Human meprin alpha and beta homo-oligomers: cleavage of basement membrane proteins and sensitivity to metalloprotease inhibitors.
about
Cleavage of nidogen-1 by cathepsin S impairs its binding to basement membrane partnersMeprins, membrane-bound and secreted astacin metalloproteinasesMEP1A allele for meprin A metalloprotease is a susceptibility gene for inflammatory bowel diseaseRemodelling the extracellular matrix in development and diseaseIntestinal epithelium in inflammatory bowel diseaseMMP-2 induced vein relaxation via inhibition of [Ca2+]e-dependent mechanisms of venous smooth muscle contraction. Role of RGD peptidesLRP1 Modulates APP Intraneuronal Transport and Processing in Its Monomeric and Dimeric StateThe 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.Discovery of an enzyme and substrate selective inhibitor of ADAM10 using an exosite-binding glycosylated substrateRole of meprins to protect ileal mucosa of Crohn's disease patients from colonization by adherent-invasive E. coliEnhanced activity of meprin-α, a pro-migratory and pro-angiogenic protease, in colorectal cancer.Microbial-induced meprin β cleavage in MUC2 mucin and a functional CFTR channel are required to release anchored small intestinal mucus.Potent tumor targeting drug release system comprising MMP-2 specific peptide fragment with self-assembling characteristicsBalance of meprin A and B in mice affects the progression of experimental inflammatory bowel disease.Inhibition of bone morphogenetic protein 1 by native and altered forms of alpha2-macroglobulin.Isoform-specific interactions between meprin metalloproteases and the catalytic subunit of protein kinase A: significance in acute and chronic kidney injury.A Comparative Study of Fibronectin Cleavage by MMP-1, -3, -13, and -14Development of high throughput screening assays and pilot screen for inhibitors of metalloproteases meprin α and β.Proteomic analyses reveal an acidic prime side specificity for the astacin metalloprotease family reflected by physiological substratesVillin and actin in the mouse kidney brush-border membrane bind to and are degraded by meprins, an interaction that contributes to injury in ischemia-reperfusionStructural basis for the inhibition of M1 family aminopeptidases by the natural product actinonin: Crystal structure in complex with E. coli aminopeptidase N.A soluble form of the Mer receptor tyrosine kinase inhibits macrophage clearance of apoptotic cells and platelet aggregation.Actinonin, a meprin A inhibitor, protects the renal microcirculation during sepsisMeprin 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.The metalloproteases meprin α and meprin β: unique enzymes in inflammation, neurodegeneration, cancer and fibrosis.Hepatocyte nuclear factor 4alpha in the intestinal epithelial cells protects against inflammatory bowel diseaseMeprin A metalloproteinase and its role in acute kidney injury.The bone morphogenetic protein 1/Tolloid-like metalloproteinasesProinterleukin-18 is activated by meprin beta in vitro and in vivo in intestinal inflammation.Meprin A and meprin alpha generate biologically functional IL-1beta from pro-IL-1betaMeprin A metalloproteases enhance renal damage and bladder inflammation after LPS challenge.Hypoxia Associated Proteolytic Processing of OS-9 by the Metalloproteinase Meprin β.IL-17 expression by breast-cancer-associated macrophages: IL-17 promotes invasiveness of breast cancer cell lines.Metalloproteases meprin α and meprin β are C- and N-procollagen proteinases important for collagen assembly and tensile strengthDisruption of the meprin alpha and beta genes in mice alters homeostasis of monocytes and natural killer cells.Meprin metalloproteases inactivate interleukin 6.Pharmacological targets in the renal peritubular microenvironment: implications for therapy for sepsis-induced acute kidney injury.
