Resultats de la cerca - S. Gurusiddappa

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  1. 1
    The Fibronectin-binding MSCRAMM FnbpA ofStaphylococcus aureus Is a Bifunctional Protein That Also Binds to Fibrinogen

    The Fibronectin-binding MSCRAMM FnbpA ofStaphylococcus aureus Is a Bifunctional Protein That Also Binds to Fibrinogen per Elisabeth R. Wann, Sivashankarappa Gurusiddappa, Magnus Höök

    Publicat 2000
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  2. 2
    Heparin-binding peptides from thrombospondins 1 and 2 contain focal adhesion-labilizing activity.

    Heparin-binding peptides from thrombospondins 1 and 2 contain focal adhesion-labilizing activity. per Joanne E. Murphy-Ullrich, S. Gurusiddappa, William A. Frazier, Magnus Höök

    Publicat 1993
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  3. 3
    SdrG, a Fibrinogen-binding Bacterial Adhesin of the Microbial Surface Components Recognizing Adhesive Matrix Molecules Subfamily from Staphylococcus epidermidis, Targets the Thrombin Cleavage Site in the Bβ Chain

    SdrG, a Fibrinogen-binding Bacterial Adhesin of the Microbial Surface Components Recognizing Adhesive Matrix Molecules Subfamily from Staphylococcus epidermidis, Targets the Thromb... per Stacey Davis, Sivashankarappa Gurusiddappa, Kirk W. McCrea, Samuel Perkins, Magnus Höök

    Publicat 2001
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  4. 4
    Health benefits of finger millet (Eleusine coracana L.) polyphenols and dietary fiber: a review

    Health benefits of finger millet (Eleusine coracana L.) polyphenols and dietary fiber: a review per Devi, Palanisamy Bruntha, Vijayabharathi, Rajendran, Sathyabama, Sathyaseelan, Malleshi, Nagappa Gurusiddappa, Priyadarisini, Venkatesan Brindha

    Publicat 2011
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  5. 5
    The Fibrinogen-binding MSCRAMM (Clumping Factor) of Staphylococcus aureus Has a Ca2+-dependent Inhibitory Site

    The Fibrinogen-binding MSCRAMM (Clumping Factor) of Staphylococcus aureus Has a Ca2+-dependent Inhibitory Site per D. P. O’Connell, Tamanna Nanavaty, Damien McDevitt, Sivashankarappa Gurusiddappa, Magnus Höök, Timothy J. Foster

    Publicat 1998
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  6. 6
    Two different genes coding for fibronectin‐binding proteins from <i>Streptococcus dysgalactiae</i>

    Two different genes coding for fibronectin‐binding proteins from <i>Streptococcus dysgalactiae</i> per Per‐Eric Lindgren, Martin J. McGavin, Christer Signäs, Bengt Guss, Sivashankarappa Gurusiddappa, Magnus Höök, Martin Lindberg

    Publicat 1993
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  7. 7
    Multiple Binding Sites in Collagen Type I for the Integrins α1β1 and α2β1

    Multiple Binding Sites in Collagen Type I for the Integrins α1β1 and α2β1 per Yi Xu, Sivashankarappa Gurusiddappa, Rebecca L. Rich, Rick T. Owens, Douglas R. Keene, Richard Mayne, Agneta Höök, Magnus Höök

    Publicat 2000
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  8. 8
    A ‘Collagen Hug’ Model for Staphylococcus aureus CNA binding to collagen

    A ‘Collagen Hug’ Model for Staphylococcus aureus CNA binding to collagen per Yinong Zong, Yi Xu, Xiaowen Liang, Douglas R. Keene, Agneta Höök, Shivasankarappa Gurusiddappa, Magnus Höök, Sthanam V.L. Narayana

    Publicat 2005
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  9. 9
    A ‘Collagen Hug' Model for Staphylococcus aureus CNA binding to collagen

    A ‘Collagen Hug' Model for Staphylococcus aureus CNA binding to collagen per Zong, Yinong, Xu, Yi, Liang, Xiaowen, Keene, Douglas R, Höök, Agneta, Gurusiddappa, Shivasankarappa, Höök, Magnus, Narayana, Sthanam V L

    Publicat 2005
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  10. 10
    A ‘Collagen Hug' model for Staphylococcus aureus CNA binding to collagen

    A ‘Collagen Hug' model for Staphylococcus aureus CNA binding to collagen per Zong, Yinong, Xu, Yi, Liang, Xiaowen, Keene, Douglas R, Höök, Agneta, Gurusiddappa, Shivasankarappa, Höök, Magnus, Narayanas, Sthanam V L

    Publicat 2006
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  11. 11
    β-Neurexin Is a Ligand for the Staphylococcus aureus MSCRAMM SdrC

    β-Neurexin Is a Ligand for the Staphylococcus aureus MSCRAMM SdrC per Barbu, E. Magda, Ganesh, Vannakambadi K., Gurusiddappa, Shivasankarappa, Mackenzie, R. Chris, Foster, Timothy J., Sudhof, Thomas C., Höök, Magnus

    Publicat 2010
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  12. 12
    Borrelia burgdorferi Binds Fibronectin through a Tandem β-Zipper, a Common Mechanism of Fibronectin Binding in Staphylococci, Streptococci, and Spirochetes

