I. Polikarpov

发表

Crystallization and preliminary X‐ray diffraction studies of isoform α1 of the human thyroid hormone receptor ligand‐binding domain

F. M. Nunes, R. Aparício, M. M. Santos, 2004 .

Molecular basis of the thermostability and thermophilicity of laminarinases: X-ray structure of the hyperthermostable laminarinase from Rhodothermus marinus and molecular dynamics simulations.

Thiago C. F. Gomes, Rodrigo L. Silveira, L. Martínez, 2011, The journal of physical chemistry. B.

Average protein density is a molecular‐weight‐dependent function

Igor Polikarpov, I. Polikarpov, H. Fischer, 2004, Protein science : a publication of the Protein Society.

Enzymatic versatility and thermostability of a new aryl-alcohol oxidase from Thermothelomyces thermophilus M77.

I. Polikarpov, M. Kadowaki, P. Higasi, 2020, Biochimica et biophysica acta. General subjects.

A review on bioprocessing of paddy straw to ethanol using simultaneous saccharification and fermentation

I. Polikarpov, Sachin Kumar, A. Chandel, 2019, Process Biochemistry.

Biophysical and biochemical studies of a major endoglucanase secreted by Xanthomonas campestris pv. campestris.

I. Polikarpov, Mario de Oliveira Neto, F. R. Rosseto, 2016, Enzyme and microbial technology.

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

I. Polikarpov, H. Fischer, A. Craievich, 2010 .

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

D. Macquarrie, I. Polikarpov, L. Gomez, 2016 .

Conformational differences between the wild type and V30M mutant transthyretin modulate its binding to genistein: implications to tetramer stability and ligand-binding.

J. Kelly, I. Polikarpov, D. Foguel, 2010, Journal of structural biology.

Liquid ammonia pretreatment optimization for improved release of fermentable sugars from sugarcane bagasse

J. G. Filgueiras, I. Polikarpov, Sachin Kumar, 2020 .

Nanoscale conformational ordering in polyanilines investigated by SAXS and AFM.

Igor Polikarpov, Osvaldo N Oliveira, L. Mattoso, 2007, Journal of colloid and interface science.

Mechanisms of peroxisome proliferator activated receptor γ regulation by non-steroidal anti-inflammatory drugs

Tuo Deng, Igor Polikarpov, Amanda Bernardes, 2015, Nuclear receptor signaling.

Recent Trends in Structure‐Based Drug Design and Energetics

I. Polikarpov, A. Andricopulo, R. Guido, 2010 .

Polymeric nanoparticles loaded with the 3,5,3'-triiodothyroacetic acid (Triac), a thyroid hormone: factorial design, characterization, and release kinetics.

I. Polikarpov, J. Fernandes, M. Forim, 2012, Nanotechnology, science and applications.

On the subtle tuneability of cellulose hydrogels: implications for binding of biomolecules demonstrated for CBM 1.

I. Polikarpov, J. Lowe, I Polikarpov, 2017, Journal of materials chemistry. B.

Enzymes for lignocellulosic biomass polysaccharide valorization and production of nanomaterials

I. Polikarpov, V. Pellegrini, Ana Gabriela Veiga Sepulchro, 2020 .

Comparison of different crystal forms of 3-dehydroquinase from Salmonella typhi and its implication for the enzyme activity.

Wen-Hwa Lee, Lindsay Sawyer, Igor Polikarpov, 2002, Acta crystallographica. Section D, Biological crystallography.

Thermal adaptation strategies of the extremophile bacterium Thermus filiformis based on multi-omics analysis

Diego Mauricio Riaño-Pachón, F. Squina, M. B. Couger, 2017, Extremophiles.

Catalytic mechanism of inulinase from Arthrobacter sp. S37.

Kyoung-Yun Kim, Igor Polikarpov, Su-Il Kim, 2008, Biochemical and biophysical research communications.

Purification, characterization, gene cloning and preliminary X-ray data of the exo-inulinase from Aspergillus awamori.

I. Polikarpov, A. Golubev, R. Wattiez, 2002, The Biochemical journal.

Preparation and characterization of polymeric nanoparticles loaded with the flavonoid luteolin, by using factorial design

I. Polikarpov, J. Fernandes, M. Forim, 2012 .

Identification of a novel ligand binding motif in the transthyretin channel.

Igor Polikarpov, I. Polikarpov, D. Foguel, 2010, Bioorganic & medicinal chemistry.

Crystal structures of Leptospira interrogans FAD-containing ferredoxin-NADP+ reductase and its complex with NADP+

I. Polikarpov, E. Ceccarelli, A. S. Nascimento, 2007, BMC Structural Biology.

Low-resolution envelope, biophysical analysis and biochemical characterization of a short-chain specific and halotolerant carboxylesterase from Bacillus licheniformis.

I. Polikarpov, A. S. Nascimento, M. Kadowaki, 2018, International journal of biological macromolecules.

Low-Resolution Molecular Models Reveal the Oligomeric State of the PPAR and the Conformational Organization of Its Domains in Solution

P. Webb, I. Polikarpov, Mario de Oliveira Neto, 2012, PloS one.

Preliminary X-ray diffraction studies of rabbit muscle triose phosphate isomerase (TIM).

R. Aparício, I. Polikarpov, S. Ferreira, 2000, Acta crystallographica. Section D, Biological crystallography.

INVESTIGATION OF POROSITY, WETTABILITY AND MORPHOLOGY OF THE CHEMICALLY PRETREATED SUGARCANE BAGASSE

I. Polikarpov, P. Crnkovic, G. Cruz, 2013 .

Biological Crystallography Protein Crystal Structure Solution by Fast Incorporation of Negatively and Positively Charged Anomalous Scatterers

Z. Dauter, I. Polikarpov, R. Nagem, 2022 .

Recent advances in the enzymatic production and applications of xylooligosaccharides

I. Polikarpov, V. Pellegrini, Ana Gabriela Veiga Sepulchro, 2021, World Journal of Microbiology and Biotechnology.

β-Lactoglobulin: Structural Studies, Biological Clues

Su-Ying Wu, I. Polikarpov, L. Sawyer, 1998 .

