A matrix metalloproteinase expressed on the surface of invasive tumour cells
about
Cloning and characterization of human MMP-23, a new matrix metalloproteinase predominantly expressed in reproductive tissues and lacking conserved domains in other family membersRegulation of matrix metalloproteinase-9 and inhibition of tumor invasion by the membrane-anchored glycoprotein RECKLeukolysin/MMP25/MT6-MMP: a novel matrix metalloproteinase specifically expressed in the leukocyte lineageAAC-11 overexpression induces invasion and protects cervical cancer cells from apoptosisMembrane-type 6 matrix metalloproteinase (MT6-MMP, MMP-25) is the second glycosyl-phosphatidyl inositol (GPI)-anchored MMPMT1-MMP cleaves Dll1 to negatively regulate Notch signalling to maintain normal B-cell developmentMembrane-type 1 matrix metalloproteinase cytoplasmic tail-binding protein-1 is a new member of the Cupin superfamily. A possible multifunctional protein acting as an invasion suppressor down-regulated in tumorsMolecular cloning of MADM: a catalytically active mammalian disintegrin-metalloprotease expressed in various cell typesCo-operative interactions between NFAT (nuclear factor of activated T cells) c1 and the zinc finger transcription factors Sp1/Sp3 and Egr-1 regulate MT1-MMP (membrane type 1 matrix metalloproteinase) transcription by glomerular mesangial cellsIdentification and characterization of a novel human matrix metalloproteinase with unique structural characteristics, chromosomal location, and tissue distributionDetection of a latent soluble form of membrane type 1 matrix metalloprotease bound with tissue inhibitor of matrix metalloproteinases-2 in periprosthetic tissues and fluids from loose arthroplasty endoprosthesesThe universal dynamics of tumor growthCytoskeletal protein ABP-280 directs the intracellular trafficking of furin and modulates proprotein processing in the endocytic pathwayRegulation of membrane type-1 matrix metalloproteinase activation by proprotein convertasesTransmembrane transforming growth factor-alpha tethers to the PDZ domain-containing, Golgi membrane-associated protein p59/GRASP55ARK5 is a tumor invasion-associated factor downstream of Akt signalingMultiple molecular targets of resveratrol: Anti-carcinogenic mechanismsTetraspanin proteins regulate membrane type-1 matrix metalloproteinase-dependent pericellular proteolysisGelatinase-A (MMP-2), gelatinase-B (MMP-9) and membrane type matrix metalloproteinase-1 (MT1-MMP) are involved in different aspects of the pathophysiology of malignant gliomasTargeting migration inducting gene-7 inhibits carcinoma cell invasion, early primary tumor growth, and stimulates monocyte oncolytic activityThe molecular mechanisms of the thrombotic complications of atherosclerosisMatriptase and HAI-1 are expressed by normal and malignant epithelial cells in vitro and in vivoThe integrin alpha(v)beta8 mediates epithelial homeostasis through MT1-MMP-dependent activation of TGF-beta1The metzincins--topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidasesFibroblast biology. Role of synovial fibroblasts in the pathogenesis of rheumatoid arthritisMatrix metalloproteinases: old dogs with new tricksHuman breast cancer cell-mediated bone collagen degradation requires plasminogen activation and matrix metalloproteinase activityInhibition of c-Jun NH2-terminal kinase or extracellular signal-regulated kinase improves lung injuryThe Role of Matrix Metalloproteinase Polymorphisms in Ischemic StrokeStudies in mice reveal a role for anthrax toxin receptors in matrix metalloproteinase function and extracellular matrix homeostasisAnthrax toxin receptor 2 functions in ECM homeostasis of the murine reproductive tract and promotes MMP activityQuantitative FRET imaging to visualize the invasiveness of live breast cancer cellsTargeting MT1-MMP as an ImmunoPET-Based Strategy for Imaging GliomasThe