type II transmembrane serine protease-mediated signaling in cancer.MicroRNA-17-92 cluster regulates osteoblast proliferation and differentiation.Cleavage of hepatocyte growth factor activator inhibitor-1 by membrane-type MMP-1 activates matriptase.TMPRSS4 promotes invasion, migration and metastasis of human tumor cells by facilitating an epithelial-mesenchymal transition.Autoactivation of matriptase in vitro: requirement for biomembrane and LDL receptor domain.Matriptase activates stromelysin (MMP-3) and promotes tumor growth and angiogenesis.HAI-1 regulates activation and expression of matriptase, a membrane-bound serine protease.Signaling mechanisms responsible for lysophosphatidic acid-induced urokinase plasminogen activator expression in ovarian cancer cells.Simultaneous activation and hepatocyte growth factor activator inhibitor 1-mediated inhibition of matriptase induced at activation foci in human mammary epithelial cells.Matriptase activation and shedding with HAI-1 is induced by steroid sex hormones in human prostate cancer cells, but not in breast cancer cells.Inhibition of cyclooxygenase-2-mediated matriptase activation contributes to the suppression of prostate cancer cell motility and metastasis.Regulation of matriptase and HAI-1 system, a novel therapeutic target in human endometrial cancer cells.Changing the selectivity profile - from substrate analog inhibitors of thrombin and factor Xa to potent matriptase inhibitors.

P2860

Q23923551-A36B2604-743D-4414-A869-7A8CB82A3530 Q23923553-3E5B8120-AA94-4A82-B93C-5E7E27210A8E Q27314964-16513545-FCED-448B-BE38-E6F9DC495FBF Q27676066-68D873A5-6EF0-4F22-9845-8C1923DE8FEC Q27684175-04C687BF-02EC-49E7-A22C-E79D28AC0DFE Q33237770-A252ACB2-A962-4A8C-AFCC-2D0FFB5EB595 Q33253539-279B7DC2-F1E1-4E7B-BFBE-61361BE6F832 Q33661373-E0C50A15-9F72-46D0-A87C-BA70CC32908C Q33917709-B4823983-F6E8-4757-80B9-F41ABB500113 Q34358331-20E250E3-B02C-4FEE-BF4B-DB825653349B Q34809525-5883E313-5E67-4865-BE3C-717D0FD3E189 Q34878519-DCD3179D-4127-4492-AB07-B1D484F8AE62 Q35023006-5CF75799-741F-4036-A7A0-EB035B49BA04 Q35088270-6A43664E-AB27-486F-AC4D-73DBA0AAD6EA Q35823094-6ABDA326-E233-4F3B-ABAD-71D7B587405F Q35885514-4B2A60EB-2EE1-4353-BB41-C01A2E4BC9E7 Q37401353-AB4B684A-A9E7-4EAF-A459-AF977BCDAAE1 Q37431387-3727179A-06F9-42ED-B2B6-2C920D9130D6 Q37801943-1AD45EF9-AD46-415C-AAD1-64444FC31111 Q38760934-B2F6801B-AA47-4A03-B2E8-8233EFA6582A Q39015415-971BAC12-E9BA-422C-B1C4-A90FC428E437 Q39152048-E00C5B77-2581-4550-A76E-1581F0EBB552 Q39437208-B53E2EA0-4749-4EB1-8C7F-C5A2DE398108 Q40060517-1EE44BBD-522E-48FA-9A8D-49581CA9A238 Q40161979-02A39FED-6037-4C9C-A9FF-542A2C527328 Q40227949-D9090594-9D12-407E-B557-A377D2121416 Q40440887-CF0109BF-A35C-4E5A-8608-02A6D92B2A9B Q40470278-AE54EA58-0C49-4D67-AD46-7EB79C404785 Q40482136-BB5C9661-EF80-4DED-87DB-865F590703C7 Q46935250-4F0E1BA1-BAD2-4B35-8A22-58F9D738011C Q51075784-17F4A6D8-2F3A-48F0-81E7-25FE87538068 Q52645865-9D4324CD-9368-4BF1-9908-BFC08AD061CE Q53099256-6B2DD6F3-1821-4717-8738-E9FFEFECA70F

P2860

Inhibition of tumor invasion by genomic down-regulation of matriptase through suppression of activation of receptor-bound pro-urokinase

http://www.wikidata.org/entity/Q28241119

description

2004 nî lūn-bûn

@nan

2004 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2004 թվականի ապրիլին հրատարակված գիտական հոդված