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

I. Polikarpov, C. Rosa, S. S. da Silva, 2014, Biotechnology for Biofuels.

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

E. deAzevedo, I. Polikarpov, L. Gomez, 2013, Biotechnology for Biofuels.

The structure of the D49 phospholipase A2 piratoxin III from Bothrops pirajai reveals unprecedented structural displacement of the calcium-binding loop: possiblerelationship to cooperative substrate binding.

D. Rigden, I. Polikarpov, S. Marangoni, 2003, Acta crystallographica. Section D, Biological crystallography.

Structural modeling of high-affinity thyroid receptor–ligand complexes

L. Martínez, I. Polikarpov, M. Skaf, 2010, European Biophysics Journal.

Crystal structure of the extracellular region of human tissue factor

D. Stuart, I. Polikarpov, E. Jones, 1994, Nature.

Biochemical characterization, low-resolution SAXS structure and an enzymatic cleavage pattern of BlCel48 from Bacillus licheniformis.

I. Polikarpov, M. Kadowaki, E. A. de Araújo, 2017, International journal of biological macromolecules.

Crystal structure of the extracellular region of human tissue factor

D. Stuart, I. Polikarpov, E. Jones, 1994, Nature.

Environments of the four tryptophans in the extracellular domain of human tissue factor: comparison of results from absorption and fluorescence difference spectra of tryptophan replacement mutants with the crystal structure of the wild-type protein.

C. A. Hasselbacher, I. Polikarpov, A. Guha, 1995, Biophysical journal.

Crystallization and preliminary X-ray diffraction analysis of a new xyloglucanase from Xanthomonas campestris pv. campestris.

I. Polikarpov, M. Murakami, M. Kadowaki, 2013, Acta crystallographica. Section F, Structural biology and crystallization communications.

Potential of oleaginous yeast Trichosporon sp., for conversion of sugarcane bagasse hydrolysate into biodiesel.

B S Chadha, Igor Polikarpov, I. Polikarpov, 2017, Bioresource technology.

Structure, Substrate Complexation and Reaction Mechanism of Bacterial Asparaginases

I. Polikarpov, M. Sanches, S. Krauchenco, 2007 .

BIOTECHNOLOGICALLY RELEVANT ENZYMES AND PROTEINS Functional characterization of a novel thermophilic exo-arabinanase from Thermothielavioides terrestris

F. Squina, I. Polikarpov, Josman Velasco, 2020 .

Structural insights into the hydrolysis pattern and molecular dynamics simulations of GH45 subfamily a endoglucanase from Neurospora crassa OR74A.

I. Polikarpov, M. Kadowaki, 2019, Biochimie.

Isolation and characterization of a β-galactosidase from a new Amazon forest strain of Aspergillus niger as a potential accessory enzyme for biomass conversion

I. Polikarpov, A. Golubev, C. Farinas, 2014 .

Multifaceted characterization of sugarcane bagasse under different steam explosion severity conditions leading to distinct enzymatic hydrolysis yields

E. deAzevedo, I. Polikarpov, A. Chandel, 2019, Industrial Crops and Products.

Design of an enzyme cocktail consisting of different fungal platforms for efficient hydrolysis of sugarcane bagasse: Optimization and synergism studies

I. Polikarpov, N. Pereira, Johanna Méndez Arias, 2016, Biotechnology progress.

Non-productive adsorption of bacterial β-glucosidases on lignins is electrostatically modulated and depends on the presence of fibronection type III-like domain.

F. Squina, I. Polikarpov, V. M. da Silva, 2016, Enzyme and microbial technology.

Combination of Sodium Hydroxide and Lime as a Pretreatment for Conversion of Date Palm Leaves into a Promising Ruminant Feed: An Optimization Approach

F. Ahmadi, I. Polikarpov, A. Rajaee Rad, 2015 .

Side by Side Comparison of Chemical Compounds Generated by Aqueous Pretreatments of Maize Stover, Miscanthus and Sugarcane Bagasse

L. Trindade, I. Polikarpov, W. Boerjan, 2014, BioEnergy Research.

Mapping the lignin distribution in pretreated sugarcane bagasse by confocal and fluorescence lifetime imaging microscopy

I. Polikarpov, C. A. Rezende, F. Guimarães, 2013, Biotechnology for Biofuels.

Physical techniques shed light on the differences in sugarcane bagasse structure subjected to steam explosion pretreatments at equivalent combined severity factors

E. deAzevedo, I. Polikarpov, L. Ramos, 2020 .

Short communication: investigating the effect of saffron (Crocus sativus L.) nano-sizing on its colour extraction efficiency: a preliminary study

I. Polikarpov, M. Sadeghi, M. Karbasi, 2017, Natural product research.

Structural Insights into Human Peroxisome Proliferator Activated Receptor Delta (PPAR-Delta) Selective Ligand Binding

P. Webb, I. Polikarpov, D. Trivella, 2012, PloS one.

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

E. deAzevedo, I. Polikarpov, C. A. Rezende, 2015, Biotechnology for Biofuels.

Biochemical characterization and low-resolution SAXS structure of two-domain endoglucanase BlCel9 from Bacillus licheniformis

I. Polikarpov, Mario de Oliveira Neto, E. A. de Araújo, 2018, Applied Microbiology and Biotechnology.

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

I. Polikarpov, A. Craievich, Vassili Piiadov, 2018, Protein science : a publication of the Protein Society.

Mode of PPAR γ activation by luteolin

Rodrigo L. Silveira, P. Webb, I. Polikarpov, 2012 .

