catechin and leupeptins

catechin has been researched along with leupeptins in 6 studies

Research

Studies (6)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's0 (0.00)29.6817
2010's6 (100.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Bartolini, G; Farabegoli, F; Orlandi, M; Ostan, R; Papi, A1
Chen, SC; Chiang, CK; Chuang, YT; Huang, KH; Kuo, KL; Liu, SH; Pu, YS; Tsai, YC; Weng, TI1
Bettuzzi, S; Bonacini, M; Giovanna Troglio, M; Modernelli, A; Naponelli, V; Ramazzina, I; Rizzi, F1
Choi, SJ; Heo, CH; Kim, HM; Kim, HS; Moon, JY1
Chen, M; Gan, L; Li, L; Liu, B; Liu, L; Shan, Z; Xiao, C; Xu, T; Yao, S; Zhao, Y; Zhong, L1
Dong, L; Fan, J; Fan, X; Gong, Y; Jiang, X; Jin, P; Li, L; Mao, S; Quan, Y; Wang, S; Wang, Y; Zhang, T1

Other Studies

6 other study(ies) available for catechin and leupeptins

ArticleYear
(-)-Epigallocatechin-3-gallate downregulates Pg-P and BCRP in a tamoxifen resistant MCF-7 cell line.
    Phytomedicine : international journal of phytotherapy and phytopharmacology, 2010, Volume: 17, Issue:5

    Topics: Antineoplastic Agents, Phytogenic; Apoptosis; ATP Binding Cassette Transporter, Subfamily B, Member 1; ATP Binding Cassette Transporter, Subfamily G, Member 2; ATP-Binding Cassette Transporters; bcl-2-Associated X Protein; Breast Neoplasms; Camellia sinensis; Catechin; Cell Line, Tumor; Cell Proliferation; Dose-Response Relationship, Drug; Down-Regulation; Drug Resistance, Neoplasm; Gene Expression; Humans; Leupeptins; Mitoxantrone; Multidrug Resistance-Associated Proteins; Neoplasm Proteins; Plant Extracts; Protease Inhibitors; Proto-Oncogene Proteins c-bcl-2; RNA, Messenger; Tamoxifen

2010
Down-regulation of glucose-regulated protein (GRP) 78 potentiates cytotoxic effect of celecoxib in human urothelial carcinoma cells.
    PloS one, 2012, Volume: 7, Issue:3

    Topics: Apoptosis; Catechin; Celecoxib; Cell Line, Tumor; Cell Survival; Cyclooxygenase 2 Inhibitors; Down-Regulation; Drug Synergism; Endoplasmic Reticulum; Endoplasmic Reticulum Chaperone BiP; G1 Phase Cell Cycle Checkpoints; Heat-Shock Proteins; Humans; Indoles; Leupeptins; Pyrazoles; RNA, Small Interfering; Stress, Physiological; Sulfonamides; Unfolded Protein Response; Urinary Bladder Neoplasms

2012
EGCG antagonizes Bortezomib cytotoxicity in prostate cancer cells by an autophagic mechanism.
    Scientific reports, 2015, Oct-16, Volume: 5

    Topics: Antineoplastic Agents; Autophagy; Bortezomib; Catechin; Cell Line, Tumor; Endoplasmic Reticulum Stress; Eukaryotic Initiation Factor-2; Humans; Leupeptins; Male; Microtubule-Associated Proteins; Prostatic Neoplasms; Proteasome Inhibitors; Transcription Factor CHOP; Up-Regulation

2015
α-Syntrophin stabilizes catalase to reduce endogenous reactive oxygen species levels during myoblast differentiation.
    The FEBS journal, 2017, Volume: 284, Issue:13

    Topics: Aldehydes; Animals; Antioxidants; Blotting, Western; Calcium-Binding Proteins; Catalase; Catechin; Cell Differentiation; Cell Line; Cysteine Proteinase Inhibitors; Leupeptins; Membrane Proteins; Mice; Microscopy, Fluorescence, Multiphoton; Muscle Development; Muscle Proteins; Myoblasts; Oxidative Stress; Protein Stability; Reactive Oxygen Species; Reverse Transcriptase Polymerase Chain Reaction; RNA Interference

2017
Epigallocatechin-3-gallate promotes all-trans retinoic acid-induced maturation of acute promyelocytic leukemia cells via PTEN.
    International journal of oncology, 2017, Volume: 51, Issue:3

    Topics: Catechin; Cell Differentiation; Chromones; Drug Resistance, Neoplasm; Gene Expression Regulation, Neoplastic; HL-60 Cells; Humans; Leukemia, Promyelocytic, Acute; Leupeptins; Morpholines; Phenanthrenes; Promyelocytic Leukemia Protein; Proteolysis; PTEN Phosphohydrolase; Retinoic Acid Receptor alpha; Tretinoin

2017
Epigallocatechin-3-gallate (EGCG) inhibits aggregation of pulmonary fibrosis associated mutant surfactant protein A2 via a proteasomal degradation pathway.
    The international journal of biochemistry & cell biology, 2019, Volume: 116

    Topics: Animals; Butylamines; Catechin; CHO Cells; Cricetulus; Cysteine Proteinase Inhibitors; Detergents; Gene Expression; Leupeptins; Mutation; Octoxynol; Proteasome Endopeptidase Complex; Protein Aggregates; Protein Stability; Proteolysis; Pulmonary Fibrosis; Pulmonary Surfactant-Associated Protein A; Recombinant Proteins; Solubility

2019