Результати пошуку - Soumya S. Ray

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  1. 1
    Crystal Structure of the Flagellar σ/Anti-σ Complex σ28/FlgM Reveals an Intact σ Factor in an Inactive Conformation

    Crystal Structure of the Flagellar σ/Anti-σ Complex σ28/FlgM Reveals an Intact σ Factor in an Inactive Conformation за авторством Margareta K. Sörenson, Soumya S. Ray, Seth A. Darst

    Опубліковано 2004
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  2. 2
    Small-molecule-mediated stabilization of familial amyotrophic lateral sclerosis-linked superoxide dismutase mutants against unfolding and aggregation

    Small-molecule-mediated stabilization of familial amyotrophic lateral sclerosis-linked superoxide dismutase mutants against unfolding and aggregation за авторством Soumya S. Ray, Richard J. Nowak, Robert H. Brown, Peter T. Lansbury

    Опубліковано 2005
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  3. 3
    The Parkinson Disease-linked LRRK2 Protein Mutation I2020T Stabilizes an Active State Conformation Leading to Increased Kinase Activity

    The Parkinson Disease-linked LRRK2 Protein Mutation I2020T Stabilizes an Active State Conformation Leading to Increased Kinase Activity за авторством Soumya S. Ray, Samantha Bender, Stephanie Kang, Regina Lin, Marcie A. Glicksman, Min Liu

    Опубліковано 2014
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  4. 4
    Triosephosphate isomerase from Plasmodium falciparum:. the crystal structure provides insights into antimalarial drug design

    Triosephosphate isomerase from Plasmodium falciparum:. the crystal structure provides insights into antimalarial drug design за авторством Sameer Velanker, Soumya S. Ray, Rajesh S. Gokhale, S Suma, Hemalatha Balaram, P. Balaram, MRN Murthy

    Опубліковано 1997
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  5. 5
    Type II Kinase Inhibitors Show an Unexpected Inhibition Mode against Parkinson’s Disease-Linked LRRK2 Mutant G2019S

    Type II Kinase Inhibitors Show an Unexpected Inhibition Mode against Parkinson’s Disease-Linked LRRK2 Mutant G2019S за авторством Min Liu, Samantha Bender, Gregory D. Cuny, Woody Sherman, Marcie A. Glicksman, Soumya S. Ray

    Опубліковано 2013
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  6. 6
    Elucidating the Aβ42 Anti-Aggregation Mechanism of Action of Tramiprosate in Alzheimer’s Disease: Integrating Molecular Analytical Methods, Pharmacokinetic and Clinical Data

    Elucidating the Aβ42 Anti-Aggregation Mechanism of Action of Tramiprosate in Alzheimer’s Disease: Integrating Molecular Analytical Methods, Pharmacokinetic and Clinical Data за авторством Petr Kočiš, Martin Tolar, Yongxin Yu, William Sinko, Soumya S. Ray, Kaj Blennow, Howard Fillit, John A. Hey

    Опубліковано 2017
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  7. 7
    Predicting resistance of clinical Abl mutations to targeted kinase inhibitors using alchemical free-energy calculations

    Predicting resistance of clinical Abl mutations to targeted kinase inhibitors using alchemical free-energy calculations за авторством Kevin Hauser, Christopher Negron, Steven K. Albanese, Soumya S. Ray, Thomas Steinbrecher, Robert Abel, John D. Chodera, Lingle Wang

    Опубліковано 2018
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  8. 8
    Structure–activity relationship study of selective benzimidazole-based inhibitors of Cryptosporidium parvum IMPDH

    Structure–activity relationship study of selective benzimidazole-based inhibitors of Cryptosporidium parvum IMPDH за авторством Sivapriya Kirubakaran, Suresh Kumar Gorla, Lisa Sharling, Minjia Zhang, Xiaoping Liu, Soumya S. Ray, Iain Macpherson, Boris Striepen, Lizbeth Hedstrom, Gregory D. Cuny

    Опубліковано 2012
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  9. 9
    Structural basis for conformational plasticity of the Parkinson's disease-associated ubiquitin hydrolase UCH-L1

    Structural basis for conformational plasticity of the Parkinson's disease-associated ubiquitin hydrolase UCH-L1 за авторством Chittaranjan Das, Quyen Q. Hoang, C.A. Kreinbring, Sarah J. Luchansky, Robin K. Meray, Soumya S. Ray, Peter T. Lansbury, Dagmar Ringe, Gregory A. Petsko

    Опубліковано 2006
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  10. 10
    The structure of unliganded reverse transcriptase from the human immunodeficiency virus type 1.