Biochemical and structural insights into a thermostable cellobiohydrolase from Myceliophthora thermophila

I. Polikarpov, M. Kadowaki, P. Higasi, 2018, The FEBS journal.

Expression, purification, crystallization and preliminary X-ray diffraction analysis of Aspergillus terreus endo-β-1,4-glucanase from glycoside hydrolase family 12.

I. Polikarpov, F. Segato, J. Muniz, 2014, Acta crystallographica. Section F, Structural biology communications.

Structural diversity of carbohydrate esterases

I. Polikarpov, A. S. Nascimento, A. M. Nakamura, 2017 .

Cellulose nanofibers production using a set of recombinant enzymes.

I. Polikarpov, C. A. Rezende, V. Mastelaro, 2020, Carbohydrate polymers.

Purification, crystallization and preliminary X-ray study of beta-xylosidase from Trichoderma reesei.

I. Polikarpov, A. Golubev, E. Eneyskaya, 2000, Acta crystallographica. Section D, Biological crystallography.

Conformational variability of the stationary phase survival protein E from Xylella fastidiosa revealed by X‐ray crystallography, small‐angle X‐ray scattering studies, and normal mode analysis

R. Aparício, I. Polikarpov, M. A. D. de Toledo, 2017, Proteins.

Crystal structure of a small heat-shock protein from Xylella fastidiosa reveals a distinct high-order structure.

R. Aparício, I. Polikarpov, M. A. D. de Toledo, 2017, Acta crystallographica. Section F, Structural biology communications.

Crystal structure of β1→6‐galactosidase from Bifidobacterium bifidum S17: trimeric architecture, molecular determinants of the enzymatic activity and its inhibition by α‐galactose

I. Polikarpov, A. S. Nascimento, M. Murakami, 2016, The FEBS journal.

Crystal structure of a putative exo-β-1,3-galactanase from Bifidobacterium bifidum S17.

I. Polikarpov, A. Godoy, C. Camilo, 2015, Acta crystallographica. Section F, Structural biology communications.

Structural dataset for the PPARγ V290M mutant

P. Webb, I. Polikarpov, A. C. Puhl, 2016, Data in brief.

Crystallization and preliminary X-ray diffraction analysis of a novel trypsin inhibitor from seeds of Copaifera langsdorffii.

I. Polikarpov, R. Nagem, S. Marangoni, 2001, Acta crystallographica. Section D, Biological crystallography.

Probing conformational changes in orphan nuclear receptor: the NGFI-B intermediate is a partially unfolded dimer.

R. Portugal, I. Polikarpov, Mario de Oliveira Neto, 2008, Biophysical chemistry.

Development and validation of a fast RP-HPLC method to determine the analogue of the thyroid hormone, 3,5,3′-triiodothyroacetic acid (TRIAC), in polymeric nanoparticles

V. Zucolotto, I. Polikarpov, M. F. G. F. Silva, 2011 .

Crystal structure of alpha-galactosidase from Trichoderma reesei and its complex with galactose: implications for catalytic mechanism.

A. N. Savel'ev, I. Polikarpov, A. Golubev, 2004, Journal of molecular biology.

Biochemical and biophysical characterization of novel GH10 xylanase prospected from a sugar cane bagasse compost-derived microbial consortia.

I. Polikarpov, M. Kadowaki, D. E. Evangelista, 2018, International journal of biological macromolecules.

Mapping the intramolecular vibrational energy flow in proteins reveals functionally important residues

L. Martínez, P. Webb, I. Polikarpov, 2011 .

Biomass as a Feedstock

A. J. Hunt, A. Matharu, I. Polikarpov, 2015 .

The stability and aggregation properties of the GTPase domain from human SEPT4.

I. Polikarpov, Mario de Oliveira Neto, W. Garcia, 2008, Biochimica et biophysica acta.

Effects of 3,5,3′-Triiodothyroacetic Acid, Nanoencapsulated or Not, on Intact and Atrophic Skin in Rats

V. Zucolotto, I. Polikarpov, J. Cancino, 2014 .

Crystallization and preliminary diffraction data of neurotoxin Ts-gamma from the venom of the scorpion Tityus serrulatus.

I. Polikarpov, A. Golubev, S. Marangoni, 1998, Acta crystallographica. Section D, Biological crystallography.

Crystallization and synchrotron X-ray diffraction studies of human interleukin-22.

J. Renauld, I. Polikarpov, R. Nagem, 2002, Acta crystallographica. Section D, Biological crystallography.

Expression, purification, crystallization and preliminary X-ray diffraction analysis of Bifidobacterium adolescentis xylose isomerase.

I. Polikarpov, A. Bernardes, C. V. dos Reis, 2013, Acta crystallographica. Section F, Structural biology and crystallization communications.

Thermal and Morphological Evaluation of Chemically Pretreated Sugarcane Bagasse

I. Polikarpov, P. Crnkovic, G. Cruz, 2013 .

The structure of the extended E2 DNA‐binding domain of the bovine papillomavirus‐1

I. Polikarpov, G. de Prat-Gay, J. Barbosa, 2020, Proteins.

Quantitative structure-activity relationships for a series of selective estrogen receptor-beta modulators

I. Polikarpov, A. Andricopulo, L. B. Salum, 2007, SAR and QSAR in environmental research.

The Characterization of the Endoglucanase Cel12A from Gloeophyllum trabeum Reveals an Enzyme Highly Active on β-Glucan

I. Polikarpov, A. Tsang, A. Bernardes, 2014, PloS one.

Analysis of carbohydrate-active enzymes in Thermogemmatispora sp. strain T81 reveals carbohydrate degradation ability.

