Publication Detail
The publication detail shows the title, authors (with indicators showing other profiled authors), information on the publishing organization, abstract and a link to the article in PubMed. This abstract is what is used to create the fingerprint of the publication. If any grants are referenced by the publication, they will be listed here as well.
The cutting edge: membrane-anchored serine protease activities in the pericellular microenvironment.
Toni M Antalis; Marguerite S Buzza; Kathryn M Hodge; John D Hooper; Sarah Netzel-Arnett (Profiled Author: Toni Antalis)
Center for Vascular and Inflammatory Diseases and Department of Physiology, University of Maryland School of Medicine, Baltimore, MD 21201, USA. tantalis@som.umaryland.edu
The Biochemical journal 2010;428(3):325-46.
The serine proteases of the trypsin-like (S1) family play critical roles in many key biological processes including digestion, blood coagulation, and immunity. Members of this family contain N- or C-terminal domains that serve to tether the serine protease catalytic domain directly to the plasma membrane. These membrane-anchored serine proteases are proving to be key components of the cell machinery for activation of precursor molecules in the pericellular microenvironment, playing vital functions in the maintenance of homoeostasis. Substrates activated by membrane-anchored serine proteases include peptide hormones, growth and differentiation factors, receptors, enzymes, adhesion molecules and viral coat proteins. In addition, new insights into our understanding of the physiological functions of these proteases and their involvement in human pathology have come from animal models and patient studies. The present review discusses emerging evidence for the diversity of this fascinating group of membrane serine proteases as potent modifiers of the pericellular microenvironment through proteolytic processing of diverse substrates. We also discuss the functional consequences of the activities of these proteases on mammalian physiology and disease.
3 Originating Grant
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1.
ANTALIS, TONI M.
Protease Pathways in the Gastrointestinal Tract
25 July 2009 - 30 June 2011
NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES
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2.
Antalis, Toni M
New Function for the Serpin PAI-2 as a Regular of pRb
1 August 2003 - 31 May 2009
NATIONAL CANCER INSTITUTE
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3.
Antalis, Toni M
NEW FUNCTION SERPIN PAI 2 AS A REGULAR OF RB
1 July 2002 - 30 June 2010
NATIONAL CANCER INSTITUTE
Scientific Context
This section shows information related to the publication - computed using the fingerprint of the publication - including related publications, related experts and related grants with fingerprints representing significant amounts of overlap between their fingerprint and this publication. The red dots indicate whether those experts or terms appear within the publication, thereby showing potential and actual connections.
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Proceedings of the National Academy of Sciences of the United States of America 2011;108(31):12881-6. -
2.
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1992G A Clawson; L L Norbeck; C L Hatem; C Rhodes; P Amiri; J H McKerrow; S R Patierno; G Fiskum
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