Marina Bukhtiyarova

Merck & Co., Inc., Rahway, NJ, USA (United States)

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Co-Authors

Alexey L. Nuzhdin

Boreskov Institute of Catalysis

G. A. Bukhtiyarova

Boreskov Institute of Catalysis

Eric B. Springman

Ansys (United States)

АС

А. С. Иванова

Karelian Research Centre

L. M. Plyasova

Boreskov Institute of Catalysis

Andrey V. Bukhtiyarov

Boreskov Institute of Catalysis

ВВ

В. В. Каичев

Boreskov Institute of Catalysis

H.V. Namboodiri

Ansys (United States)

Andrew Cooke

United States Department of the Treasury

Michael Karpusas

Agricultural University of Athens

Cooperative Institutions

Merck & Co., Inc., Rahway, NJ, USA (United States)

126

United States Military Academy

109

Boreskov Institute of Catalysis

Siberian Branch of the Russian Academy of Sciences

Russian Academy of Sciences

Novosibirsk State University

Ansys (United States)

University of Gothenburg

Technische Universität Braunschweig

Australian National University

Author Statistics

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Research Field

Phase composition and texture of Sr(La)Mn hexaaluminates

Kinetics and Catalysis (2009)

Marina Bukhtiyarova А. С. Иванова Г. С. Литвак L. M. Plyasova

Texture (cosmology)

Specific surface area

Thermal Treatment

10.1134/s0023158409060056

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Citations (3)

Transesterification of rapeseed oil under flow conditions catalyzed by basic solids: MAl(La)O (M=Sr, Ba), MMgO (M=Y, La)

Applied Catalysis A General (2012)

O. V. Sherstyuk А. С. Иванова M. Yu. Lebedev Marina Bukhtiyarova L. G. Matvienko

10.1016/j.apcata.2012.01.014

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Citations (13)

Inhibition of the Bovine Viral Diarrhoea Virus NS3 Serine Protease by a Boron-Modified Peptidyl Mimetic of its Natural Substrate

Antiviral chemistry & chemotherapy (2001)

Marina Bukhtiyarova Christopher J. Rizzo Charles A. Kettner Bruce D. Korant Helen Scarnati

Bovine viral diarrhoea virus (BVDV) is closely related to hepatitis C virus (HCV), and has been used as a surrogate virus in drug development for HCV infection. Similar to HCV, BVDV-encoded NS3 serine proteinase is responsible for multiple cleavages in the viral polyprotein, generating mature NS4A, NS4B, NS5A and NS5B proteins. NS3-dependent cleavage sites of BVDV contain a strictly conserved leucine at P1, and either serine or alanine at P1'. The full length BVDV NS3/4A serine protease has been cloned and expressed in bacterial cells. The enzyme has been purified from the soluble portion of Escherichia coli via a two-step purification procedure employing chromatography on heparin resin and gel filtration. The protease activity was characterized using in vitro translated BVDV NS4A/B and NS5A/B polyprotein substrates. A boronic acid analogue of the BVDV NS4A/NS4B cleavage site was synthesized and shown to be an efficient inhibitor of the NS3 serine protease in vitro. The compound, designated DPC-AB9144-00, inhibited approximately 75% of the NS3/4 activity at 10 microM with the NS4A/B substrate. However, no antiviral activity was detected with DPC-AB9144-00 in BVDV-infected Madin-Darby bovine kidney cells at concentrations as great as 90 pM, suggesting permeability or that other cellular-derived limitations were present.

NS3

NS2-3 protease

Pestivirus

NS5A

NS5B

MASP1

10.1177/095632020101200607

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Citations (24)

Crystal Structure of F169A p38 Kinase

M. Karpusas H.V. Namboodiri Marina Bukhtiyarova Eric B. Springman

10.2210/pdb2pkj/pdb

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Citations (0)

Two classes of p38α MAP kinase inhibitors having a common diphenylether core but exhibiting divergent binding modes

Bioorganic & Medicinal Chemistry Letters (2005)

Enrique L. Michelotti Kristofer K. Moffett Duyan Nguyen Martha J. Kelly Rupa Shetty

Moiety

Molecular model

10.1016/j.bmcl.2005.08.038

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Citations (32)

The rational design of a novel potent analogue of the 5′-AMP-activated protein kinase inhibitor compound C with improved selectivity and cellular activity

Bioorganic & Medicinal Chemistry Letters (2010)

Fouzia Machrouhi Nouara Ouhamou Keith R. Laderoute Joy M. Calaoagan Marina Bukhtiyarova

AMP-Activated Protein Kinase

Lead compound

10.1016/j.bmcl.2010.09.088

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Citations (20)

Performance of Ba-containing catalysts in the transesterification reaction of rapeseed oil with methanol under flow conditions

Catalysis Communications (2011)

А. С. Иванова O. V. Sherstyuk Marina Bukhtiyarova Р. Г. Кукушкин L. G. Matvienko

10.1016/j.catcom.2011.12.008

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Citations (8)

Characterization of non-active site TrkA selective kinase inhibitors and implications on obtaining kinase selectivity

Acta Crystallographica Section A Foundations and Advances (2017)

Hua-Poo Su Keith Rickert Christine Burlein Kartik Narayan Marina Bukhtiyarova

Current therapies for chronic pain can have insufficient efficacy and lead to side effects, necessitating research on novel targets against pain.Although originally identified as an oncogene, TrkA is linked to pain and elevated levels of NGF, the ligand for TrkA, are associated with chronic pain.Antibodies that block TrkA interaction with its ligand, NGF, are in clinical trials for pain relief.Here, we describe the identification of TrkA-specific inhibitors and the structural basis for their selectivity over other Trk family kinases.The x-ray structures reveal a novel binding site outside the kinase active site that utilizes residues from the kinase domain and the juxtamembrane region.Three modes of binding with the juxtamembrane region are characterized through a series of ligand-bound complexes.The structures indicate a critical pharmacophore on the compounds that leads to the distinct binding modes.The mode of interaction can allow TrkA selectivity over TrkB and TrkC or promiscuous, pan-Trk inhibition.This highlights the difficulty in characterizing the structure-activity relationship of a chemical series in the absence of structural information due to substantial differences in the interacting residues.These structures illustrate the flexibility of binding to sequences outside of, but adjacent to, the kinase domain of TrkA.This knowledge allows development of compounds with specificity for TrkA or the family of Trk proteins and has implications on obtaining selectivity for kinase targets in drug discovery.

10.1107/s0108767317098221

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Citations (0)

Cerastecins inhibit membrane lipooligosaccharide transport in drug-resistant Acinetobacter baumannii

Nature Microbiology (2024)

Hao Wang Andrii Ishchenko Jason W. Skudlarek Pamela Shen Liudmila Dzhekieva

Acinetobacter baumannii

Carbapenem

10.1038/s41564-024-01667-0

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Citations (7)

Identification of potent inhibitors of the sortilin-progranulin interaction