    Borrelia burgdorferi Binds Fibronectin through a Tandem β-Zipper, a Common Mechanism of Fibronectin Binding in Staphylococci, Streptococci, and Spirochetes per Sophie Raibaud, Ulrich Schwarz‐Linek, Jung Hwa Kim, Huw T. Jenkins, Elizabeth R. Baines, Sivashankarappa Gurusiddappa, Magnus Höök, Jennifer R. Potts

    Publicat 2005
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  13. 13
    A “dock, lock, and latch” Structural Model for a Staphylococcal Adhesin Binding to Fibrinogen

    A “dock, lock, and latch” Structural Model for a Staphylococcal Adhesin Binding to Fibrinogen per Karthe Ponnuraj, M. Gabriela Bowden, Stacey Davis, S. Gurusiddappa, Dwight Moore, Damon Choe, Yi Xu, Magnus Höök, Sthanam V.L. Narayana

    Publicat 2003
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  14. 14
    β-Neurexin Is a Ligand for the Staphylococcus aureus MSCRAMM SdrC

    β-Neurexin Is a Ligand for the Staphylococcus aureus MSCRAMM SdrC per E. Magda Barbu, Vannakambadi K. Ganesh, Shivasankarappa Gurusiddappa, Roger C. MacKenzie, Timothy J. Foster, Thomas C. Südhof, Magnus Höök

    Publicat 2010
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  15. 15
    The Tandem β-Zipper Model Defines High Affinity Fibronectin-binding Repeats within Staphylococcus aureus FnBPA

    The Tandem β-Zipper Model Defines High Affinity Fibronectin-binding Repeats within Staphylococcus aureus FnBPA per Nicola A. G. Meenan, Livia Visai, Viviana Valtulina, Ulrich Schwarz‐Linek, Nicole C. Norris, Sivashankarappa Gurusiddappa, Magnus Höök, Pietro Speziale, Jennifer R. Potts

    Publicat 2007
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  16. 16
    Evidence for the “Dock, Lock, and Latch” Ligand Binding Mechanism of the Staphylococcal Microbial Surface Component Recognizing Adhesive Matrix Molecules (MSCRAMM) SdrG

    Evidence for the “Dock, Lock, and Latch” Ligand Binding Mechanism of the Staphylococcal Microbial Surface Component Recognizing Adhesive Matrix Molecules (MSCRAMM) SdrG per M. Gabriela Bowden, Alejandro P. Heuck, Karthe Ponnuraj, Elena Kolosova, Damon Choe, Sivashankarappa Gurusiddappa, Sthanam V.L. Narayana, Arthur E. Johnson, Magnus Höök

    Publicat 2007
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  17. 17
    A Structural Model of the Staphylococcus aureus ClfA–Fibrinogen Interaction Opens New Avenues for the Design of Anti-Staphylococcal Therapeutics

    A Structural Model of the Staphylococcus aureus ClfA–Fibrinogen Interaction Opens New Avenues for the Design of Anti-Staphylococcal Therapeutics per Vannakambadi K. Ganesh, Julián Rivera, Emanuel Smeds, Ya-Ping Ko, M. Gabriela Bowden, Elisabeth R. Wann, Shivasankarappa Gurusiddappa, J. Ross Fitzgerald, Magnus Höök

    Publicat 2008
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  18. 18
    A Structural Model of the Staphylococcus aureus ClfA–Fibrinogen Interaction Opens New Avenues for the Design of Anti-Staphylococcal Therapeutics

    A Structural Model of the Staphylococcus aureus ClfA–Fibrinogen Interaction Opens New Avenues for the Design of Anti-Staphylococcal Therapeutics per Ganesh, Vannakambadi K., Rivera, Jose J., Smeds, Emanuel, Ko, Ya-Ping, Bowden, M. Gabriela, Wann, Elisabeth R., Gurusiddappa, Shivasankarappa, Fitzgerald, J. Ross, Höök, Magnus

    Publicat 2008
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  19. 19
    Global gene expression profiling confirms the molecular fidelity of primary tumor-based orthotopic xenograft mouse models of medulloblastoma

    Global gene expression profiling confirms the molecular fidelity of primary tumor-based orthotopic xenograft mouse models of medulloblastoma per Xiumei Zhao, Zhigang Liu, Litian Yu, Yujing Zhang, Patricia Baxter, Horatiu Voicu, Sivashankarappa Gurusiddappa, Joseph Luan, Jack M. Su, Hon-Chiu Eastwood Leung, Xiao‐Nan Li

    Publicat 2012
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  20. 20
    Global gene expression profiling confirms the molecular fidelity of primary tumor-based orthotopic xenograft mouse models of medulloblastoma

    Global gene expression profiling confirms the molecular fidelity of primary tumor-based orthotopic xenograft mouse models of medulloblastoma per Zhao, Xiumei, Liu, Zhigang, Yu, Litian, Zhang, Yujing, Baxter, Patricia, Voicu, Horatiu, Gurusiddappa, Sivashankarappa, Luan, Joseph, Su, Jack M., Leung, Hon-chiu Eastwood, Li, Xiao-Nan

    Publicat 2012
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