Distinct populations of basal keratinocytes express stromelysin-1 and stromelysin-2 in chronic wounds.
about
Matrix metalloproteinase induction in fibrosis and fibrotic nodule formation due to silica inhalationEpilysin, a novel human matrix metalloproteinase (MMP-28) expressed in testis and keratinocytes and in response to injuryFunctional characterization of three novel tissue-specific anion exchangers SLC26A7, -A8, and -A9Neutrophil activity in chronic venous leg ulcers--a target for therapy?Stem Cells for Cutaneous Wound HealingMatrix Metalloproteinase-10 (MMP-10) Interaction with Tissue Inhibitors of Metalloproteinases TIMP-1 and TIMP-2: BINDING STUDIES AND CRYSTAL STRUCTUREMatrix Metalloproteinase-10/TIMP-2 Structure and Analyses Define Conserved Core Interactions and Diverse Exosite Interactions in MMP/TIMP ComplexesPro-collagenase-1 (matrix metalloproteinase-1) binds the alpha(2)beta(1) integrin upon release from keratinocytes migrating on type I collagenGelatinase B is involved in the in vitro wound repair of human respiratory epitheliumHuman macrophage metalloelastase. Genomic organization, chromosomal location, gene linkage, and tissue-specific expressionMMP-10/stromelysin-2 promotes invasion of head and neck cancer.Matrix metalloproteinases in repair.The proteolytic environment of chronic wounds.Hydrolyzed eggshell membrane immobilized on phosphorylcholine polymer supplies extracellular matrix environment for human dermal fibroblasts.Transcriptional regulation of stromelysin-1 gene expression is altered during progression of mouse mammary epithelial cells from functionally normal to malignant.Inflammation in nonhealing diabetic wounds: the space-time continuum does matterMatrix metalloproteinases are expressed during ductal and alveolar mammary morphogenesis, and misregulation of stromelysin-1 in transgenic mice induces unscheduled alveolar developmentProteolytic events of wound-healing--coordinated interactions among matrix metalloproteinases (MMPs), integrins, and extracellular matrix molecules.The cellular proliferative phase of the wound repair process.MMP-10 is overexpressed, proteolytically active, and a potential target for therapeutic intervention in human lung carcinomas.Physiology and pathophysiology of matrix metalloproteases.Parallel expression of macrophage metalloelastase (MMP-12) in duodenal and skin lesions of patients with dermatitis herpetiformisCollagenase-3 (MMP-13) is expressed by tumor cells in invasive vulvar squamous cell carcinomas.Collagenase-3 (matrix metalloproteinase-13) expression is induced in oral mucosal epithelium during chronic inflammationDynamics of matrix turnover during pathologic remodeling of the extracellular matrix.Role of matrix metalloproteinases in failure to re-epithelialize after corneal injury.MMP-10 Regulates Collagenolytic Activity of Alternatively Activated Resident MacrophagesTh2 Cytokines Suppress Lipoteichoic Acid-Induced Matrix Metalloproteinase Expression and Keratinocyte Migration in Response to Wounding.The activity of collagenase-1 is required for keratinocyte migration on a type I collagen matrix.Individual matrix metalloproteinases control distinct transcriptional responses in airway epithelial cells infected with Pseudomonas aeruginosa.Control of matrix metalloproteinase catalytic activityMatrix Metalloproteinase 10 Degradomics in Keratinocytes and Epidermal Tissue Identifies Bioactive Substrates With Pleiotropic FunctionsDifferential patterns of stromelysin-2 (MMP-10) and MT1-MMP (MMP-14) expression in epithelial skin cancersUpregulation and differential