B. Henrissat, I. Polikarpov, R. Sparling, 2018, Canadian journal of microbiology.

Crystal structure of the IL-22/IL-22R1 complex

J. Renauld, I. Polikarpov, L. Bleicher, 2008 .

Crystallization and preliminary X-ray diffraction analysis of endoglucanase III from Trichoderma harzianum.

I. Polikarpov, F. Henrique-Silva, W. Malagó, 2012, Acta crystallographica. Section F, Structural biology and crystallization communications.

Purification, crystallization and preliminary crystallographic analysis of peroxidase from the palm tree Chamaerops excelsa.

V. Shnyrov, G. Zhadan, I. Polikarpov, 2011, Acta crystallographica. Section F, Structural biology and crystallization communications.

Pressure denaturation of β‐lactoglobulin

I. Polikarpov, S. Ferreira, V. L. Valente-Mesquita, 2000 .

Pressure denaturation of beta-lactoglobulin. Different stabilities of isoforms A and B, and an investigation of the Tanford transition.

I. Polikarpov, S. Ferreira, V. L. Valente-Mesquita, 2000, European journal of biochemistry.

Crystallization and preliminary X-ray diffraction analysis of human IL-22 bound to its soluble decoy receptor IL-22BP.

J. Renauld, I. Polikarpov, A. S. Nascimento, 2009, Acta crystallographica. Section F, Structural biology and crystallization communications.

Purification, crystallization and preliminary X-ray diffraction analysis of royal palm tree (Roystonea regia) peroxidase.

V. Shnyrov, I. Polikarpov, A. S. Nascimento, 2007, Acta crystallographica. Section F, Structural biology and crystallization communications.

Crystallization and preliminary X-ray crystallographic analysis of the heterodimeric crotoxin complex and the isolated subunits crotapotin and phospholipase A2.

I. Polikarpov, R. Arni, M. Murakami, 2007, Acta crystallographica. Section F, Structural biology and crystallization communications.

Crystallization and preliminary X-ray diffraction studies of ferredoxin reductase from Leptospira interrogans.

I. Polikarpov, E. Ceccarelli, A. S. Nascimento, 2006, Acta crystallographica. Section F, Structural biology and crystallization communications.

Purification, crystallization and preliminary diffraction study of beta-galactosidase from Penicillium sp.

I. Polikarpov, A. Golubev, E. Eneyskaya, 2000, Acta crystallographica. Section D, Biological crystallography.

Crystallization and preliminary X-ray diffraction analysis of the catalytic subunit of ADP-glucose pyrophosphorylase from potato tuber.

I. Polikarpov, J. Preiss, R. Arni, 2000, Acta crystallographica. Section D, Biological crystallography.

Crystallization and preliminary crystal analysis of yeast hexokinase PI and PII.

I. Polikarpov, A. Golubev, P. Kuser, 1999, Acta crystallographica. Section D, Biological crystallography.

Crystallization and preliminary X-ray diffraction studies of human catalase.

R. Aparício, I. Polikarpov, R. Nagem, 1999, Acta crystallographica. Section D, Biological crystallography.

Crystallization and preliminary diffraction studies of a recombinant major urinary protein.

I. Polikarpov, S. Krauchenco, P. Kuser, 1999, Acta crystallographica. Section D, Biological crystallography.

Crystallization and preliminary X-ray diffraction studies of piratoxin III, a D-49 phospholipase A2 from the venom of Bothrops pirajai.

I. Polikarpov, A. Soares, S. Marangoni, 1999, Acta crystallographica. Section D, Biological crystallography.

Crystallization and preliminary X-ray diffraction studies of piratoxin II, a phospholipase A2 isolated from the venom of Bothrops pirajai.

I. Polikarpov, S. Marangoni, M. Toyama, 1998, Acta crystallographica. Section D, Biological crystallography.

Crystal structure of the IL‐22/IL‐22R1 complex and its implications for the IL‐22 signaling mechanism

J. Renauld, I. Polikarpov, L. Bleicher, 2008, FEBS letters.

Multienzyme Cellulose Films as Sustainable and Self-Degradable Hydrogen Peroxide-Producing Material.

I. Polikarpov, K. Edler, D. Mattia, 2020, Biomacromolecules.

SAXS Studies of the Endoglucanase Cel12A from Gloeophyllum trabeum Show Its Monomeric Structure and Reveal the Influence of Temperature on the Structural Stability of the Enzyme

I. Polikarpov, Mario de Oliveira Neto, L. S. Miotto, 2014, Materials.

Simulated Annealing of Two Electron Density Solution Systems

I. Polikarpov, Y. Mascarenhas, M. O. Neto, 2008 .

Crystal structure of the Kunitz (STI)-type inhibitor from Delonix regia seeds.

I. Polikarpov, S. Marangoni, S. Krauchenco, 2003, Biochemical and biophysical research communications.

Herbaspirillum seropedicae signal transduction protein PII is structurally similar to the enteric GlnK.

I. Polikarpov, M. Buck, F. Pedrosa, 2002, European journal of biochemistry.

3D QSAR comparative molecular field analysis on nonsteroidal farnesoid X receptor activators.

