Cathepsin B and its endogenous inhibitors: the role in tumor malignancy.
about
Cystatin C: a new renal marker and its potential use in small animal medicineVASP-E: specificity annotation with a volumetric analysis of electrostatic isopotentials.Cathepsin B acts as a dominant execution protease in tumor cell apoptosis induced by tumor necrosis factor.Decreased metastatic spread in mice homozygous for a null allele of the cystatin C protease inhibitor genePurification and characterisation of an inhibitor of a cathepsin B-like proteinase from sunflower seed.Cystatin E/M suppresses legumain activity and invasion of human melanomaCathepsins B, L and cystatin C in cyst fluid of ovarian tumors.Cysteine proteinases and the pathogenesis of amebiasis.Reduction of metastasis using a non-volatile buffer.Specific and efficient peptide substrates for assaying the proteolytic activity of prostate-specific antigen.Acidity generated by the tumor microenvironment drives local invasionBioShuttle mobility in living cells studied with high-resolution FCS & CLSM methodologiesCysteine proteinases mediate extracellular prohormone processing in the thyroid.Pericellular mobilization of the tissue-destructive cysteine proteinases, cathepsins B, L, and S, by human monocyte-derived macrophages.Crystal structure of human cystatin D, a cysteine peptidase inhibitor with restricted inhibition profile.Evaluating methods for modeling epistasis networks with application to head and neck cancer.Metabolism and its sequelae in cancer evolution and therapy.Cathepsin B and other proteases in human colorectal carcinoma.Microenvironmental and cellular consequences of altered blood flow in tumours.Relationship between cathepsin D, urokinase, and plasminogen activator inhibitors in malignant vs benign breast tumours.A novel amplicon at 8p22-23 results in overexpression of cathepsin B in esophageal adenocarcinoma.Recent insights into the cell biology of thyroid angiofollicular units.The role of cellular proteases and their inhibitors in invasion and metastasis. Introductionary overview.Cathepsin B: multiple roles in cancer.Real-time monitoring of drug release.Regulation of proteolytic activity in tissues.Extracellular acidification alters lysosomal trafficking in human breast cancer cells.Mosquito cathepsin B-like protease involved in embryonic degradation of vitellin is produced as a latent extraovarian precursor.Differential localization of cysteine protease inhibitors and a target cysteine protease, cathepsin B, by immuno-confocal microscopy.Degradation of extracellular-matrix proteins by human cathepsin B from normal and tumour tissues.Human tumour cathepsin B. Comparison with normal liver cathepsin B.Quantitative study of the binding of cysteine proteinases to basement membranes.Demonstration of cathepsins B, H and L in xenografts of normal and Duchenne-muscular-dystrophy muscles transplanted into nude mice.Influence of cathepsin D expression in lung adenocarcinoma on prognosis: possible importance of its expression in tumor cells and stromal cells, and its intracellular polarization in tumor cells.Plasma membrane association of cathepsin B in human prostate cancer: biochemical and immunogold electron microscopic analysis.Functional expression of recombinant human stefin A in mammalian and bacterial cells.Ratio of cathepsin B to stefin A identifies heterogeneity within Gleason histologic scores for human prostate cancer.Multifunctional anti-angiogenic activity of the cyclic peroxide ANO-2 with antitumor activity.Expression of high molecular weight cysteine proteinase inhibitor in ovarian cancer tissues: regulation of cathepsin B expression by placental CPI.Lactic Acid: No Longer an Inert and End-Product of Glycolysis.
P2860
Q27010861-D9035386-2614-4D36-B321-21C4D7EFB16FQ30366195-001E3E3F-2C24-4219-B9DC-6E2A10A35435Q30481000-94726205-0EA5-40A0-86CB-C5F46A402F50Q30854542-363C20C7-F2AD-4B1C-9EBA-32AB2CF8036AQ33261230-FF294A6C-A694-4F4D-8607-5D7919B2A412Q33523914-D8555B48-8DF8-4134-9F08-3E0723060AE5Q33739577-61BC71B5-3C88-4740-B59D-2B01FDBA3EA3Q33886180-71C81C21-0C4D-4595-B76E-9B0AE48C593CQ34000971-86C11FE0-2BAD-4127-8CD6-B1D4A4BC4F26Q34013817-49BEE010-3433-4FA4-B2D3-B5403E22A614Q34320819-A7F2A020-2B93-4DCB-B4A6-0AB736582D3EQ34343478-84F5EDFA-D6EA-4400-BB01-EB3C30C4BDE7Q34343802-EBA59B62-866D-429C-B016-939804D58E13Q34385281-F5C581F3-624C-4C03-AC0C-33DE1DFEC7D1Q34397220-2FB1539A-F8A6-4BC9-97D3-F2F217B9D739Q35093840-60392CFD-B443-4B15-B5F0-7C5BF437628CQ35657799-0C5052D0-CCE2-41B4-81CB-2F09330F8D00Q35833965-249FDE69-4B51-47D6-BA9C-4E3344264985Q35904989-55B9DAA3-DAEC-452A-B273-02FD08A10C4DQ35993235-02E7F427-3FEA-44F1-AEB1-2E9ED54B26FBQ36524591-C8E2073E-B13E-491A-9EFC-2D2CC0BF934DQ36724051-2D9422B0-AE90-4110-9A89-F1948B4BAE6BQ37802608-2C6FD46F-1668-4CD7-8659-84420D92C5B4Q38200056-B9B63FFC-4728-4E85-8BFE-5DAA91263326Q39753844-DBAF264D-99BD-401F-A6A0-C972432230E4Q40575091-22E6995D-7C19-40ED-B719-7FEAC89F5132Q40589703-6027C810-3F04-4B77-A934-D83BDD3318C9Q40639725-BB74F269-6925-4B7C-948D-420556C5E5F2Q41032656-144E88BA-BBFB-4054-9A8D-F6203F1745A4Q41849893-C594D281-799A-4906-896C-DC96CD46D207Q41861833-C306A5B5-BB3A-4BC7-8BEA-67CD55EC7E77Q41877708-395F4EF8-8294-490F-8024-8412B5EA87CFQ42161387-1C223F04-7831-497B-B01E-ABAA8EA4A35BQ42439378-9CB0AAEA-7896-415C-974B-87D214D44BF4Q42514298-2C81628D-B6B6-429F-8289-AFF3282D20F3Q42745469-D4F7937E-17B7-4A94-9DFF-690A605E397FQ43728397-F4E716E3-8F7A-46E6-98E7-FAE2AB852DDFQ44062574-437F6838-7987-41F0-A010-7C544DFD39E6Q44573925-C4204D02-68BB-45BB-AA81-7C8131CAECE0Q50095883-0141E4F5-6757-40CC-B020-F3B8DD7B0F0B
P2860
Cathepsin B and its endogenous inhibitors: the role in tumor malignancy.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on December 1990
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Cathepsin B and its endogenous inhibitors: the role in tumor malignancy.
@en
Cathepsin B and its endogenous inhibitors: the role in tumor malignancy.
@nl
type
label
Cathepsin B and its endogenous inhibitors: the role in tumor malignancy.
@en
Cathepsin B and its endogenous inhibitors: the role in tumor malignancy.
@nl
prefLabel
Cathepsin B and its endogenous inhibitors: the role in tumor malignancy.
@en
Cathepsin B and its endogenous inhibitors: the role in tumor malignancy.
@nl
P2093
P356
P1476
Cathepsin B and its endogenous inhibitors: the role in tumor malignancy.
@en
P2093
P2860
P2888
P304
P356
10.1007/BF00049523
P577
1990-12-01T00:00:00Z