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  • Milestones in Magnetic Resonance Imaging and Transcranial Sonography of Movement Disorders MOVEMENT DISORDERS Berg, D., Steinberger, J. D., Olanow, C. W., Naidich, T. P., Yousry, T. A. 2011; 26 (6): 979-992

    Abstract

    Twenty-five years ago, when this journal was initiated, imaging of movement disorders was in its infancy. Since that time, magnetic resonance imaging has become a standard technique that is routinely performed in patients with movement disorders in order to exclude secondary causes and in some instances to provide specific information that aids in making the diagnosis of a neurodegenerative condition. Transcranial sonography is a more recent advance and is now widely employed to aid in the diagnosis of Parkinson's disease and possibly in detecting individuals in the premotor phases of the disease. Investigations are currently under way to evaluate the value of this technique in other movement disorders.

    View details for DOI 10.1002/mds.23766

    View details for Web of Science ID 000291353900007

    View details for PubMedID 21626543

  • Effects of Limiting Extension at the alpha IIb Genu on Ligand Binding to Integrin alpha IIb beta 3 JOURNAL OF BIOLOGICAL CHEMISTRY Blue, R., Li, J., Steinberger, J., Murcia, M., Filizola, M., Coller, B. S. 2010; 285 (23): 17604-17613

    Abstract

    Structural data of integrin alphaIIbbeta3 have been interpreted as supporting a model in which: 1) the receptor exists primarily in a "bent," low affinity conformation on unactivated platelets and 2) activation induces an extended, high affinity conformation prior to, or following, ligand binding. Previous studies found that "clasping" the alphaIIb head domain to the beta3 tail decreased fibrinogen binding. To study the role of alphaIIb extension about the genu, we introduced a disulfide "clamp" between the alphaIIb thigh and calf-1 domains. Clamped alphaIIbbeta3 had markedly reduced ability to bind the large soluble ligands fibrinogen and PAC-1 when activated with monoclonal antibody (mAb) PT25-2 but not when activated by Mn(2+) or by coexpressing the clamped alphaIIb with a beta3 subunit containing the activating mutation N339S. The clamp had little effect on the binding of the snake venom kistrin (M(r) 7,500) or alphaIIbbeta3-mediated adhesion to immobilized fibrinogen, but it did diminish the enhanced binding of mAb AP5 in the presence of kistrin. Collectively, our studies support a role for alphaIIb extension about the genu in the binding of ligands of 340,000 and 900,000 M(r) with mAb-induced activation but indicate that it is not an absolute requirement. Our data are consistent with alphaIIb extension resulting in increased access to the ligand-binding site and/or facilitating the conformational change(s) in beta3 that affect the intrinsic affinity of the binding pocket for ligand.

    View details for DOI 10.1074/jbc.M110.107763

    View details for Web of Science ID 000278133400039

    View details for PubMedID 20363746

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