Results 231 to 240 of about 190,299 (260)
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SEP-1 - a subtilisin-like serine endopeptidase from germinated seeds of Hordeum vulgare L. cv. Morex

Planta, 2002
Proteolysis is crucial for all living cells. It regulates protein processing, intracellular protein levels and removes abnormal or damaged proteins from the cell, working as a cellular housekeeper. By means of proteolysis, cells can control the short-lived regulatory proteins that affect processes such as signal transduction and reception ...
FONTANINI, DEBORA, Jones B.L.
openaire   +2 more sources

Metabolic Effects of Cellular Necrosis Caused by Exfoliative Toxin C (ExhC) from

Journal of Proteome Research
Exfoliative toxins (ETs) are glutamyl endopeptidases (GEPs) belonging to the chymotrypsin-like serine protease family (CLSPs), and they play crucial roles in diverse skin diseases.
Carolina Gismene   +10 more
semanticscholar   +1 more source

Purification and characterization of an alkaline serine endopeptidase from a feather-degradingXanthomonas maltophiliastrain

Canadian Journal of Microbiology, 2002
A keratinolytic Xanthomonas maltophilia strain (POA-1), cultured on feather meal broth, using keratin as its sole source of carbon and nitrogen, secretes several extracellular peptidases. The major serine peptidase was purified to homogeneity by a five-step procedure. Its purity was evaluated by capillary zone electrophoresis.
C H, De Toni   +4 more
openaire   +2 more sources

The Hog Louse Haematopinus suis (Phtiraptera) Midgut Morphology and Function. Comparison With Hemiptera and Holometabola.

Archives of Insect Biochemistry and Physiology
The taxon Paraneoptera, comprising Condylognatha (Hemiptera e Thysanoptera) and Psocodea (Phthiraptera and Psocoptera), is paraphyletic, according to recent genomic studies. The midgut morphology and digestive physiology of Haematopinus suis (Phtiraptera)
Ericson K Gonçalves   +3 more
semanticscholar   +1 more source

Prolyl Endopeptidase and Dipeptidyl Peptidase IV are Distantly Related Members of the Same Family of Serine Proteases

Biological Chemistry Hoppe-Seyler, 1992
Prolyl endopeptidase and dipeptidyl peptidase IV are serine proteases which cleave the peptide bonds at the carboxy group of proline residues. They do not show amino acid sequence homology with the known serine enzymes, but a possible relationship between them has not yet been examined.
L, Polgár, E, Szabo
openaire   +2 more sources

Kallikrein-related peptidases: mechanistic understanding for potential therapeutic targeting in cancer

Expert opinion on therapeutic targets
Introduction Human kallikrein-related peptidases (KLKs) represent a subgroup of 15 serine endopeptidases involved in various physiological processes and pathologies, including cancer.
Glykeria N. Daneva   +3 more
semanticscholar   +1 more source

Endopeptidases Proteases Enzymes in Proteins

, 2021
A. Razzaq, Khadija Quddoos, A. Aftab
semanticscholar   +1 more source

Affinity and Specificity of Serine Endopeptidase-Protein Inhibitor Interactions

Journal of Molecular Biology, 1993
Stanley Krystek   +2 more
openaire   +1 more source

IgA-specific serine endopeptidase

1998
Dietmar Schomburg, Dörte Stephan
openaire   +1 more source

α‐Ketobenzothiazole Serine Protease Inhibitors of Aberrant HGF/c‐MET and MSP/RON Kinase Pathway Signaling in Cancer

ChemMedChem, 2016
Zhenfu Han   +7 more
semanticscholar   +1 more source

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