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Alexei V. Buevich
Researcher at Merck & Co.
Publications - 118
Citations - 1963
Alexei V. Buevich is an academic researcher from Merck & Co.. The author has contributed to research in topics: Chemistry & Psymberin. The author has an hindex of 23, co-authored 110 publications receiving 1594 citations. Previous affiliations of Alexei V. Buevich include Rutgers University & Russian Academy of Sciences.
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An orally available non-nucleotide STING agonist with antitumor activity
Bo-Sheng Pan,Samanthi A. Perera,Jennifer Piesvaux,Jeremy Presland,Gottfried K. Schroeder,Jared N. Cumming,B. Wesley Trotter,Michael D. Altman,Alexei V. Buevich,Brandon Cash,Saso Cemerski,Wonsuk Chang,Yiping Chen,Peter J. Dandliker,Guo Feng,Andrew M. Haidle,Timothy J. Henderson,James P. Jewell,Ilona Kariv,Ian Knemeyer,Johnny E. Kopinja,Brian M. Lacey,Jason Laskey,Charles A. Lesburg,Rui Liang,Brian Long,Min Lu,Yanhong Ma,Ellen C. Minnihan,Greg O’Donnell,Ryan D. Otte,Laura Price,Larissa Rakhilina,Berengere Sauvagnat,Sharad K. Sharma,Sriram Tyagarajan,Hyun Chong Woo,Daniel F. Wyss,Serena Xu,David Jonathan Bennett,George H. Addona +40 more
TL;DR: A previously unknown compound (MSA-2) that exhibits “closed” STING conformation and antitumor immunity is identified and identified in a phenotypic screen for chemical inducers of interferon-β secretion.
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LR-HSQMBC: A Sensitive NMR Technique To Probe Very Long-Range Heteronuclear Coupling Pathways
TL;DR: The LR-HSQMBC NMR experiment can be extended to provide data similar to that afforded by 1,n-ADEQUATE even in sample-limited situations by optimizing responses for very small (n)JCH coupings as opposed to relying on the markedly less sensitive detection of long-range coupled ( 13)C-(13)C homonuclear pairs at natural abundance.
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Chemoselective Peptide Modification via Photocatalytic Tryptophan β-Position Conjugation.
Younong Yu,Li-Kang Zhang,Alexei V. Buevich,Guoqing Li,Haiqun Tang,Petr Vachal,Steven L. Colletti,Zhi-Cai Shi +7 more
TL;DR: A chemoselective peptide modification method via photocatalytic tryptophan β-position conjugation has been discovered, providing a novel approach toward peptide modifications to support the discovery of new therapeutic peptides, protein labeling and bioconjugation.
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Backbone dynamics of the natively unfolded pro-peptide of subtilisin by heteronuclear NMR relaxation studies
TL;DR: The results suggest that PPS experiences a higher degree of correlated motion at pH 6.0 and that electrostatic interactions may be important for inducing correlated motions on the nanosecond timescale in unfolded PPS.
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Synergistic Combination of CASE Algorithms and DFT Chemical Shift Predictions: A Powerful Approach for Structure Elucidation, Verification, and Revision
TL;DR: This work has demonstrated that the proposed synergistic approach is an unbiased, reliable, and very efficient structure verification and de novo structure elucidation method that can be applied to difficult structural problems when other experimental methods would be difficult or impossible to use.