Igor Polikarpov

Research interests

Publications

• Carbohydrate binding modules enhance cellulose enzymatic hydrolysis by increasing access of cellulases to the substrate

  Carbohydrate Polymers · 2019 · 10.1016/j.carbpol.2019.01.108

• SAXSMoW 2.0: Online calculator of the molecular weight of proteins in dilute solution from experimental SAXS data measured on a relative scale

  Protein Science · 2018 · 10.1002/pro.3528

• Structural and compositional changes in sugarcane bagasse subjected to hydrothermal and organosolv pretreatments and their impacts on enzymatic hydrolysis

  Industrial Crops and Products · 2018 · 10.1016/j.indcrop.2018.01.014

• Structural diversity of carbohydrate esterases

  Biotechnology Research and Innovation · 2017 · 10.1016/j.biori.2017.02.001

• Efficient sugar production from sugarcane bagasse by microwave assisted acid and alkali pretreatment

  Biomass and Bioenergy · 2016 · 10.1016/j.biombioe.2016.06.017

• Quantitative 13C MultiCP solid-state NMR as a tool for evaluation of cellulose crystallinity index measured directly inside sugarcane biomass

  Biotechnology for Biofuels · 2015 · 10.1186/s13068-015-0292-1

• Multi-scale structural and chemical analysis of sugarcane bagasse in the process of sequential acid–base pretreatment and ethanol production by Scheffersomyces shehatae and Saccharomyces cerevisiae

  Biotechnology for Biofuels · 2014 · https://doi.org/10.1186/1754-6834-7-63

• Evaluating the composition and processing potential of novel sources of Brazilian biomass for sustainable biorenewables production

  Biotechnology for Biofuels · 2014 · 10.1186/1754-6834-7-10

• Effects of pretreatment on morphology, chemical composition and enzymatic digestibility of eucalyptus bark: a potentially valuable source of fermentable sugars for biofuel production – part 1

  Biotechnology for Biofuels · 2013 · 10.1186/1754-6834-6-75

• Molecular Mechanism of Peroxisome Proliferator-Activated Receptor α Activation by WY14643: a New Mode of Ligand Recognition and Receptor Stabilization

  Journal of Molecular Biology · 2013 · 10.1016/j.jmb.2013.05.010

• Medium Chain Fatty Acids Are Selective Peroxisome Proliferator Activated Receptor (PPAR) γ Activators and Pan-PPAR Partial Agonists

  PLoS ONE · 2012 · https://doi.org/10.1371/journal.pone.0036297

• Chemical and morphological characterization of sugarcane bagasse submitted to a delignification process for enhanced enzymatic digestibility

  Biotechnology for Biofuels · 2011 · https://doi.org/10.1186/1754-6834-4-54

• Enzymatic hydrolysis of pretreated sugar cane bagasse using Penicillium funiculosum and Trichoderma harzianum cellulases

  Process Biochemistry · 2011 · 10.1016/j.procbio.2011.01.022

• Dissecting structure–function–stability relationships of a thermostable GH5-CBM3 cellulase from Bacillus subtilis 168

  Biochemical Journal · 2011 · 10.1042/bj20110869

• Determination of the molecular weight of proteins in solution from a single small-angle X-ray scattering measurement on a relative scale

  Journal of Applied Crystallography · 2009 · https://doi.org/10.1107/s0021889809043076

• Structural Rearrangements in the Thyroid Hormone Receptor Hinge Domain and Their Putative Role in the Receptor Function

  Journal of Molecular Biology · 2006 · 10.1016/j.jmb.2006.05.008

• Crystal Structure of Exo-inulinase from Aspergillus awamori: The Enzyme Fold and Structural Determinants of Substrate Recognition

  Journal of Molecular Biology · 2004 · 10.1016/j.jmb.2004.09.024

• Average protein density is a molecular‐weight‐dependent function

  Protein Science · 2004 · https://doi.org/10.1110/ps.04688204

• Crystal Structure of Recombinant Human Interleukin-22

  Structure · 2002 · 10.1016/s0969-2126(02)00797-9

• The High Resolution Crystal Structure of Yeast Hexokinase PII with the Correct Primary Sequence Provides New Insights into Its Mechanism of Action

  Journal of Biological Chemistry · 2000 · 10.1074/jbc.m910412199

• The two types of 3-dehydroquinase have distinct structures but catalyze the same overall reaction.

  Nature Structural Biology · 1999 · 10.1038/9287

• β-Lactoglobulin

  International Dairy Journal · 1998 · 10.1016/s0958-6946(98)00021-1

• Bovine β-lactoglobulin at 1.8 Å resolution — still an enigmatic lipocalin

  Structure · 1997 · https://doi.org/10.1016/s0969-2126(97)00205-0

• Substrate binding is required for assembly of the active conformation of the catalytic site in Ntn amidotransferases: evidence from the 1.8 å crystal structure of the glutaminase domain of glucosamine 6-phosphate synthase

  Structure · 1996 · 10.1016/s0969-2126(96)00087-1

• Crystal structure of the extracellular region of human tissue factor

  Nature · 1994 · 10.1038/370662a0

Current projects

No projects listed.