Dimer Interface of the Membrane Type 1 Matrix Metalloproteinase Hemopexin Domain: CRYSTAL STRUCTURE AND BIOLOGICAL FUNCTIONSMT1-MMP recognition by ERM proteins and its implication in CD44 sheddingCrystal structure of the haemopexin-like C-terminal domain of gelatinase AThe C-terminal (haemopexin-like) domain structure of human gelatinase A (MMP2): structural implications for its functionAdipose extracellular matrix remodelling in obesity and insulin resistancecDNA sequence and mRNA tissue distribution of a novel human matrix metalloproteinase with a potential transmembrane segmentEvaluation of some newer matrix metalloproteinases
P2860
Q22001456-F3A06A4F-A541-482C-9163-9FDE883403F9Q22004018-3784DEE6-D3E6-4B96-8F7C-2E00652629E1Q22011043-A4DABE2D-FF2C-4D78-8BCA-67E9CFA8D52CQ22253978-7F73CCA9-7201-45A9-BB3D-94E31E304AA5Q24290409-BC579F89-F57A-455F-A841-30F78BB0CDA1Q24302346-A9B6AC31-818D-49D4-9179-55B791D111D0Q24304420-F181AF1E-B2A6-4D53-8349-5BFB35CF01A5Q24310056-66D758FD-A629-4E81-86F7-7E1827AF1BB3Q24311377-DDD7EC9F-3D0E-4470-ADE6-C32BB491A28CQ24317893-89EFDBE1-96F2-4013-B552-FCC1EB438A47Q24338121-CD311C5D-8CDE-4075-8CFF-50078F94282AQ24537729-3E3C8310-D3D9-42C3-ABFE-6A5A112195DDQ24542345-2FAE7584-0A51-4140-9DB3-ACA5CC3844B7Q24550531-35677070-BFB3-43EA-BAEB-BE8CA5BB7256Q24595955-0CF4505E-0608-4E78-8F04-DCB244D44C80Q24603024-E83DEA9F-5EA5-4603-AB98-B5D2D52A97A9Q24648759-5D39B380-3C7F-498B-B936-FB1B56F835C1Q24649625-5AC2329B-6104-48CD-BB01-B8DD3B04E9ACQ24649857-3F8329D8-4334-467C-95E6-1E25FD501B4FQ24650655-FE1BD2DE-94D2-448A-8D22-01DD66C1FCF1Q24656816-1131D6F4-3777-4DFF-9431-CB5227E3C166Q24672921-DB1B77E9-3326-435F-84C2-1C5D75E3B00DQ24673453-88C689E5-48BD-46DD-9BD0-779648700AD4Q24675153-F0778364-E4A8-46EA-9789-6227A7EC1968Q24792470-25853E14-6DD0-4C61-A56F-3D9A24B61C16Q24795980-A4087E9E-E6AE-416A-B472-8B06A3818CBAQ24803810-807C3AE4-5B27-4537-95E9-F573B33F0963Q24808687-B7E2B616-E16A-41CB-A3F4-7CED5665CDA7Q26741200-213198ED-9C18-433D-8657-0AD303A7A09AQ27010122-EF7042AC-6350-45DD-A227-8F77D463FB16Q27304959-0C1C17E7-2F35-413F-A56F-C3AC39C46F80Q27334885-FC287B72-42F8-439B-B7B9-D801574B4FB4Q27335251-73C4D9B6-B958-4375-9DD2-3C886B33C9E2Q27666418-AE5CC02E-D159-46D8-8F83-BF311EE8460BQ27701853-E0E08AFE-B512-4D9F-B249-A8BBAF4F2FEFQ27729731-C30495CA-43EC-4A03-8C17-6226CD04CEB9Q27732240-C91D84E8-4166-496D-9555-23AB90D2332FQ28069494-103E63EA-1EA8-4CAC-B17A-B8DF0542EBB6Q28115693-B2D95828-1B51-49AA-A5C0-3C5132F86127Q28140362-B8B05376-43AF-4A4A-9445-01B058165BC5
P2860
A matrix metalloproteinase expressed on the surface of invasive tumour cells
description
1994 nî lūn-bûn
@nan
1994 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
A matrix metalloproteinase expressed on the surface of invasive tumour cells
@ast
A matrix metalloproteinase expressed on the surface of invasive tumour cells
@en
A matrix metalloproteinase expressed on the surface of invasive tumour cells
@en-gb
A matrix metalloproteinase expressed on the surface of invasive tumour cells
@nl
type
label
A matrix metalloproteinase expressed on the surface of invasive tumour cells
@ast
A matrix metalloproteinase expressed on the surface of invasive tumour cells
@en
A matrix metalloproteinase expressed on the surface of invasive tumour cells
@en-gb
A matrix metalloproteinase expressed on the surface of invasive tumour cells
@nl
prefLabel
A matrix metalloproteinase expressed on the surface of invasive tumour cells
@ast
A matrix metalloproteinase expressed on the surface of invasive tumour cells
@en
A matrix metalloproteinase expressed on the surface of invasive tumour cells
@en-gb
A matrix metalloproteinase expressed on the surface of invasive tumour cells
@nl
P2093
P3181
P356
P1433
P1476
A matrix metalloproteinase expressed on the surface of invasive tumour cells
@en
P2093
A Shinagawa
E Yamamoto
P2888
P3181
P356
10.1038/370061A0
P407
P577
1994-07-07T00:00:00Z
P6179
1038954765