Results 11 to 20 of about 25,778,187 (334)

The Homology Modeling and Docking Investigation of Human Cathepsin B [PDF]

open access: yesInternational Journal of Medical Toxicology and Forensic Medicine, 2020
Background: Cathepsin B comprises a group of lysosomal cysteine proteases belonging to the Papain family; it has an intracellular function in the process of protein catabolism, antigen processing in the immune response, and Alzheimer’s disease.
Afshin Khara   +2 more
doaj   +3 more sources

Cathepsin B gene disruption induced Leishmania donovani proteome remodeling implies cathepsin B role in secretome regulation. [PDF]

open access: yesPLoS ONE, 2013
Leishmania cysteine proteases are potential vaccine candidates and drug targets. To study the role of cathepsin B cysteine protease, we have generated and characterized cathepsin B null mutant L. donovani parasites. L.
Teklu Kuru Gerbaba, Lashitew Gedamu
doaj   +2 more sources

Cathepsin B promotes collagen biosynthesis, which drives bronchiolitis obliterans syndrome

open access: yesEuropean Respiratory Journal, 2020
Bronchiolitis obliterans syndrome (BOS) is a major complication after lung transplantation (LTx). BOS is characterised by massive peribronchial fibrosis, leading to air trapping-induced pulmonary dysfunction.
C. Morrone   +9 more
semanticscholar   +2 more sources

CTSB (cathepsin B) [PDF]

open access: yesAtlas of Genetics and Cytogenetics in Oncology and Haematology, 2011
Review on CTSB (cathepsin B), with data on DNA, on the protein encoded, and where the gene is implicated.
Jevnikar, Z, Kos, J
openaire   +4 more sources

Exploring the Association between Cathepsin B and Parkinson’s Disease [PDF]

open access: yesBrain Sciences
Objective: The aim of this study is to investigate the association between Cathepsin B and Parkinson’s Disease (PD), with a particular focus on determining the role of N-acetylaspartate as a potential mediator.
Changhao Lu   +9 more
doaj   +2 more sources

Cathepsin B in programmed cell death machinery: mechanisms of execution and regulatory pathways

open access: yesCell Death and Disease, 2023
Cathepsin B (CatB), a cysteine protease, is primarily localized within subcellular endosomal and lysosomal compartments. It is involved in the turnover of intracellular and extracellular proteins.
Zhen Xie   +10 more
semanticscholar   +1 more source

Smart Delivery Systems Responsive to Cathepsin B Activity for Cancer Treatment

open access: yesPharmaceutics, 2023
Cathepsin B is a lysosomal cysteine protease, contributing to vital cellular homeostatic processes including protein turnover, macroautophagy of damaged organelles, antigen presentation, and in the extracellular space, it takes part in tissue remodeling,
V. S. Egorova   +5 more
semanticscholar   +1 more source

Molecular Features of CA-074 pH-Dependent Inhibition of Cathepsin B

open access: yesBiochemistry, 2022
CA-074 is a selective inhibitor of cathepsin B, a lysosomal cysteine protease. CA-074 has been utilized in numerous studies to demonstrate the role of this protease in cellular and physiological functions. Cathepsin B in numerous human disease mechanisms
Michael C. Yoon   +6 more
semanticscholar   +1 more source

Trafficking of Full-Length and N-Terminally Truncated Cathepsin B in Human Colorectal Carcinoma Cells

open access: yesApplied Sciences, 2021
Cathepsin B is an endo-lysosomal cysteine protease. However, its increased expression and altered localization to the extracellular space, to mitochondria, or to the nucleus has been linked to tumor progression.
Tripti Tamhane   +7 more
doaj   +1 more source

Selective neutral pH inhibitor of cathepsin B designed based on cleavage preferences at cytosolic and lysosomal pH conditions

open access: yesACS Chemical Biology, 2021
Cathepsin B is a cysteine protease that normally functions within acidic lysosomes for protein degradation, but in numerous human diseases, cathepsin B translocates to the cytosol having neutral pH where the enzyme activates inflammation and cell death ...
Michael C. Yoon   +12 more
semanticscholar   +1 more source

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