I. Polikarpov, A. Andricopulo, K. M. Honorio, 2007, Journal of molecular graphics & modelling.

Differential effects of TR ligands on hormone dissociation rates: Evidence for multiple ligand entry/exit pathways

J. Baxter, P. Webb, I. Polikarpov, 2009, The Journal of Steroid Biochemistry and Molecular Biology.

Structural basis of GC-1 selectivity for thyroid hormone receptor isoforms

L. Martínez, F. M. Nunes, R. Aparício, 2008, BMC Structural Biology.

Family 1 carbohydrate binding-modules enhance saccharification rates

I. Polikarpov, B. L. Mello, 2014, AMB Express.

Biochemical characterization and low-resolution SAXS structure of two-domain endoglucanase BlCel9 from Bacillus licheniformis

I. Polikarpov, Mario de Oliveira Neto, E. A. de Araújo, 2018, Applied Microbiology and Biotechnology.

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

E. deAzevedo, I. Polikarpov, W. Garcia, 2011, Biotechnology for biofuels.

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

F. Squina, I. Polikarpov, R. Ward, 2012, The Biochemical journal.

Structural features of lignin obtained at different alkaline oxidation conditions from sugarcane bagasse

A. R. Gonçalves, I. Polikarpov, A. Craievich, 2012 .

Unlocking the structural features for the xylobiohydrolase activity of an unusual GH11 member identified in a compost‐derived consortium

I. Polikarpov, P. Dupree, T. Tryfona, 2021, Biotechnology and bioengineering.

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

I. Polikarpov, A. Castro, R. N. Maeda, 2011 .

Biochemical characterization and low-resolution SAXS structure of an exo-polygalacturonase from Bacillus licheniformis.

I. Polikarpov, M. Kadowaki, E. A. de Araújo, 2018, New biotechnology.

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

Igor Polikarpov, E. deAzevedo, I. Polikarpov, 2014, Biotechnology for Biofuels.

Crystal structure of exo-inulinase from Aspergillus awamori: the enzyme fold and structural determinants of substrate recognition.

I. Polikarpov, A. Rojas, A. Golubev, 2004, Journal of molecular biology.

Transcriptome Profile of Trichoderma harzianum IOC-3844 Induced by Sugarcane Bagasse

I. Polikarpov, R. Vicentini, R. Kuroshu, 2014, PloS one.

Structure-based identification of novel PPAR gamma ligands.

I. Polikarpov, A. S. Nascimento, A. Mafud, 2013, Bioorganic & medicinal chemistry letters.

Doping in poly(o-ethoxyaniline) nanostructured films studied with atomic force spectroscopy (AFS).

L. Mattoso, I. Polikarpov, O. N. Oliveira, 2008, Micron.

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

I. Polikarpov, J. Littlechild, M. Isupov, 1996, Structure.

Involvement of the C terminus in intramolecular nitrogen channeling in glucosamine 6-phosphate synthase: evidence from a 1.6 A crystal structure of the isomerase domain.

I. Polikarpov, A. Teplyakov, G. Obmolova, 1998, Structure.

Crystal structure of recombinant human interleukin-22.

J. Renauld, I. Polikarpov, C. Ogata, 2002, Structure.

Sugarcane waste as a valuable source of lipophilic molecules

A. J. Hunt, J. Clark, I. Polikarpov, 2015 .

Mode of Peroxisome Proliferator-Activated Receptor γ Activation by Luteolin

Igor Polikarpov, Ana C Puhl, Amanda Bernardes, 2012, Molecular Pharmacology.

Characterization of a New Glyoxal Oxidase from the Thermophilic Fungus Myceliophthora thermophila M77: Hydrogen Peroxide Production Retained in 5-Hydroxymethylfurfural Oxidation

I. Polikarpov, A. Costa-Filho, M. Kadowaki, 2018, Catalysts.

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

Darren R. Flower, Lindsay Sawyer, Igor Polikarpov, 1997 .

Thermodynamic characterization of the palm tree Roystonea regia peroxidase stability.

V. Shnyrov, J. Calvete, L. Sanz, 2008, Biochimie.

Hemocyanin facilitates lignocellulose digestion by wood-boring marine crustaceans

J. G. Filgueiras, I. Polikarpov, P. Dupree, 2018, Nature Communications.

Substrate specificity of the Chamaerops excelsa palm tree peroxidase. A steady-state kinetic study

V. Shnyrov, G. Zhadan, J. Calvete, 2012 .

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

Leandro Martínez, Tuo Deng, Alessandro S. Nascimento, 2012, PloS one.

Crystal structures of beta-galactosidase from Penicillium sp. and its complex with galactose.

I. Polikarpov, A. Rojas, A. Golubev, 2004, Journal of molecular biology.

GH43 endo-arabinanase from Bacillus licheniformis: Structure, activity and unexpected synergistic effect on cellulose enzymatic hydrolysis.

J. G. Filgueiras, I. Polikarpov, A. S. Nascimento, 2018, International journal of biological macromolecules.

Targeted metatranscriptomics of compost-derived consortia reveals a GH11 exerting an unusual exo-1,4-β-xylanase activity

E. deAzevedo, I. Polikarpov, D. Riaño-Pachón, 2017, Biotechnology for Biofuels.

Three-dimensional structure of an unusual Kunitz (STI) type trypsin inhibitor from Copaifera langsdorffii.

I. Polikarpov, R. Nagem, S. Marangoni, 2004, Biochimie.

Dissecting the Relation between a Nuclear Receptor and GATA: Binding Affinity Studies of Thyroid Hormone Receptor and GATA2 on TSHβ Promoter

I. Polikarpov, D. Veprintsev, Guilherme M. Santos, 2010, PloS one.

Molecular characterization of a family 5 glycoside hydrolase suggests an induced-fit enzymatic mechanism

Rodrigo L. Silveira, I. Polikarpov, E. Prates, 2016, Scientific Reports.

Recognition by the thyroid hormone receptor of canonical DNA response elements.

I. Polikarpov, L. Lima, A. T. Ranzani, 2010, Biochemistry.

Crystallization and preliminary X-ray study of haem-binding protein from the bloodsucking insect Rhodnius prolixus.

I. Polikarpov, R. Nagem, M. Sorgine, 2001, Acta crystallographica. Section D, Biological crystallography.

Expression, purification, and characterization of rat protein tyrosine phosphatase η catalytic domain

A. Fusco, R. Portugal, I. Polikarpov, 2005 .

Closed conformation of the active site loop of rabbit muscle triosephosphate isomerase in the absence of substrate: evidence of conformational heterogeneity.

