Results 201 to 210 of about 57,258 (253)

Isotope Dilution NanoLC-MS/MS Quantitation of Methylglyoxal DNA-Protein Cross-Links: Formation and Repair in Human Cells. [PDF]

Anal Chem
Omondi RO, Barnes EM, Gurajala KC, Fisette G, Chaudray IA, Erber L.   +5 more
europepmc   +1 more source

Technical and biological factors driving inter-individual body burden of arsenic species in murine models of human arsenic exposure. [PDF]

Toxicol Sci
Wang L, Wang Q, Wolfe TM, Pinkham NV, Erickson R, Yoshinaga M, McDermott TR, Walk ST.   +7 more
europepmc   +1 more source

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Entamoeba histolytica: Cysteine proteinase activity and virulence. Focus on cysteine proteinase 5 expression levels

Experimental Parasitology, 2009
Cysteine proteinase (CP) activity and CP5 mRNA levels were analyzed in eleven samples of Entamoeba histolytica isolated from patients presenting different clinical profiles. The virulence degree of the isolates, determined in hamster liver, correlated well with the clinical form of the patient and culture conditions.
E F Silva, Jorge L Pesquero
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Cysteine proteinases and metastasis

CANCER AND METASTASIS REVIEW, 1984
Cysteine proteinases are a subclass of endopeptidases which require activation by thiol reagents. A tumor cysteine proteinase which appears to be related to lysosomal cathepsin B has been implicated in the ability of tumor cells to invade the extracellular matrix and to metastasize to secondary sites.
B F, Sloane, K V, Honn
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Cysteine proteinases in chondrosarcomas

Matrix Biology, 2001
The aim of the present study was to define the role of cathepsins B, H, K, L and S in the pathogenesis of human chondrosarcomas. For this purpose 40 tumour samples obtained from 12 patients with the diagnosis of conventional chondrosarcoma were systematically investigated for the expression of cathepsin mRNAs by Northern hybridisation, and for ...
M, Söderström, T, Ekfors, T, Böhling, A, Aho, H T, Aro, E, Vuorio   +5 more
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Novel Cysteine Proteinase Inhibitors Homologous to the Proregions of Cysteine Proteinases

Current Protein & Peptide Science, 2002
Propeptides of papain-like cysteine proteinases such as papain, cathepsins B, L and S are potent inhibitors of their cognate cysteine proteinases with Ki values in the nanomolar range, and they exhibit highest inhibition selectivity for enzymes from which they originate. Recent studies have identified novel inhibitor proteins that are homologous to the
Y, Yamamoto, M, Kurata, S, Watabe, R, Murakami, S Y, Takahashi   +4 more
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Cysteine proteinases of parasitic protozoa

Parasitology Today, 1990
Proteinases are involved with many processes in living organisms. In recent years, there has been increasing interest in elucidating the functions the enzymes perform in parasites. These studies have revealed that one class of proteinases, the cysteine proteinases, predominates in many parasitic protozoa.
M J, North, J C, Mottram, G H, Coombs
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Autodegradation of lysosomal cysteine proteinases

Biochemical and Biophysical Research Communications, 1987
Repeated injections of Ep-475, a potent cysteine proteinase inhibitor, into rats caused several-fold increase in the hepatic contents of the lysosomal cysteine proteinases cathepsin B, H and L and in the activities of other lysosomal hydrolases. The rates of degradation of these lysosomal enzymes, estimated by repeated injections of cycloheximide, were
E, Kominami, T, Tsukahara, Y, Bando, N, Katunuma   +3 more
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Parasite cysteine proteinases

Perspectives in Drug Discovery and Design, 1996
Cysteine proteinases of protozoan and helminth parasites are considered to have a high potential as targets for novel antiparasite agents. This has stimulated research on the enzymes and a large body of data has now been accumulated. This Perspective provides an overview of the current situation, with recent advances being highlighted.
Colin D. Robertson, Graham H. Coombs, Michael J. North, Jeremy C. Mottram   +3 more
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