TY - JOUR
T1 - Serpins flex their muscle
T2 - I. Putting the clamps on proteolysis in diverse biological systems
AU - Silverman, Gary A.
AU - Whisstock, James C.
AU - Bottomley, Stephen P.
AU - Huntington, James A.
AU - Kaiserman, Dion
AU - Luke, Cliff J.
AU - Pak, Stephen C.
AU - Reichhart, Jean Marc
AU - Bird, Phillip I.
PY - 2010/8/6
Y1 - 2010/8/6
N2 - Serpins compose the largest superfamily of peptidase inhibitors and are well known as regulators of hemostasis and thrombolysis. Studies using model organisms, from plants to vertebrates, now show that serpins and their unique inhibitory mechanism and conformational flexibility are exploited to control proteolysis in molecular pathways associated with cell survival, development, and host defense. In addition, an increasing number of non-inhibitory serpins are emerging as important elements within a diversity of biological systems by serving as chaperones, hormone transporters, or anti-angiogenic factors.
AB - Serpins compose the largest superfamily of peptidase inhibitors and are well known as regulators of hemostasis and thrombolysis. Studies using model organisms, from plants to vertebrates, now show that serpins and their unique inhibitory mechanism and conformational flexibility are exploited to control proteolysis in molecular pathways associated with cell survival, development, and host defense. In addition, an increasing number of non-inhibitory serpins are emerging as important elements within a diversity of biological systems by serving as chaperones, hormone transporters, or anti-angiogenic factors.
UR - http://www.scopus.com/inward/record.url?scp=77955302605&partnerID=8YFLogxK
U2 - 10.1074/jbc.R110.112771
DO - 10.1074/jbc.R110.112771
M3 - Short survey
C2 - 20498369
AN - SCOPUS:77955302605
SN - 0021-9258
VL - 285
SP - 24299
EP - 24305
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 32
ER -