Zobrazeno 1 - 10
of 29
pro vyhledávání: '"H.W. Christinger"'
Autor:
Arieh Gertler, H.W. Christinger, P.A. Elkins, Anthony A. Kossiakoff, E. Sakal, Y. Sandowski, A.M. de Vos
Publikováno v:
Nature Structural Biology. 7:808-815
Ternary complex between placental lactogen and the extracellular domain of the prolactin receptor
Autor:
Germaine Fuh, Christian Wiesmann, H.W. Christinger, Yongmei Chen, Henry B. Lowman, A.M. de Vos, P. Mckay, Bing Li
Publikováno v:
Journal of Molecular Biology. 293:865-881
The Fab portion of a humanized antibody (Fab-12; IgG form known as rhuMAb VEGF) to vascular endothelial growth factor (VEGF) has been affinity-matured through complementarity-determining region (CDR) mutation, followed by affinity selection using mon
Autor:
Sarah G. Hymowitz, H.W. Christinger, Mark P. O'Connell, A.M. de Vos, Germaine Fuh, Robert F. Kelley, M.H. Ultsch, Avi Ashkenazi
Publikováno v:
Molecular Cell. 4(4):563-571
Formation of a complex between Apo2L (also called TRAIL) and its signaling receptors, DR4 and DR5, triggers apoptosis by inducing the oligomerization of intracellular death domains. We report the crystal structure of the complex between Apo2L and the
Autor:
Brian C. Cunningham, C.J. Keenan, Wayne J. Fairbrother, Andrea G. Cochran, Christian Wiesmann, H.W. Christinger, A.M. de Vos, Gloria Meng
Publikováno v:
Biochemistry. 37:17765-17772
Vascular endothelial growth factor (VEGF) is a specific and potent angiogenic factor and, therefore, a prime therapeutic target for the development of antagonists for the treatment of cancer. As a first step toward this goal, phage display was used t
Autor:
Germaine Fuh, Jeffrey Tom, Clifford Quan, Stephanie Shriver, Wayne J. Fairbrother, Christopher J. Keenan, Andrea G. Cochran, Brian C. Cunningham, James A. Wells, H.W. Christinger
Publikováno v:
Biochemistry. 37:17754-17764
Peptides that inhibit binding of vascular endothelial growth factor (VEGF) to its receptors, KDR and Flt-1, have been produced using phage display. Libraries of short disulfide-constrained peptides yielded three distinct classes of peptides that bind
Publikováno v:
Structure. 6:637-648
Background: Vascular endothelial growth factor (VEGF) is an endothelial cell-specific mitogen and is a potent angiogenic and vascular permeabilizing factor. VEGF is also an important mediator of pathological angiogenesis associated with cancer, rheum
Publikováno v:
Structure. 5:1325-1338
Background: Vascular endothelial growth factor (VEGF) is an endothelial cell-specific angiogenic and vasculogenic mitogen. VEGF also plays a role in pathogenic vascularization which is associated with a number of clinical disorders, including cancer
Autor:
Bruce Keyt, Lea T. Berleau, Napoleone Ferrara, Brian C. Cunningham, Yves A. Muller, H.W. Christinger, Abraham M. de Vos
Publikováno v:
Proteins: Structure, Function, and Genetics. 26:353-357
Vascular endothelial growth factor (VEGF) is a potent angiogenic factor with a unique specificity for vascular endothelial cells. In addition to its role in vasculogenesis and embryonic angiogenesis, VEGF is implicated in pathologic neovascularizatio
Publikováno v:
The Journal of biological chemistry. 279(11)
Placental growth factor (PlGF) is a member of the vascular endothelial growth factor (VEGF) family and plays an important role in pathological angiogenic events. PlGF exerts its biological activities through binding to VEGFR1, a receptor tyrosine kin
Autor:
Anthony A. Kossiakoff, Y. Sandowski, E. Sakal, Arieh Gertler, P.A. Elkins, H.W. Christinger, A.M. de Vos
Publikováno v:
Acta crystallographica. Section D, Biological crystallography. 54(Pt 6 Pt 2)
Growth hormone and prolactin control somato-lactogenic biology. While high-resolution crystal structures have been determined for receptor complexes of human growth hormone, no such information exists for prolactin. A stable 1:2 complex was formed be