Integrin activation.

Integrin-mediated cell adhesion is important for development, immune responses, hemostasis and wound healing. Integrins also function as signal transducing receptors that can control intracellular pathways that regulate cell survival, proliferation, and cell fate. Conversely, cells can modulate the affinity of integrins for their ligands a process operationally defined as integrin activation. Analysis of activation of integrins has now provided a detailed molecular understanding of this unique form of "inside-out" signal transduction and revealed new paradigms of how transmembrane domains (TMD) can transmit long range allosteric changes in transmembrane proteins. Here, we will review how talin and mediates integrin activation and how the integrin TMD can transmit these inside out signals

A case of rupture of the biceps brachii and brachialis muscles by direct violence

T

Generalizing Boolean Satisfiability I: Background and Survey of Existing Work

This is the first of three planned papers describing ZAP, a satisfiability engine that substantially generalizes existing tools while retaining the performance characteristics of modern high-performance solvers. The fundamental idea underlying ZAP is that many problems passed to such engines contain rich internal structure that is obscured by the Boolean representation used; our goal is to define a representation in which this structure is apparent and can easily be exploited to improve computational performance. This paper is a survey of the work underlying ZAP, and discusses previous attempts to improve the performance of the Davis-Putnam-Logemann-Loveland algorithm by exploiting the structure of the problem being solved. We examine existing ideas including extensions of the Boolean language to allow cardinality constraints, pseudo-Boolean representations, symmetry, and a limited form of quantification. While this paper is intended as a survey, our research results are contained in the two subsequent articles, with the theoretical structure of ZAP described in the second paper in this series, and ZAP's implementation described in the third

Data management study, volume 5. Appendix I - Contract or data package overall management /MA/, scheduling /SC/, MANNING and financial /MF/ Final report

Overall management, scheduling, manpower, and financial aspects of Voyager data managemen

Review of \u3cem\u3eGeneralist Practice: A Task-Centered Approach.\u3c/em\u3e Eleanor Reardon Tolson, William J. Reid and Charles D. Garvin. Reviewed by Leon H. Ginsberg, University of South Carolina.

Eleanor Reardon Tolson, William J. Reid and Charles D. Garvin, Generalist Practice: A Task-Centered Approach. New York: Columbia, University Press, 1994. $37.50 hardcover

A review of the available objective-type tests used in college science courses since 1938

Thesis (Ed.M.)--Boston Universit

Affinity modulation of platelet integrin alphaIIbbeta3 by beta3-endonexin, a selective binding partner of the beta3 integrin cytoplasmic tail.

Platelet agonists increase the affinity state of integrin alphaIIbbeta3, a prerequisite for fibrinogen binding and platelet aggregation. This process may be triggered by a regulatory molecule(s) that binds to the integrin cytoplasmic tails, causing a structural change in the receptor. beta3-Endonexin is a novel 111-amino acid protein that binds selectively to the beta3 tail. Since beta3-endonexin is present in platelets, we asked whether it can affect alphaIIbbeta3 function. When beta3-endonexin was fused to green fluorescent protein (GFP) and transfected into CHO cells, it was found in both the cytoplasm and the nucleus and could be detected on Western blots of cell lysates. PAC1, a fibrinogen-mimetic mAb, was used to monitor alphaIIbbeta3 affinity state in transfected cells by flow cytometry. Cells transfected with GFP and alphaIIbbeta3 bound little or no PAC1. However, those transfected with GFP/beta3-endonexin and alphaIIbbeta3 bound PAC1 specifically in an energy-dependent fashion, and they underwent fibrinogen-dependent aggregation. GFP/beta3-endonexin did not affect levels of surface expression of alphaIIbbeta3 nor did it modulate the affinity of an alphaIIbbeta3 mutant that is defective in binding to beta3-endonexin. Affinity modulation of alphaIIbbeta3 by GFP/beta3-endonexin was inhibited by coexpression of either a monomeric beta3 cytoplasmic tail chimera or an activated form of H-Ras. These results demonstrate that beta3-endonexin can modulate the affinity state of alphaIIbbeta3 in a manner that is structurally specific and subject to metabolic regulation. By analogy, the adhesive function of platelets may be regulated by such protein-protein interactions at the level of the cytoplasmic tails of alphaIIbbeta3