Igor Polikarpov, R. Aparício, I. Polikarpov, 2003, Journal of molecular biology.

Molecular mechanism of peroxisome proliferator-activated receptor α activation by WY14643: a new mode of ligand recognition and receptor stabilization.

Clarisse G. Ricci, P. Webb, I. Polikarpov, 2013, Journal of molecular biology.

Flavonoid interactions with human transthyretin: combined structural and thermodynamic analysis.

I. Polikarpov, D. Foguel, L. Lima, 2012, Journal of structural biology.

The binding of synthetic triiodo l-thyronine analogs to human transthyretin: molecular basis of cooperative and non-cooperative ligand recognition.

I. Polikarpov, D. Foguel, L. Lima, 2011, Journal of structural biology.

Statistical coupling analysis of aspartic proteinases based on crystal structures of the Trichoderma reesei enzyme and its complex with pepstatin A.

A. Wlodawer, A. Gustchina, I. Polikarpov, 2008, Journal of molecular biology.

Response to Moras et al.

I. Polikarpov, V. Ollendorff, F. Rastinejad, 2015, Trends in biochemical sciences.

Nuclear receptor full-length architectures: confronting myth and illusion with high resolution.

I. Polikarpov, V. Ollendorff, F. Rastinejad, 2015, Trends in biochemical sciences.

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

Lindsay Sawyer, Igor Polikarpov, N. Isaacs, 1999, Nature Structural Biology.

Revealing the insoluble metasecretome of lignocellulose-degrading microbial communities

I. Polikarpov, N. Bruce, Yi Li, 2017, Scientific Reports.

The X-ray structure of a recombinant major urinary protein at 1.75 A resolution. A comparative study of X-ray and NMR-derived structures.

I. Polikarpov, L. Franzoni, A. Spisni, 2001, Acta crystallographica. Section D, Biological crystallography.

Essential Metabolic Routes as a Way to ESKAPE From Antibiotic Resistance

I. Polikarpov, C. Wrenger, A. S. Nascimento, 2019, bioRxiv.

Insights into the dual cleavage activity of the GH16 laminarinase enzyme class on β-1,3 and β-1,4 glycosidic bonds

F. Squina, I. Polikarpov, M. Skaf, 2021, The Journal of biological chemistry.

Three-Dimensional Structure of the Fab from a Human IgM Cold Agglutinin1

B. Braden, R. Aparício, I. Polikarpov, 2000, The Journal of Immunology.

Insights into the structure and function of fungal β‐mannosidases from glycoside hydrolase family 2 based on multiple crystal structures of the Trichoderma harzianum enzyme

R. Aparício, I. Polikarpov, A. S. Nascimento, 2014, The FEBS journal.

Aspergillus niger β-Glucosidase Has a Cellulase-like Tadpole Molecular Shape

F. Squina, I. Polikarpov, E. Prates, 2013, The Journal of Biological Chemistry.

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

E. deAzevedo, I. Polikarpov, A. Curvelo, 2018 .

Paludibacter propionicigenes GH10 xylanase as a tool for enzymatic xylooligosaccharides production from heteroxylans.

I. Polikarpov, V. Arantes, A. Curvelo, 2022, Carbohydrate polymers.

Structure and function of interleukin-22 and other members of the interleukin-10 family

J. Renauld, I. Polikarpov, L. Dumoutier, 2010, Cellular and Molecular Life Sciences.

Side by Side Comparison of Chemical Compounds Generated by Aqueous Pretreatments of Maize Stover, Miscanthus and Sugarcane Bagasse

L. Trindade, I. Polikarpov, W. Boerjan, 2014, BioEnergy Research.

Light-stimulated T. thermophilus two-domain LPMO9H: Low-resolution SAXS model and synergy with cellulases.

I. Polikarpov, Josman Velasco, F. Segato, 2021, Carbohydrate polymers.

Functional characterization of a lytic polysaccharide monooxygenase from the thermophilic fungus Myceliophthora thermophila

I. Polikarpov, A. Costa-Filho, V. Eijsink, 2018, PloS one.

Defining functional diversity for lignocellulose degradation in a microbial community using multi-omics studies

E. deAzevedo, I. Polikarpov, N. Bruce, 2018, Biotechnology for Biofuels.

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

I. Polikarpov, J. Scott, V. Pellegrini, 2019, Carbohydrate polymers.

Xyloglucan processing machinery in Xanthomonas pathogens and its role in the transcriptional activation of virulence factors

G. F. Persinoti, F. Gozzo, I. Polikarpov, 2021, Nature Communications.

Crystal structure of a soluble decoy receptor IL‐22BP bound to interleukin‐22

J. Renauld, I. Polikarpov, L. Bleicher, 2009, FEBS letters.

Functional Characterization and Low-Resolution Structure of an Endoglucanase Cel45A from the Filamentous Fungus Neurospora crassa OR74A: Thermostable Enzyme with High Activity Toward Lichenan and β-Glucan

I. Polikarpov, M. Kadowaki, C. Camilo, 2015, Molecular Biotechnology.

Interleukin-22 and its crystal structure.

J. Renauld, I. Polikarpov, R. Nagem, 2006, Vitamins and hormones.

Biochemical characterization and low-resolution SAXS shape of a novel GH11 exo-1,4-β-xylanase identified in a microbial consortium

I. Polikarpov, N. Bruce, S. McQueen-Mason, 2019, Applied Microbiology and Biotechnology.

Structure and dynamics of Trichoderma harzianum Cel7B suggest molecular architecture adaptations required for a wide spectrum of activities on plant cell wall polysaccharides.