@hy

2004年の論文

@ja

2004年論文

@yue

2004年論文

@zh-hant

2004年論文

@zh-hk

2004年論文

@zh-mo

2004年論文

@zh-tw

2004年论文

@wuu

name

Inhibition of tumor invasion b ...... f receptor-bound pro-urokinase

@ast

Inhibition of tumor invasion b ...... f receptor-bound pro-urokinase

@en

Inhibition of tumor invasion b ...... f receptor-bound pro-urokinase

@nl

type

label

Inhibition of tumor invasion b ...... f receptor-bound pro-urokinase

@ast

Inhibition of tumor invasion b ...... f receptor-bound pro-urokinase

@en

Inhibition of tumor invasion b ...... f receptor-bound pro-urokinase

@nl

prefLabel

Inhibition of tumor invasion b ...... f receptor-bound pro-urokinase

@ast

Inhibition of tumor invasion b ...... f receptor-bound pro-urokinase

@en

Inhibition of tumor invasion b ...... f receptor-bound pro-urokinase

@nl

P1433

Q28241119-D42D66F1-E92A-4525-871B-8435CF44785E

P1476

Q28241119-0D4B3D32-6497-49A7-9B39-14CC795F8E2A

P2093

Q28241119-08CF01F3-4D80-446A-9322-A86FC3E00486

Q28241119-35E9D7FD-C3B5-4CA4-8C84-AA2A75B0120E

Q28241119-6C0E029E-AA87-4D6C-B2FC-F37D3A88939E

Q28241119-78B04F16-7C45-42A9-9205-1D3D8FC63005

Q28241119-7BF37E97-5C5B-43DE-849C-3F4249B1875C

Q28241119-BB7E802D-10EF-42F1-B764-A123F54BFF76

Q28241119-DCDA16FE-2C8D-4D8D-85F5-A0924E8CD5ED

Q28241119-E890B859-2C4A-45A5-8802-47C22C4A8319

P2860

Q28241119-03BF9CA6-6757-411B-A259-38ED5D972DCD

Q28241119-0594E7F2-8911-472D-8D20-4CFD61CF9A00

Q28241119-127B73B6-9819-4D8F-86F4-DB9F6E84CA13

Q28241119-15AB807B-0ECF-427E-9695-E4574BE2BD51

Q28241119-2E6306FF-8003-4A60-AB6E-BA0431C9813B

Q28241119-32BFD6E3-3A06-4448-8D6F-C23D11D8F4A8

Q28241119-4EEBCB0C-3712-455E-A157-9CDF0566D671

Q28241119-58B272B8-3DFE-442B-BE59-9F8AA6161079

Q28241119-595CDD79-6A34-49B4-A0F0-599A6554ACED

Q28241119-67720DF7-8746-43E8-B747-FCE23106A519

P304

Q28241119-CCE2624C-13FA-4C84-B3B6-FCF5572C425D

P31

Q28241119-448CEAEB-7758-4ADD-8A2D-AC06C5EC219A

P3181

Q28241119-DFC2FC79-1C73-41D4-AAB9-02900CE06F1D

P356

Q28241119-4161468D-E1F0-4C60-93E0-DE0CCE3E0935

P407

Q28241119-0CA7CC2C-6156-4EF1-A4B8-B0E06E0CBCCF

P433

Q28241119-7E8E8DF2-5E27-42D3-A856-35E993EE4957

P478

Q28241119-13B43583-79ED-44CF-8E88-2218CB590041

P577

Q28241119-D53F6D8B-A39D-40C4-B8F1-B1C27E6839BB

P698

Q28241119-23B277DE-7FA8-427F-9C4F-1B4972F40318

P3181

P356

P1433

Journal of Biological Chemistry

P1476

Inhibition of tumor invasion b ...... f receptor-bound pro-urokinase

@en

P2093

Chen-Yong Lin

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

Hiroshi Kobayashi

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

Mika Suzuki

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

Mitsuaki Suzuki

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

Naohiro Kanayama

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

Robert B Dickson

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

Toshihiko Terao

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

Yasushi Saga

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

P2860

Molecular cloning of cDNA for matriptase, a matrix-degrading serine protease with trypsin-like activity

Cellular localization of membrane-type serine protease 1 and identification of protease-activated receptor-2 and single-chain urokinase-type plasminogen activator as substrates

Reverse biochemistry: use of macromolecular protease inhibitors to dissect complex biological processes and identify a membrane-type serine protease in epithelial cancer and normal tissue

Lipofection: a highly efficient, lipid-mediated DNA-transfection procedure

Matriptase and HAI-1 are expressed by normal and malignant epithelial cells in vitro and in vivo

Efficient in vitro synthesis of biologically active RNA and RNA hybridization probes from plasmids containing a bacteriophage SP6 promoter

Purification and characterization of a complex containing matriptase and a Kunitz-type serine protease inhibitor from human milk

Ovarian tumor cells express a transmembrane serine protease: a potential candidate for early diagnosis and therapeutic intervention

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

Activation of hepatocyte growth factor and urokinase/plasminogen activator by matriptase, an epithelial membrane serine protease

P304

14899-908

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

P31

scholarly article

P3181

560801

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

P356

10.1074/JBC.M313130200

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

P407

P433

15

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

P478

279

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

P577

2004-04-09T00:00:00Z

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

P698

14747469

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