TY - JOUR
T1 - Conformational changes in adhesive proteins modulate their adhesive function
AU - Ugarova, T.
AU - Agbanyo, F. R.
AU - Plow, E. F.
PY - 1995
Y1 - 1995
N2 - A large family of glycoproteins mediates cell adhesion by binding to cellular receptors. As a group, these adhesive proteins are large in size, multi-domainal in composition, and are capable of self-association. A general property of the adhesive proteins is their susceptibility to structural modulation, and conformational change provides a mechanism for regulation of their adhesive functions. To illustrate this concept, conformational alterations of thrombospondin, fibrinogen and fibronectin are shown to modulate their adhesive potential. Thus, conformational status of the adhesive proteins contributes to the regulation of cell adhesion.
AB - A large family of glycoproteins mediates cell adhesion by binding to cellular receptors. As a group, these adhesive proteins are large in size, multi-domainal in composition, and are capable of self-association. A general property of the adhesive proteins is their susceptibility to structural modulation, and conformational change provides a mechanism for regulation of their adhesive functions. To illustrate this concept, conformational alterations of thrombospondin, fibrinogen and fibronectin are shown to modulate their adhesive potential. Thus, conformational status of the adhesive proteins contributes to the regulation of cell adhesion.
UR - http://www.scopus.com/inward/record.url?scp=0029119077&partnerID=8YFLogxK
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U2 - 10.1055/s-0038-1642686
DO - 10.1055/s-0038-1642686
M3 - Article
C2 - 8578468
AN - SCOPUS:0029119077
SN - 0340-6245
VL - 74
SP - 253
EP - 257
JO - Thrombosis and Haemostasis
JF - Thrombosis and Haemostasis
IS - 1
ER -