An overview of the serpin superfamily

By R. Law, Qingwei Zhang, S. McGowan, Ashley M. Buckle, G. Silverman, W. Wong, Carlos J. Rosado, C. Langendorf, R. Pike, Philip I Bird and 1 more. Genome Biology, 2006

706 citations recorded by the source corpus.

Serpins are a broadly distributed family of protease inhibitors that use a conformational change to inhibit target enzymes. They are central in controlling many important proteolytic cascades, including the mammalian coagulation pathways. Serpins are conformationally labile and many of the disease-linked mutations of serpins result in misfolding or in pathogenic, inactive polymers.

Subfields: Cancer Research, Cell Biology, Hematology

View Paper: https://www.semanticscholar.org/paper/f00a046576e1159ff1f3073f1f99fb4a42c9b97e

How researchers see this paper

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

In Cancer Research

1. J. Lieberman
2. Guido Kroemer
3. Benjamin T. Porebski
4. Ashley M. Buckle
5. H. Habib
6. K. Fazili
7. R. Weinberg

In Cell Biology

1. P. Boya
2. Guido Kroemer
3. Benjamin T. Porebski
4. Ashley M. Buckle
5. H. Habib
6. K. Fazili

In Hematology

1. Benjamin T. Porebski
2. Ashley M. Buckle
3. H. Habib
4. K. Fazili

Citations in the corpus

• 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).”
• Plant protease inhibitors: a defense strategy in plants (2007, background): “pathways involved in up-regulating the host immune response (Law et al., 2006).”
• Serpins Promote Cancer Cell Survival and Vascular Cooption in Brain Metastasis (2014, neutral): “Four serpins (NS and serpins B2, E1, and E2) selectively inhibit PA (Law et al., 2006).”
• Consensus protein design (2016, background): “The delicate balance between function and misfolding is exemplified by members of the serine protease inhibitor or serpin superfamily (Gettins, 2002; Lomas and Carrell, 2002; Law et al., 2006; Krishnan and Gierasch, 2011).”
• 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).”
• Common Genetic Variation In Cellular Transport Genes and Epithelial Ovarian Cancer (EOC) Risk (2015, background): “The serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 7 (SERPINA7), also known as thyroxine-binding globulin (TBG), is a protein that binds thyroid hormones thyroxin (T4) and 3,5,3’-triiodothyronine (T3) in circulation [52].”