Evolution of vertebrate fibrin formation and the process of its dissolution. Export

@article{citeulike:186162, abstract = {The thrombin-catalysed conversion of fibrinogen into a fibrin gel is common to all extant vertebrates. Because fibrin formation is both temporary and risky, an effective scheme for fibrinolysis evolved concomitantly. In this regard, the fibrinogen molecule is well adapted both for network polymerization and for subsequent dismantling. The question is, has it always been so? It has long been known that the three non-identical chains that compose vertebrate fibrinogen are descended from a common ancestor, and the original molecule must have been either a homotrimer or a dimer thereof. Three-dimensional studies on core fragments of fibrinogen are revealing new insights about both fibrin formation and its destruction. These studies are also showing exactly what structural changes have accompanied changes in function for the various domains. Chief among these is the reversal of direction for the alpha chain after replacement of its C-terminal domain.}, address = {Center for Molecular Genetics, University of California at San Diego, La Jolla 92093-0634, USA.}, author = {Doolittle, R. F. and Spraggon, G. and Everse, S. J.}, citeulike-article-id = {186162}, citeulike-linkout-0 = {http://view.ncbi.nlm.nih.gov/pubmed/9524761}, citeulike-linkout-1 = {http://www.hubmed.org/display.cgi?uids=9524761}, issn = {0300-5208}, journal = {Ciba Found Symp}, keywords = {blood, clotting, evo}, posted-at = {2005-05-08 02:07:47}, priority = {2}, title = {Evolution of vertebrate fibrin formation and the process of its dissolution.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/9524761}, volume = {212}, year = {1997} }

TY - JOUR ID - citeulike:186162 L3 - citeulike-article-id:186162 N2 - The thrombin-catalysed conversion of fibrinogen into a fibrin gel is common to all extant vertebrates. Because fibrin formation is both temporary and risky, an effective scheme for fibrinolysis evolved concomitantly. In this regard, the fibrinogen molecule is well adapted both for network polymerization and for subsequent dismantling. The question is, has it always been so? It has long been known that the three non-identical chains that compose vertebrate fibrinogen are descended from a common ancestor, and the original molecule must have been either a homotrimer or a dimer thereof. Three-dimensional studies on core fragments of fibrinogen are revealing new insights about both fibrin formation and its destruction. These studies are also showing exactly what structural changes have accompanied changes in function for the various domains. Chief among these is the reversal of direction for the alpha chain after replacement of its C-terminal domain. JF - Ciba Found Symp SN - 0300-5208 AD - Center for Molecular Genetics, University of California at San Diego, La Jolla 92093-0634, USA. TI - Evolution of vertebrate fibrin formation and the process of its dissolution. VL - 212 KW - blood KW - clotting KW - evo AU - Doolittle, RF AU - Spraggon, G AU - Everse, SJ PY - 1997/// UR - http://view.ncbi.nlm.nih.gov/pubmed/9524761 ER -