I. Polikarpov, A. S. Nascimento, M. Kadowaki, 2019, Biochimica et biophysica acta. General subjects.

Functional characterization and comparative analysis of two heterologous endoglucanases from diverging subfamilies of glycosyl hydrolase family 45.

I. Polikarpov, Josman Velasco, F. Segato, 2019, Enzyme and microbial technology.

Structure, computational and biochemical analysis of PcCel45A endoglucanase from Phanerochaete chrysosporium and catalytic mechanisms of GH45 subfamily C members

Rodrigo L. Silveira, Caroline S. Pereira, I. Polikarpov, 2018, Scientific Reports.

Cloning, heterologous expression and biochemical characterization of a non-specific endoglucanase family 12 from Aspergillus terreus NIH2624.

F. Squina, I. Polikarpov, A. Damasio, 2017, Biochimica et biophysica acta. Proteins and proteomics.

Biochemical Characterization and Low-Resolution SAXS Molecular Envelope of GH1 β-Glycosidase from Saccharophagus degradans

S. R. Marana, I. Polikarpov, H. Brognaro, 2016, Molecular Biotechnology.

A Novel Member of GH16 Family Derived from Sugarcane Soil Metagenome

F. Squina, I. Polikarpov, T. Alvarez, 2015, Applied Biochemistry and Biotechnology.

High-throughput cloning, expression and purification of glycoside hydrolases using Ligation-Independent Cloning (LIC).

I. Polikarpov, C. Camilo, 2014, Protein expression and purification.

Crystallization and preliminary diffraction analysis of the catalytic domain of major extracellular endoglucanase from Xanthomonas campestris pv. campestris.

I. Polikarpov, Maxuel O. Andrade, F. R. Rosseto, 2013, Acta crystallographica. Section F, Structural biology and crystallization communications.

Recombinant Trichoderma harzianum endoglucanase I (Cel7B) is a highly acidic and promiscuous carbohydrate-active enzyme

F. Squina, I. Polikarpov, C. A. Rezende, 2015, Applied Microbiology and Biotechnology.

Effect of pH and temperature on the global compactness, structure, and activity of cellobiohydrolase Cel7A from Trichoderma harzianum

I. Polikarpov, Francieli Colussi, W. Garcia, 2011, European Biophysics Journal.

Impact of cellulose properties on enzymatic degradation by bacterial GH48 enzymes: Structural and mechanistic insights from processive Bacillus licheniformis Cel48B cellulase.

I. Polikarpov, M. Skaf, L. Ramos, 2021, Carbohydrate polymers.

Crystal structures of bovine beta-lactoglobulin in the orthorhombic space group C222(1). Structural differences between genetic variants A and B and features of the Tanford transition.

I. Polikarpov, L. Sawyer, S. Ferreira, 2001, European journal of biochemistry.

Orphan nuclear receptor NGFI‐B forms dimers with nonclassical interface

R. Portugal, I. Polikarpov, L. Bleicher, 2007, Protein science : a publication of the Protein Society.

An alternative conformation of ERβ bound to estradiol reveals H12 in a stable antagonist position

I. Polikarpov, A. S. Nascimento, M. Skaf, 2017, Scientific Reports.

Crystal structure of an unusual Kunitz-type trypsin inhibitor from Copaifera langsdorffii seeds

I. Polikarpov, R. Nagem, S. Marangoni, 2004 .

Low-resolution structure and fluorescence anisotropy analysis of protein tyrosine phosphatase eta catalytic domain.

A. Fusco, I. Polikarpov, L. Lima, 2007, Biophysical journal.

Ligand induced interaction of thyroid hormone receptor beta with its coregulators

Igor Polikarpov, I. Polikarpov, R. Garratt, 2008, The Journal of Steroid Biochemistry and Molecular Biology.

RXR agonist modulates TR: corepressor dissociation upon 9-cis retinoic acid treatment.

I. Polikarpov, J. Xavier-Neto, Juliana Fattori, 2015, Molecular Endocrinology.

Draft Genome Sequence of the Thermophile Thermus filiformis ATCC 43280, Producer of Carotenoid-(Di)glucoside-Branched Fatty Acid (Di)esters and Source of Hyperthermostable Enzymes of Biotechnological Interest

F. Squina, M. B. Couger, I. Polikarpov, 2015, Genome Announcements.

Xanthomonas campestris expansin-like X domain is a structurally disordered beta-sheet macromolecule capable of synergistically enhancing enzymatic efficiency of cellulose hydrolysis

I. Polikarpov, M. Oliveira Neto, L. G. Dolce, 2015, Biotechnology Letters.

Stability of L-asparaginase: an enzyme used in leukemia treatment.

I. Polikarpov, J. Abrahão-Neto, A. Stecher, 1999, Pharmaceutica acta Helvetiae.

Structural comparison of Escherichia coli L-asparaginase in two monoclinic space groups.

Igor Polikarpov, I. Polikarpov, J. Barbosa, 2003, Acta crystallographica. Section D, Biological crystallography.

Nutrient availability shapes the microbial community structure in sugarcane bagasse compost-derived consortia

I. Polikarpov, N. Bruce, S. McQueen-Mason, 2016, Scientific Reports.

Cloning, purification, crystallization and preliminary X-ray studies of a carbohydrate-binding module (CBM_E1) derived from sugarcane soil metagenome.