P2860
Q24298124-9A8EE5F4-5C79-486C-B733-4E364FA99725Q24646365-C785DA0C-8696-404E-86E2-22B74033F277Q24657607-C79BFD75-E32B-4827-9BC9-F2ABB654E4E9Q26864798-0BAA0785-5295-4DA8-A537-A2E48372F6B7Q27022092-A8CEB9C9-FF22-4DE3-91B3-7ACEDCCF2ACCQ28584210-AAD7ADC8-965D-4EA3-BE77-CAEF38E06130Q30847074-748A362A-08B2-4DC2-B9FC-08A32B3BDD9DQ33334334-1EB36319-D627-42CA-8B60-3949D32673F1Q33338489-D6A5CB68-F7BA-432C-B668-79A64BE66805Q33676656-C39688FD-716F-4480-8C40-63AE28BBA85BQ33685019-1A466B96-3928-428E-B682-08CE487976ADQ33940892-0E44962C-AB4F-4B8F-8146-36FF638B2200Q34077651-87C05CB1-C4E6-4EE1-AB0A-201EECA66E86Q34120082-8A9CF1A7-A4E2-402F-BB36-C4538A204E23Q34386859-1CF62249-6CBA-480F-B042-2BAA902A11D1Q34597685-33952677-EA0B-4584-973A-F814A71E6398Q34653027-29347FDE-128D-4FF6-B234-E251359B2610Q34801085-C3E91904-1FB9-48B2-84FA-BA29B5201DBFQ34978046-76880C9F-EC4A-43F5-9728-947AE59F5C33Q35116223-3FA3CC34-DCF0-4951-8453-EBADE4EFA6EFQ35264713-87CAB673-B5A7-4AC4-8683-586E9AA3A9C9Q35326081-D8C24342-5B82-4882-857F-42F32F47486CQ35571741-948F101A-ED7F-45FA-B8FD-E47ABCD1B775Q35616136-0B87137D-6B3E-45EB-846D-7AA02A9407EBQ35693793-FEEC1FAF-4A98-46CA-A33C-0A62D4C18337Q36156032-EE44DA77-719E-471C-B3AE-C3EB82FD41AFQ36503385-3BE19343-F518-41D4-8956-892E5F650993Q36613779-B2171DE0-3D62-4926-98D2-884FAF0B3450Q36732009-D913AFA4-66EC-4AAD-9F36-04ABFA7C7569Q36836257-2048C6DD-2F62-4856-9EAA-CA0EF2EA8F4DQ36846125-F7AD3303-F51C-49E4-8822-EDE47A6EB817Q36968427-61D16111-9F26-47C9-8B43-1EF01C1C122FQ36985463-52B6403D-9351-4752-8D7A-A9D1CD9E2E52Q37086108-1C4659C9-8F97-4C84-A479-ED417CD52390Q37127955-DDF9CD82-DC96-4288-9B70-2A7CD36605D4Q37131308-7A932F6B-5FFC-4910-BCE5-EE0D59907886Q37143394-018D3500-E08A-4950-88D2-740D4B310E71Q37172385-62D1EE48-0E91-4853-9C93-6B7E1D429720Q37635798-F73EE3D7-7C05-4716-A7DD-5EAEBB6A9DE3Q37978478-8D08790F-A666-4ECF-A709-63C2D7DF9A5F
P2860
Human meprin alpha and beta homo-oligomers: cleavage of basement membrane proteins and sensitivity to metalloprotease inhibitors.
description
2004 nî lūn-bûn
@nan
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
2004年论文
@zh
2004年论文
@zh-cn
name
Human meprin alpha and beta ho ...... to metalloprotease inhibitors.
@en
type
label
Human meprin alpha and beta ho ...... to metalloprotease inhibitors.
@en
prefLabel
Human meprin alpha and beta ho ...... to metalloprotease inhibitors.
@en
P2093
P2860
P356
P1433
P1476
Human meprin alpha and beta ho ...... to metalloprotease inhibitors.
@en
P2093
Christoph Becker
Daniel Lottaz
Danny Köhler
Erwin E Sterchi
Hans-Willi Krell
Irene Yiallouros
Markus-N Kruse
Walter Stöcker
P2860
P304
P356
10.1042/BJ20031163
P407
P577
2004-03-01T00:00:00Z