Results 331 to 340 of about 13,268,265 (360)
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IMMUNOHISTOCHEMICAL STUDY ON CATHEPSIN-B AND CATHEPSIN-D IN PANCREATIC-CANCER

Oncology Reports, 1994
Lysosomal enzymes, cathepsin B and D, have been studied in their possible relationship to the ability of malignant cells to invade and metastasize. In the current investigation, these cathepsins were detected immunohistochemically using avidin-biotin-peroxidase complex method in the pancreatic cancer cells of 21 patients.
M Sowa   +8 more
openaire   +3 more sources

Cathepsin B-like cysteine proteinase activity in sputum and immunohistologic identification of cathepsin B in alveolar macrophages.

American Review of Respiratory Disease, 2015
Cathepsin B-like cysteine proteinase activity was measured, using a fluorimetric assay, in sputum samples from 27 subjects with chronic obstructive airways disease. Thirteen of the subjects had a current acute respiratory infection.
D. Burnett, J. Crocker, R. Stockley
semanticscholar   +1 more source

Structural requirements for cathepsin B and cathepsin H inhibition by kininogens

Journal of Protein Chemistry, 1996
Domain 3 (D3) of human kininogens, the major cysteine proteinase inhibitors in plasma, has been shown to be the tightest binding inhibitory domain for cathepsins B and H. D3 was expressed in three fragments as its exon products as follows: exon 7 (Gly235-Gln292), exon 8 (Gln292-Gly328), and exon 9 (Gln329-Met357).
Bilqees Bano   +4 more
openaire   +3 more sources

The current stage of cathepsin B inhibitors as potential anticancer agents.

Future Medicinal Chemistry, 2014
Cathepsin B is a lysosomal cysteine peptidase, with an important role in the development and progression of cancer. It is involved in the degradation of extracellular matrix proteins, a process promoting invasion and metastasis of tumor cells and tumor ...
J. Kos, A. Mitrović, Bojana Mirković
semanticscholar   +1 more source

The action of cathepsin B and collagenolytic cathepsin in the degradation of collagen

1977
Cathepsin B and collagenolytic cathepsin were obtained from bovine spleen and human placenta and identified as thiol proteinases. Both enzymes degraded insoluble fibrous collagen maximally at pH 3.5 and soluble monomeric collagen near pH 4.5. The response to activators and inhibitors was similar for both enzymes.
D J, Etherington, P J, Evans
openaire   +2 more sources

Clinical significance of cathepsin L and cathepsin B in dilated cardiomyopathy

Molecular and Cellular Biochemistry, 2017
Dysregulated expression of lysosomal cysteine cathepsins is associated with adverse cardiac remodeling, a characteristic of several cardiovascular diseases. However, the information regarding the role of cysteine cathepsin L (CTSL) and cathepsin B (CTSB) in dilated cardiomyopathy (DCM) is limited.
Dharamvir Singh Arya   +9 more
openaire   +3 more sources

Tumor Cell Membrane Cathepsin B

bchm, 1998
The lysosomal cysteine peptidase cathepsin B was found to be associated with plasma membrane/endosomal fractions of murine B16 amelanotic melanoma cells. Confocal microscopy with three dimensional image analysis indicated that cathepsin B was associated with the external basal cell surface, which would be consistent with its proposed role in ...
Jennifer E. Koblinski   +4 more
openaire   +3 more sources

Cathepsins D and B in breast cancer [PDF]

open access: possible, 1996
The name cathepsin is derived from a Greek word meaning to digest and was used originally for acidic proteases, with the letters designating individual enzymes [1,2]. Examples of cathepsins are found in three classes of proteases, for example, cathepsin D is an aspartic protease, cathepsin B a cysteine protease, and cathepsin G is a serine protease ...
Bonnie F. Sloane, Wei-Ping Ren
openaire   +2 more sources

Prodrug-inspired probes selective to cathepsin B over other cysteine cathepsins.

Journal of Medicinal Chemistry, 2014
Cathepsin B (CTB) is a cysteine protease believed to be an important therapeutic target or biomarker for several diseases including aggressive cancer, arthritis, and parasitic infections.
M. Chowdhury   +6 more
semanticscholar   +1 more source

Entamoeba histolytica: Purification of cathepsin B

Experimental Parasitology, 1985
A cytotoxic cysteine proteinase with a molecular weight of 16,000 was isolated from axenically grown trophozoites of Entamoeba histolytica. The enzyme was purified from frozen-thawed strain HM-1 by ion-exchange chromatography on DEAE-cellulose, organomercurial agarose affinity chromatography, and size-exclusion chromatography.
Ann F. Hofbauer   +5 more
openaire   +3 more sources

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