Processing of procollagen III by meprins: new players in extracellular matrix assembly?
about
Meprins process matrix metalloproteinase-9 (MMP-9)/gelatinase B and enhance the activation kinetics by MMP-3Extended interaction network of procollagen C-proteinase enhancer-1 in the extracellular matrixStructural basis for the sheddase function of human meprin metalloproteinase at the plasma membraneADAM10 is the major sheddase responsible for the release of membrane-associated meprin A.Spinning gland transcriptomics from two main clades of spiders (order: Araneae)--insights on their molecular, anatomical and behavioral evolutionMicrobial-induced meprin β cleavage in MUC2 mucin and a functional CFTR channel are required to release anchored small intestinal mucus.Renal proteome in mice with different susceptibilities to fluorosis.Development of high throughput screening assays and pilot screen for inhibitors of metalloproteases meprin α and β.Metalloprotease meprin beta generates nontoxic N-terminal amyloid precursor protein fragments in vivo.Proteomic analyses reveal an acidic prime side specificity for the astacin metalloprotease family reflected by physiological substratesMetalloproteinases in Drosophila to humans that are central players in developmental processes.Origin and Diversification of Meprin Proteases.Production and crystallization of the C-propeptide trimer from human procollagen III.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.Post-transcriptional regulation of meprin α by the RNA-binding proteins Hu antigen R (HuR) and tristetraprolin (TTP)Meprin A metalloproteinase and its role in acute kidney injury.Metalloproteases meprin α and meprin β are C- and N-procollagen proteinases important for collagen assembly and tensile strengthMapping orphan proteases by proteomics: meprin metalloproteases deciphered as potential therapeutic targets.Matrix metalloproteinase collagenolysis in health and disease.Meprin β contributes to collagen deposition in lung fibrosis.The Metalloprotease Meprin β Is an Alternative β-Secretase of APP.The collαgen III fibril has a "flexi-rod" structure of flexible sequences interspersed with rigid bioactive domains including two with hemostatic roles.MEP1A contributes to tumor progression and predicts poor clinical outcome in human hepatocellular carcinoma.Meprin Metalloprotease Deficiency Associated with Higher Mortality Rates and More Severe Diabetic Kidney Injury in Mice with STZ-Induced Type 1 Diabetes.Determination of cleavage site of Reelin between its sixth and seventh repeat and contribution of meprin metalloproteases to the cleavage.Sizzled is unique among secreted frizzled-related proteins for its ability to specifically inhibit bone morphogenetic protein-1 (BMP-1)/tolloid-like proteinases.The metalloprotease meprin β generates amino terminal-truncated amyloid β peptide species.Heterologous Expression of the Astacin Protease Meprin β in Pichia pastoris.Morpholino knockdown of the ubiquitously expressed transmembrane serine protease TMPRSS4a in zebrafish embryos exhibits severe defects in organogenesis and cell adhesion.Undiagnosed Kidney Injury in Uninsured and Underinsured Diabetic African American Men and Putative Role of Meprin Metalloproteases in Diabetic Nephropathy.
P2860
Q24302283-61B8B8A8-83ED-4E8C-90AC-40D580D79905Q24338239-4DBB4EF9-28E2-41EA-83BA-D41569BB80D4Q27673367-0F782655-4D6B-4B72-8AFF-24C9ADFFDC89Q33676656-575F6440-0D2F-4DEF-A9EE-BEA701870889Q33955192-9B4C7542-39C5-4AD2-A0F9-6361B146CD71Q34120082-926CAAA2-DD06-4ACF-BAA0-DA614357DA99Q34544843-D790D3BE-8DB9-4A4D-A62A-2B47FAE7F0CAQ35116223-6BEFEF95-5B6C-4C5D-A34E-5E96F617ED82Q35145029-6B3EBB51-31C6-464A-BBA9-C2F183810B88Q35264713-59F9CF1D-15FE-4D0B-BFA0-3B194D2AC546Q35604976-9ACB65C4-A362-49B9-96A2-BC589BC82909Q35750369-F1D416FD-E2E8-48D3-AEAB-CF9C08C2B533Q36398682-C9A9EE4B-C4FA-4875-B879-D4DF3D8D0960Q36503385-1B09A8D8-18ED-4549-8210-30A5E9779157Q36613779-F11C5D84-0673-44B0-9F79-6F8FC97669D2Q36620740-CE17CBCF-45A6-46CE-880C-383839E59A46Q36836257-7C92B763-EDAA-46D4-884B-F09BCEAF55D7Q37143394-68B1CAAD-9E43-4CDE-AA38-B2AF2404E02CQ38182526-CCC9E9C9-0AD4-4988-BBB3-2164CAF6FE8DQ38431602-4930CE65-F2F6-4D4C-897D-5B90B05B3895Q39036654-C0492815-4536-4719-A9A5-C2332FC6E9BEQ39095782-4E23F391-8D6D-442F-91E6-FCDB361C0DD6Q41006430-B7743F37-2679-4596-A169-2CD8DC11E37EQ41056161-CBADA241-5254-47AF-8A4A-52C90BAB1F69Q41215950-1B4AD6ED-F2AB-4A29-A840-B7070143F2E9Q42484080-228A7C90-B8FC-41A5-B9D4-F763E4F1C900Q42532115-547D3E0F-A185-4B6D-AEAB-FD670FA89081Q42565677-C22B05F1-97A2-4B1E-9851-9366220B02CDQ51097578-0EB77CFD-FD08-46CB-A4A3-2DA66D26FA44Q51864651-8E89B087-F77C-41D7-8541-38168FF41609Q55006125-98A39304-0553-4053-9ADF-95E451452891
P2860
Processing of procollagen III by meprins: new players in extracellular matrix assembly?
description
2010 nî lūn-bûn
@nan
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
2010年论文
@zh
2010年论文
@zh-cn
name
Processing of procollagen III by meprins: new players in extracellular matrix assembly?
@en
Processing of procollagen III by meprins: new players in extracellular matrix assembly?
@nl
type
label
Processing of procollagen III by meprins: new players in extracellular matrix assembly?
@en
Processing of procollagen III by meprins: new players in extracellular matrix assembly?
@nl
prefLabel
Processing of procollagen III by meprins: new players in extracellular matrix assembly?
@en
Processing of procollagen III by meprins: new players in extracellular matrix assembly?
@nl
P2093
P50
P356
P1476
Processing of procollagen III by meprins: new players in extracellular matrix assembly?
@en
P2093
Bernd C Bruns
Catherine Moali
Christoph Becker-Pauly
Daniel Kronenberg
David J S Hulmes
Erwin E Sterchi
Heiko Traupe
Markus Böhm
Walter Stöcker
P2888
P304
P356
10.1038/JID.2010.202
P407
P577
2010-07-15T00:00:00Z
P6179
1013203901