The Serpins Are an Expanding Superfamily of Structurally Similar but Functionally Diverse Proteins

By G. Silverman, P. Bird, R. Carrell, F. Church, P. Coughlin, P. Gettins, J. Irving, D. Lomas, C. J. Luke, R. Moyer and 5 more. Journal of Biological Chemistry, 2001

1,263 citations recorded by the source corpus.

Published, JBC Papers in Press, July 2, 2001, DOI 10.1074/jbc.R100016200 Gary A. Silverman, Phillip I. Bird, Robin W. Carrell, Frank C. Church, Paul B. Coughlin, Peter G. W. Gettins, James A Irving, David A. Lomas, Cliff J. Luke, Richard W. Moyer, Philip A. Pemberton, Eileen Remold-O’Donnell, Guy S. Salvesen, James Travis, and James C. Whisstock From the Department of Pediatrics, Division of Newborn Medicine, Children’s Hospital, Harvard Medical School, Boston, Massachusetts 02115, Department of Biochemistry and Molecular Biology, Monash University, Melbourne, Victoria 3800, Australia, Departments of Haematology and Medicine, University of Cambridge, Wellcome Trust Centre for Molecular Mechanisms in Disease, Cambridge Institute for Medical Research, Wellcome Trust/MRC Building, Hills Road, Cambridge CB2 2XY, United Kingdom, Division of Hematology-Oncology/Medicine, University of North Carolina, Chapel Hill, North Carolina 27599, Department of Medicine, Box Hill Hospital, Monash University, Melbourne, Victoria 3128, Australia, Department of Biochemistry and Molecular Biology, University of Illinois, Chicago, Illinois 60612, Department of Molecular Genetics and Microbiology, University of Florida College of Medicine, Gainesville, Florida 32610, Arriva Pharmaceuticals, Alameda, California 94501, Center for Blood Research, Harvard Medical School, Boston, Massachusetts 02115, Burnham Institute, San Diego, California 92037, Department of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia 30602

Subfields: Biotechnology, Cancer Research, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/9002069c105295df80594447eccaa496e751e283

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Biotechnology

1. A. Córdoba‐Aguilar
2. I. González-Santoyo
3. Guido Kroemer

In Cancer Research

1. A. Córdoba‐Aguilar
2. I. González-Santoyo
3. J. Lieberman
4. Guido Kroemer
5. Ashley M. Buckle
6. Marcus E. Peter

In Molecular Biology

1. P. Boya
2. Guido Kroemer
3. A. Córdoba‐Aguilar
4. I. González-Santoyo
5. J. Lieberman
6. Ashley M. Buckle
7. James C. Whisstock
8. Marcus E. Peter

Citations in the corpus

• NF‐κB protects from the lysosomal pathway of cell death (2003, background): “…such as c-IAPs which inhibit caspases (Deveraux et al., 1998) and cystatins which inhibit papain-like cysteine cathepsins (Turk and Bode, 1991), serpins characteristically act as `suicide substrates' and inactivate proteases through the formation of a 1:1 covalent complex (Silverman et al., 2001).”
• Neutrophil Elastase, Proteinase 3, and Cathepsin G as Therapeutic Targets in Human Diseases (2010, background): “Human serpins belong to the first nine clades (A–I) of the 16 that have been described based on phylogenic relationships (Irving et al., 2000; Silverman et al., 2001; Mangan et al., 2008).”
• Hereditary and acquired angioedema: Problems and progress: Proceedings of the third C1 esterase inhibitor deficiency workshop and beyond (2004, positive): “C1-INH belongs to the family of serine protease inhibitors, or serpins, which also includes proteins such as a1-antitrypsin and antithrombin III [194] [195] [196] [197] (Fig 16) .”
• Lysosomal membrane permeabilization in cell death (2008, background): “Serpins (serine protease inhibitors) are a family of protease inhibitors that act either at the extracellular or at the intracellular levels (Silverman et al., 2001; Law et al., 2006).”
• Otolith Biochemistry—A Review (2019, background): “As a member of the Serpin superfamily, it is an inhibitor of serine proteases (Silverman et al., 2001).”
• An overview of the serpin superfamily (2006, background): “In humans, the two largest clades of the 36 serpins that have been identified are the extracellular ‘clade A’ molecules (thirteen members found on chromosomes 1, 14 and X) and the intracellular ‘clade B’ serpins (thirteen members on chromosomes 18 and 6) [3].”
• Phenoloxidase: a key component of the insect immune system (2012, background): “Other groups of serin proteases inhibitors are serpins (Silverman et al., 2001; Gettins, 2002).”
• Death by a thousand cuts: granzyme pathways of programmed cell death. (2008, background): “Serpins are the largest and most broadly distributed superfamily of protease inhibitors, with more than 1500 family members (88, 89).”