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Optimizing dentin bond durability: control of collagen degradation by matrix metalloproteinases and cysteine cathepsinsAutocatalytic processing of recombinant human procathepsin L. Contribution of both intermolecular and unimolecular events in the processing of procathepsin L in vitroCD2AP in mouse and human podocytes controls a proteolytic program that regulates cytoskeletal structure and cellular survivalCysteine peptidases of mammals: their biological roles and potential effects in the oral cavity and other tissues in health and disease.Processing and activation of lysosomal proteinases.Proteolytic processing of dynamin by cytoplasmic cathepsin L is a mechanism for proteinuric kidney disease.Cathepsin L acutely alters microvessel integrity within the neurovascular unit during focal cerebral ischemia.Podocyte migration during nephrotic syndrome requires a coordinated interplay between cathepsin L and alpha3 integrin.Chondroitin sulfate proteoglycan is a potent enhancer in the processing of procathepsin L.The lysosomal protease cathepsin L is an important regulator of keratinocyte and melanocyte differentiation during hair follicle morphogenesis and cycling.Characterization of downstream Ras signals that induce alternative protease-dependent invasive phenotypes.Procongopain from Trypanosoma congolense is processed at basic pH: an unusual feature among cathepsin L-like cysteine proteases.Cathepsin L1, the major protease involved in liver fluke (Fasciola hepatica) virulence: propetide cleavage sites and autoactivation of the zymogen secreted from gastrodermal cells.Maturation of human tripeptidyl-peptidase I in vitro.Recombinant human procathepsin S is capable of autocatalytic processing at neutral pH in the presence of glycosaminoglycans.The major secreted cathepsin L1 protease of the liver fluke, Fasciola hepatica: a Leu-12 to Pro-12 replacement in the nonconserved C-terminal region of the prosegment prevents complete enzyme autoactivation and allows definition of the molecular eveProduction and processing of a recombinant Fasciola hepatica cathepsin B-like enzyme (FhcatB1) reveals potential processing mechanisms in the parasite.
P2860
Q26866319-CB86D128-2269-4674-9EC1-1CA70C428C82Q28262233-35F3510B-B1AF-4F02-BDAB-2EA34D260763Q28572534-D538E52B-DF73-4014-A132-498C4B8F0862Q34713891-CA1E881B-2872-4B94-A27D-555B1BA62F84Q35055169-57BD5748-03E8-4E26-A583-1C755982C0B4Q35916157-9077FC50-6064-442B-B42F-617681DF1101Q36254387-2C373D48-2CDC-4D56-9BF4-CD9606172CDBQ40545315-D9585F3F-A749-464F-9E07-2CFA7CE7C79FQ40674508-1EB87791-D894-4F92-9A23-0A32DA436397Q42048079-F1338D04-47DF-4C37-B236-13D01F3A4E3BQ42529175-65816920-024F-4B91-AC23-0EE25A588558Q44529757-E828D78B-85DD-4BB7-A49D-267490A5445BQ44750364-57C34F58-43FA-419B-ADE4-D00F5F25654BQ44895882-1C1F7746-F6B5-4A82-A3CB-38459CD0C169Q45264641-94619729-2E0C-47B6-AD1F-1F06DC9F8111Q53562093-9AE9C20A-80B0-4C40-8AD6-6CAAF2B9C4ABQ53606525-1EC70B9B-1F6E-4F3F-B941-4D3672C06BAB
P2860
description
1994 nî lūn-bûn
@nan
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
1994年论文
@zh
1994年论文
@zh-cn
name
Multi-step processing of procathepsin L in vitro.
@en
type
label
Multi-step processing of procathepsin L in vitro.
@en
prefLabel
Multi-step processing of procathepsin L in vitro.
@en
P2860
P1433
P1476
Multi-step processing of procathepsin L in vitro.
@en
P2093
P2860
P304
P356
10.1016/0014-5793(94)00924-4
P407
P577
1994-10-01T00:00:00Z