about
Cleavage of nidogen-1 by cathepsin S impairs its binding to basement membrane partnersStructure-Activity Analysis of Cathepsin K/Chondroitin 4-Sulfate InteractionsThe Unusual Resistance of Avian Defensin AvBD7 to Proteolytic Enzymes Preserves Its Antibacterial ActivitySubstrate profiling of cysteine proteases using a combinatorial peptide library identifies functionally unique specificities.Human cysteine cathepsins are not reliable markers of infection by Pseudomonas aeruginosa in cystic fibrosis.Aminopeptidase N1 (EtAPN1), an M1 metalloprotease of the apicomplexan parasite Eimeria tenella, participates in parasite development.Congopain from Trypanosoma congolense: drug target and vaccine candidate.Eimeripain, a cathepsin B-like cysteine protease, expressed throughout sporulation of the apicomplexan parasite Eimeria tenella.Human and parasitic papain-like cysteine proteases: their role in physiology and pathology and recent developments in inhibitor design.The role of basic amino acid surface clusters on the collagenase activity of cathepsin KCysteine cathepsins and caspases in silicosis.Lung cysteine cathepsins: intruders or unorthodox contributors to the kallikrein-kinin system?Voltage-gated Sodium Channel Activity Promotes Cysteine Cathepsin-dependent Invasiveness and Colony Growth of Human Cancer Cells.Cysteine cathepsins and cystatins: from ancillary tasks to prominent status in lung diseases.Antimicrobial proteins and peptides in human lung diseases: A friend and foe partnership with host proteases.Active site labeling of cysteine cathepsins by a straightforward diazomethylketone probe derived from the N-terminus of human cystatin C.Synthesis of a biologically active triazole-containing analogue of cystatin A through successive peptidomimetic alkyne-azide ligations.Extracellular catalase activity protects cysteine cathepsins from inactivation by hydrogen peroxide.Straightforward synthesis of 2,4,6-trisubstituted 1,3,5-triazine compounds targeting cysteine cathepsins K and S.Antimicrobial Peptide LL-37 Is Both a Substrate of Cathepsins S and K and a Selective Inhibitor of Cathepsin L.Discordance in cathepsin B and cystatin C expressions in bronchoalveolar fluids between murine bleomycin-induced fibrosis and human idiopathic fibrosis.Proteolysis of cystatin C by cathepsin D in the breast cancer microenvironment.Procongopain from Trypanosoma congolense is processed at basic pH: an unusual feature among cathepsin L-like cysteine proteases.Human cystatin C: a new biomarker of idiopathic pulmonary fibrosis?Proteinases participating in the processing and activation of prolegumain in primary cultured rat macrophages.Regulation of cathepsin K activity by hydrogen peroxide.Differential expression of cathepsins K, S and V between young and aged Caucasian women skin epidermis.Inhibition of a cathepsin L-like cysteine protease by a chimeric propeptide-derived inhibitor.Binding of chondroitin 4-sulfate to cathepsin S regulates its enzymatic activity.Specific cleavage of the lung surfactant protein A by human cathepsin S may impair its antibacterial properties.Degradation of apolipoprotein B-100 by lysosomal cysteine cathepsins.Inhibition of trypanosomal cysteine proteinases by their propeptides.Revisiting the S2 specificity of papain by structural analogs of PheCigarette smoke induces overexpression of active human cathepsin S in lungs from current smokers with or without COPDProcessing and Maturation of Cathepsin C Zymogen: A Biochemical and Molecular Modeling AnalysisRegulation of the Proteolytic Activity of Cysteine Cathepsins by Oxidants
P50
Q24298124-D38E0265-4BE9-4631-B165-3A0574305C8EQ27666421-1C991FBD-9353-41F7-AB7B-05932095A068Q28553719-E76518A9-E979-4BFC-8BE4-E2A9AE4A12F2Q33235638-8E172F4E-C1A7-4D9B-B030-ED6D51CE01B8Q34043367-126E20A0-08ED-49F5-8DC1-9E6D72FD0B23Q34057071-52FF48A3-EE72-42E8-B073-E07BF13A7DCCQ34137760-D8F44A4A-32AB-4512-9D04-CD253F67BA38Q34211633-2D690CBE-5DB7-4781-9DE3-0360DBC386A3Q35021901-04BC805B-1080-4B4F-8BED-1381FCB8F719Q35985234-6A1CE732-EF64-43AF-9008-B74BED486EBBQ36567785-280FAFA8-522E-4EAD-9A5B-F4B60490F0EEQ37038006-926AE3E7-B38D-4C56-BCD8-3CDD649A58F9Q37136807-E387BE29-A5E0-488F-B03F-6CE083F4D0B3Q38245344-1B4F0149-DF6F-4463-AF1A-9D528B6CBFFFQ38581088-7289B7E3-9E93-4104-889E-DCD27AFB437FQ38898830-8317EF5E-1CBC-486A-A5BF-0663A33B3649Q39432547-2601C774-88D6-417C-8443-9C5FA433742BQ40002125-EB053067-0DC4-41B5-9FCC-C98A96D655AEQ40740977-5B2DFD81-4B87-486F-B23B-F7FFFAE0B5F5Q41056650-FA46D6EE-7848-41E8-ACC7-788F925F0941Q42391679-6C01EF42-BBAF-4599-B13B-028DC9AF063BQ43609079-5C443E74-9469-49C9-99F2-272E72BDAA17Q44529757-113F2E12-B561-4766-8EFA-19CB43C60243Q44870181-233C7DB9-CAF5-4A57-AFC1-8056C974B976Q44979418-98AF2D8F-8F08-423A-BEA8-D15FBF7942A8Q46268059-332F8FFF-0B02-437F-9DAC-61A2D167E3F7Q46298773-64035C01-E6C7-4851-9E6D-D82AAF3A1DE1Q46629289-A9E2F121-6EBD-4112-8827-61A463ACB0DDQ47724503-D355282A-7A8F-49F8-B640-ED709E5BF80CQ50961462-3B19F7B5-007F-404E-85E1-3CD964A00A35Q53599405-BE388A27-C2A6-428B-BEB2-3644B15AC8A9Q54125170-06D37B0A-9F0F-4F67-9EEC-DC2FEC54761CQ74643772-53431EFE-594A-4022-8DDA-1B6791517CFDQ90279399-961359A4-01FB-497A-8AF2-8FD68992BEF8Q90310495-DBDD7514-D979-4CEA-A591-B3A072A15FA7Q90363169-88C47ECD-3D6A-41F6-98F8-F5150AAF2A7D
P50
description
hulumtues
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Fabien Lecaille
@ast
Fabien Lecaille
@en
Fabien Lecaille
@es
Fabien Lecaille
@nl
Fabien Lecaille
@sl
type
label
Fabien Lecaille
@ast
Fabien Lecaille
@en
Fabien Lecaille
@es
Fabien Lecaille
@nl
Fabien Lecaille
@sl
prefLabel
Fabien Lecaille
@ast
Fabien Lecaille
@en
Fabien Lecaille
@es
Fabien Lecaille
@nl
Fabien Lecaille
@sl
P106
P108
P21
P31
P496
0000-0003-1060-4222