    The structure of unliganded reverse transcriptase from the human immunodeficiency virus type 1. за авторством David W. Rodgers, S.J. Gamblin, Bruce A. Harris, Soumya S. Ray, J S Culp, Brian D. Hellmig, Deborah J. Woolf, Christine Debouck, Stephen C. Harrison

    Опубліковано 1995
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  11. 11
    Structure–activity relationship study of beta-carboline derivatives as haspin kinase inhibitors

    Structure–activity relationship study of beta-carboline derivatives as haspin kinase inhibitors за авторством Gregory D. Cuny, Natalia P. Ulyanova, Debasis Patnaik, Jifeng Liu, Xiangjie Lin, Ken Auerbach, Soumya S. Ray, Jun Xian, Marcie A. Glicksman, Ross L. Stein, Jonathan M.G. Higgins

    Опубліковано 2012
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  12. 12
    Structure Guided Design of Potent and Selective Ponatinib-Based Hybrid Inhibitors for RIPK1

    Structure Guided Design of Potent and Selective Ponatinib-Based Hybrid Inhibitors for RIPK1 за авторством Malek Najjar, Chalada Suebsuwong, Soumya S. Ray, Roshan J. Thapa, Jenny L. Maki, Shoko Nogusa, Saumil Shah, Danish Saleh, Peter J. Gough, John Bertin, Junying Yuan, Siddharth Balachandran, Gregory D. Cuny, Alexei Degterev

    Опубліковано 2015
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  13. 13
    Inflammatory Signaling by NOD-RIPK2 Is Inhibited by Clinically Relevant Type II Kinase Inhibitors

    Inflammatory Signaling by NOD-RIPK2 Is Inhibited by Clinically Relevant Type II Kinase Inhibitors за авторством Peter Canning, Qui Ruan, Tobias Schwerd, Matouš Hrdinka, Jenny L. Maki, Danish Saleh, Chalada Suebsuwong, Soumya S. Ray, Paul E. Brennan, Gregory D. Cuny, Holm H. Uhlig, Mads Gyrd‐Hansen, Alexei Degterev, Alex N. Bullock

    Опубліковано 2015
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  14. 14
    Discovery and Optimization of a STING Agonist Platform for Application in Antibody Drug Conjugates

    Discovery and Optimization of a STING Agonist Platform for Application in Antibody Drug Conjugates за авторством Jeremy R. Duvall, Joshua D. Thomas, Raghida A. Bukhalid, Kalli C. Catcott, K. W. Bentley, Scott D. Collins, Timothy K. Eitas, Brian Jones, Eugene Kelleher, Kelly L. Lancaster, Marina Protopopova, Soumya S. Ray, Elena Ter‐Ovanesyan, Ling Xu, Liping Yang, Jeffrey Zurita, Marc Damelin, Dorin Toader, Timothy B. Lowinger

    Опубліковано 2023
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  15. 15
    Structural genomics: A pipeline for providing structures for the biologist

    Structural genomics: A pipeline for providing structures for the biologist за авторством Mark R. Chance, Anne R. Bresnick, S.K. Burley, Jiansheng Jiang, Christopher D. Lima, Andrej Šali, Steven C. Almo, J.B. Bonanno, John A. Buglino, Simon J. Boulton, Hua Chen, Narayanan Eswar, Guo-Shun He, Raymond Y. Huang, Valentin Ilyin, Linda McMahan, Ursula Pieper, Soumya S. Ray, Marc Vidal, Li‐Kai Wang

    Опубліковано 2002
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