Heterologously overexpressed, affinity-purified human meprin alpha is functionally active and cleaves components of the basement membrane in vitro
about
Meprins, membrane-bound and secreted astacin metalloproteinasesStructure of homo- and hetero-oligomeric meprin metalloproteases. Dimers, tetramers, and high molecular mass multimersActivation of human meprin-alpha in a cell culture model of colorectal cancer is triggered by the plasminogen-activating systemActivation of pro-astacin. Immunological and model peptide studies on the processing of immature astacin, a zinc-endopeptidase from the crayfish Astacus astacus.Compartmentalised expression of meprin in small intestinal mucosa: enhanced expression in lamina propria in coeliac disease.The evolution of the vertebrate metzincins; insights from Ciona intestinalis and Danio rerio.The metalloprotease meprinbeta processes E-cadherin and weakens intercellular adhesionMetalloprotease meprin beta in rat kidney: glomerular localization and differential expression in glomerulonephritis.ADAM10 is the major sheddase responsible for the release of membrane-associated meprin A.Enhanced activity of meprin-α, a pro-migratory and pro-angiogenic protease, in colorectal cancer.Isoform-specific interactions between meprin metalloproteases and the catalytic subunit of protein kinase A: significance in acute and chronic kidney injury.Development of high throughput screening assays and pilot screen for inhibitors of metalloproteases meprin α and β.Villin and actin in the mouse kidney brush-border membrane bind to and are degraded by meprins, an interaction that contributes to injury in ischemia-reperfusionMeprin metalloprotease expression and regulation in kidney, intestine, urinary tract infections and cancer.The substrate degradome of meprin metalloproteases reveals an unexpected proteolytic link between meprin β and ADAM10.Meprin A metalloproteinase and its role in acute kidney injury.Hypoxia Associated Proteolytic Processing of OS-9 by the Metalloproteinase Meprin β.Handling Metalloproteinases.Meprin Metalloprotease Deficiency Associated with Higher Mortality Rates and More Severe Diabetic Kidney Injury in Mice with STZ-Induced Type 1 Diabetes.Proteolytic processing and inactivation of CCL2/MCP-1 by meprins.Human meprin alpha and beta homo-oligomers: cleavage of basement membrane proteins and sensitivity to metalloprotease inhibitors.A profiling platform for the identification of selective metalloprotease inhibitors.Human and mouse homo-oligomeric meprin A metalloendopeptidase: substrate and inhibitor specificities.Evolution of astacin-like metalloproteases in animals and their function in development.Undiagnosed Kidney Injury in Uninsured and Underinsured Diabetic African American Men and Putative Role of Meprin Metalloproteases in Diabetic Nephropathy.
P2860
Q24646365-D46B3322-6800-4C64-AA4E-13342EF6EAEFQ28210655-1730AAE1-D928-4293-B0E5-3072FBC44E6DQ28218647-F944CF65-F72F-4F95-AF5A-9D149B076A26Q30666002-47D0B6C0-574D-450D-AC3B-CB81FC227F78Q33276900-AE022117-BCCC-40A5-83D7-7CF6DDF51A3DQ33282314-2C184434-5AF2-4529-8390-A57E6C33800CQ33334334-87D17A17-24EF-4745-A11B-8A9424D2B876Q33338489-E63A66C5-0E58-4471-B5B1-1CF70BA500A6Q33676656-0C2F222B-35E1-47B4-A33F-DA512DCDB08FQ34077651-2AC39606-AFCC-4D2F-BA5B-5CEBD800143EQ34801085-42745BB8-A478-4BAE-9ABF-BA2CD71E3FAEQ35116223-65844D2A-69B7-4FBC-878C-D51065ADB03FQ35326081-1134E644-5D7D-402E-AF90-B7E3E756FB35Q36156032-D601A118-ECD0-426D-AFCE-422AB984B0FCQ36503385-9D8FCD43-BB5A-4D34-A6D1-C8CB1D29A341Q36836257-40DA0A2C-BDDB-45D1-80D0-36AF55DFA3A6Q37127955-C4EAD656-C5F6-42B0-B636-359D6B0BA50DQ38719790-46D70083-927F-4884-B639-B037E36B2E15Q41215950-B6CD5575-40D8-4D98-9CD9-AA15A6357B3BQ41682687-2C86BEC0-0E98-4FB2-8677-708DF5E2CE40Q41827780-151FAE00-8D7B-4486-BCF7-4C5BC85BB459Q43204016-4FBBD875-0E3C-4BA1-882A-B3595CFFB98AQ46920017-1ADEF912-F90F-48F8-BD8E-061A00F2EBB5Q47220703-305C7237-933C-41AE-A413-C9731E5A047CQ55006125-8AE80620-3FF3-493D-86D4-B51A54C424CB
P2860
Heterologously overexpressed, affinity-purified human meprin alpha is functionally active and cleaves components of the basement membrane in vitro
description
2000 nî lūn-bûn
@nan
2000 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Heterologously overexpressed, ...... the basement membrane in vitro
@ast
Heterologously overexpressed, ...... the basement membrane in vitro
@en
Heterologously overexpressed, ...... the basement membrane in vitro
@nl
type
label
Heterologously overexpressed, ...... the basement membrane in vitro
@ast
Heterologously overexpressed, ...... the basement membrane in vitro
@en
Heterologously overexpressed, ...... the basement membrane in vitro
@nl
prefLabel
Heterologously overexpressed, ...... the basement membrane in vitro
@ast
Heterologously overexpressed, ...... the basement membrane in vitro
@en
Heterologously overexpressed, ...... the basement membrane in vitro
@nl
P2093
P2860
P3181
P1433
P1476
Heterologously overexpressed, ...... the basement membrane in vitro
@en
P2093
P2860
P3181
P356
10.1016/S0014-5793(99)01712-3
P407
P577
2000-01-07T00:00:00Z