expression of matrilysin (MMP-7) and metalloelastase (MMP-12) and their inhibitors TIMP-1 and TIMP-3 in Barrett's oesophageal adenocarcinomaKeratinocyte expression of MMP3 enhances differentiation and prevents tumor establishment.Wound fluids: a window into the wound environment?Matrilysin expression and function in airway epithelium.Modulation of intracellular calcium levels inhibits secretion of collagenase 1 by migrating keratinocytes.Biochemical insights into the role of matrix metalloproteinases in regeneration: challenges and recent developments.Activities of the matrix metalloproteinase stromelysin-2 (MMP-10) in matrix degradation and keratinocyte organization in wounded skin
P2860
Q23914259-100FB401-07A6-4AA9-BD8B-8354C3386338Q24290646-350E6C6F-6005-4E49-AF4A-756F4EF86865Q24292271-AFFCDA7C-D6FD-4375-8BCC-8466A3A83B47Q26999022-A242CB25-75E1-471E-BEA7-2171F712C961Q27025609-6C1D4896-E20D-44D6-B041-B90DD5B6C64AQ27678085-79C255C9-CF6A-4055-9099-D87F10499259Q27680082-25405293-B2D9-4A79-8159-E4BD139F781DQ28189768-EF3C88A4-A356-4865-9FCF-CF57A3C7BE7BQ28275280-A37EC61C-4C24-48E7-A268-A40B94B094DAQ28303334-F243C61C-7039-4378-B4DC-FF451EB05DEFQ31036986-FC2BCF01-F98C-4E47-8378-FCDAE6CD0A86Q33815962-1EC3C32B-4304-4C8F-B6FE-82E2D29AFA8FQ33815967-BCE3870F-6F51-42BF-9D86-701BF7B07FA9Q33906757-C4632D87-1816-4A4A-9E38-D8C2E29EEC9BQ34103350-B588473F-CA07-414D-A45C-968A55D0081FQ34326241-88912E94-44B5-4427-B518-1BAD507B4D82Q34452052-BA6E4648-B219-4D35-93F4-295CF5544461Q34632691-A60F10A1-B79A-46FF-B117-7D44B12E59A8Q34794368-0C3EBCCF-AFDA-417F-BCFD-38E59E7CEEF6Q34997415-4005CB5B-E541-40F1-8F9B-C1B1DE593204Q35007715-87D5DB84-1D0B-4679-A30D-8F2A657CE7C3Q35363095-CAE372F3-A247-4AC0-AB99-5CA359BD0C60Q35745256-31A8A26A-F4F0-44EE-BE5D-0502BBC64F51Q35765117-BE1B4C33-BB9D-4A27-B51A-8CE7D13E797FQ35773709-000B5648-5776-4653-BEE7-AA977EC8BC99Q35782239-1FD6BAB8-37CC-48D9-BBF7-D6051DFE11BCQ36054448-60F93C81-CE15-430A-8191-A240AF690E01Q36054535-73818C96-8D08-4E9F-8564-523D948E26B5Q36254748-CD7BAA77-E770-47F2-9281-D6E80E9AD065Q36313986-5D05B598-B5A6-43A0-9B6F-219DF5190CF3Q36465038-5AB3DDB1-6673-42C6-8D9F-1BFB6CC5FC78Q36604413-8BF13E87-7958-472E-9DEF-B407AC38AA6CQ36622753-1C2AEBCE-960C-47EA-811B-E2EC04717B7EQ36623544-8843FE8F-E511-4E94-9101-4A2318548F78Q36943114-93E27EF1-4242-4B94-A7BC-274D6F6F7D0BQ37019696-5FE6AE30-21B6-4F62-A2FC-BBE2ECBE3551Q37385157-31CE8B09-4451-47D6-B39D-4F73762E504FQ37385964-6985321D-BCC6-46DF-AC4D-DBE80F89D451Q37477458-B0213EC4-4C20-42AE-A8B1-F332D3DB24CCQ37657212-A84290A1-6718-440A-A1C8-7FB0342BAADA
P2860
Distinct populations of basal keratinocytes express stromelysin-1 and stromelysin-2 in chronic wounds.
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
Distinct populations of basal ...... romelysin-2 in chronic wounds.
@ast
Distinct populations of basal ...... romelysin-2 in chronic wounds.
@en
Distinct populations of basal ...... romelysin-2 in chronic wounds.
@nl
type
label
Distinct populations of basal ...... romelysin-2 in chronic wounds.
@ast
Distinct populations of basal ...... romelysin-2 in chronic wounds.
@en
Distinct populations of basal ...... romelysin-2 in chronic wounds.
@nl
prefLabel
Distinct populations of basal ...... romelysin-2 in chronic wounds.
@ast
Distinct populations of basal ...... romelysin-2 in chronic wounds.
@en
Distinct populations of basal ...... romelysin-2 in chronic wounds.
@nl
P2093
P2860
P356
P1476
Distinct populations of basal ...... romelysin-2 in chronic wounds.
@en
P2093
A P Pentland
H Birkedal-Hansen
H G Welgus
U K Saarialho-Kere
P2860
P356
10.1172/JCI117351
P407
P577
1994-07-01T00:00:00Z