Results 281 to 290 of about 580,293 (310)
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Engineering of proteases and protease inhibition

Current Opinion in Biotechnology, 1991
Proteases are unquestionably the single most studied class of enzymes and yet many questions still remain about their mechanisms and roles. Protein engineering offers the opportunity to provide some of the answers. In this review, recent advances towards the understanding of stability, mechanism, specificity and regulation of proteases and their ...
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Proteases and protease inhibitors in cancer

Acta Histochemica, 1998
The second conference on 'Proteases and protease inhibitors in cancer' was organized by the American Association for Cancer Research (AACR) and Acta Pathologica Microbiologica et Immunologica Scandinavica (APMIS). To understand the role of proteinases and to develop relevant synthetic inhibitors to stop or slow the progression of cancer, an integrated ...
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Proteases and Protease Inhibitors in Tumor Progression

1997
Our understanding of the role of matrix degrading proteases in cancer has dramatically expanded over the last two decades. From correlative observations linking proteases to cancer progression, we have accumulated evidence supporting a causal role for proteases in various steps of tumor progression and have become increasingly aware of the complex ...
Ralph A. Reisfeld   +5 more
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Proteases

2007
International ...
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Seed proteases and protease inhibitors

Economic Botany, 1970
This review, which unavoidably has to be of a highly selective nature, covers the literature through December, 1967, and is concerned with two classes of proteins which are involved in the metabolism of seeds: proteases and protease inhibitors. During germination, proteases degrade protein reserves of seeds with an attendant release of peptides, free ...
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Periplasmic Proteases and Protease Inhibitors

2014
In general, proteases are involved in diverse functions; the most notable include digestive, protective, and regulatory processes. Digestive proteases are involved in protein degradation for nutritional purposes. About 35% of all entries in the MEROPS database are classified as serine proteases.
Kucz Nicolette   +2 more
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Proteases and emphysema

Current Opinion in Pulmonary Medicine, 2005
The protease-antiprotease theory of emphysema is widely accepted, but exactly which cells/proteases play a role continues to be a controversial subject.Reports in humans show increased metalloproteinase activity in emphysema, but the exact role of metalloproteinases remains unclear.
Andrew Churg, Joanne L. Wright
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The aspartic proteases

Scandinavian Journal of Clinical and Laboratory Investigation, 1992
The Aspartic proteases (EC 3.4.23) are a group of proteolytic enzymes that share the same catalytic apparatus. Members of the aspartic protease family can be found in different organisms, ranging from humans to plants and retroviruses. The best known sources of aspartic proteases are the stomach of mammals, yeast and fungi, with porcine pepsin as the ...
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Proteases: a primer [PDF]

open access: possibleEssays in Biochemistry, 2002
A protease can be defined as an enzyme that hydrolyses peptide bonds. Proteases can be divided into endopeptidases, which cleave internal peptide bonds in substrates, and exopeptidases, which cleave the terminal peptide bonds. Exopeptidases can be further subdivided into aminopeptidases and carboxypeptidases.
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Lung Proteases and Protease Inhibitors

1977
Homogenates of guinea pig lung show significant protease activity at pH values from 2.2 to 9.9. Perfusion results in increased activity in both acid and alkaline ranges. Protease activity can be extracted by repeated homogenization and sonication of the pellet.
George Kalnitsky, Jeffrey Ihnen
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