F. Squina, I. Polikarpov, H. Gilbert, 2014, Acta crystallographica. Section F, Structural biology communications.

Exploring oyster mushroom (Pleurotus ostreatus) substrate preparation by varying phase I composting time: changes in bacterial communities and physicochemical composition of biomass impacting mushroom yields

I. Polikarpov, F. Segato, J. Pecchia, 2018, Journal of applied microbiology.

Pre-treatment of sugarcane bagasse with a combination of sodium hydroxide and lime for improving the ruminal degradability: optimization of process parameters using response surface methodology

F. Ahmadi, I. Polikarpov, M. Khorvash, 2016 .

Crystal structures of bovine b-lactoglobulin in the orthorhombic space

I. Polikarpov, L. Sawyer, V. L. Valente-Mesquita, 2001 .

Ajulemic Acid, a Synthetic Nonpsychoactive Cannabinoid Acid, Bound to the Ligand Binding Domain of the Human Peroxisome Proliferator-activated Receptor γ*

Igor Polikarpov, S. Dias, I. Polikarpov, 2007, Journal of Biological Chemistry.

Identification of a new hormone-binding site on the surface of thyroid hormone receptor.

L. Martínez, R. Aparício, P. Webb, 2014, Molecular endocrinology.

Crystallization and preliminary X-ray study of beta--mannosidase from Trichoderma reesei.

A. N. Savel'ev, R. Aparício, I. Polikarpov, 2000, Acta crystallographica. Section D, Biological crystallography.

Different binding and recognition modes of GL479, a dual agonist of Peroxisome Proliferator-Activated Receptor α/γ.

Igor Polikarpov, Amanda Bernardes, Letizia Giampietro, 2015, Journal of structural biology.

Energetic contributions and topographical organization of ligand binding residues of tissue factor.

J. Schullek, I. Polikarpov, T. Edgington, 1995, Biochemistry.

Characterization of Pretreated Fractions and Cellulosic Ethanol Production from Steam-Exploded Eucalyptus urograndis

I. Polikarpov, L. Ramos, A. Potthast, 2020 .

Expression, purification, crystallization and preliminary X-ray diffraction analysis of the pectin methylesterase from the sugar cane weevil Sphenophorus levis.

I. Polikarpov, F. Henrique-Silva, D. E. Evangelista, 2014, Acta crystallographica. Section F, Structural biology communications.

Expression, purification, and initial structural characterization of rat orphan nuclear receptor NOR-1 LBD domain.

R. Portugal, I. Polikarpov, M. Zakin, 2004, Protein expression and purification.

Amino acid sequence of piratoxin-II, a myotoxic lys49 phospholipase A(2) homologue from Bothrops pirajai venom.

I. Polikarpov, A. Soares, S. Marangoni, 2000, Biochimie.

Divergence in macromolecular assembly: X-ray crystallographic structure analysis of lumazine synthase from Brucella abortus.

B. Braden, I. Polikarpov, A. Cauerhff, 2000, Journal of molecular biology.

Crystallization and Preliminary X-Ray Diffraction Analysis of the Lumazine Synthase fromBrucella abortus☆

R. Poljak, B. Braden, I. Polikarpov, 1998 .

Crystallization and preliminary x-ray diffraction analysis of the lumazine synthase from Brucella abortus.

R. Poljak, B. Braden, I. Polikarpov, 1998, Journal of structural biology.

Structural insights into β-glucosidase transglycosylation based on biochemical, structural and computational analysis of two GH1 enzymes from Trichoderma harzianum.

S. R. Marana, I. Polikarpov, A. S. Nascimento, 2018, New biotechnology.

Structural and thermodynamic analysis of thrombin:suramin interaction in solution and crystal phases.

I. Polikarpov, L. Lima, Mario de Oliveira Neto, 2009, Biochimica et biophysica acta.

Crystal structure of yeast hexokinase PI in complex with glucose: A classical “induced fit” example revised

Lucas Bleicher, Igor Polikarpov, I. Polikarpov, 2008, Proteins.

Crystallization and preliminary X-ray diffraction analysis of rat protein tyrosine phosphatase η

A. Fusco, I. Polikarpov, A. S. Nascimento, 2006 .

Structural analysis of Tityus serrulatus Ts1 neurotoxin at atomic resolution: insights into interactions with Na+ channels.

I. Polikarpov, S. Marangoni, M. Toyama, 2003, Acta crystallographica. Section D, Biological crystallography.

Crystallization and preliminary X-ray analysis of bucain, a novel toxin from the Malayan krait Bungarus candidus.

S. Nirthanan, I. Polikarpov, R. Kini, 2002, Acta crystallographica. Section D, Biological crystallography.

Structural and biochemical characterization of a GH3 β-glucosidase from the probiotic bacteria Bifidobacterium adolescentis.

S. R. Marana, I. Polikarpov, A. S. Nascimento, 2018, Biochimie.

Structural and biochemical data of Trichoderma harzianum GH1 β-glucosidases

S. R. Marana, I. Polikarpov, A. S. Nascimento, 2017, Data in brief.

Recombinant Trichoderma harzianum endoglucanase I (Cel7B) is a highly acidic and promiscuous carbohydrate-active enzyme

F. Squina, I. Polikarpov, C. A. Rezende, 2015, Applied Microbiology and Biotechnology.

The MX2 macromolecular crystallography beamline: a wiggler X-ray source at the LNLS.

M. A. Raulik, I. Polikarpov, A. S. Nascimento, 2009, Journal of synchrotron radiation.

Interleukin-22 forms dimers that are recognized by two interleukin-22R1 receptor chains.

J. Renauld, I. Polikarpov, H. Fischer, 2008, Biophysical journal.

Helix 12 dynamics and thyroid hormone receptor activity: experimental and molecular dynamics studies of Ile280 mutants.

Leandro Martínez, Igor Polikarpov, Paul Webb, 2011, Journal of molecular biology.

Camptosemin, a tetrameric lectin of Camptosema ellipticum: structural and functional analysis

I. Polikarpov, M. Cominetti, W. Garcia, 2010, European Biophysics Journal.

Structural analysis of an Echinococcus granulosus actin-fragmenting protein by small-angle x-ray scattering studies and molecular modeling.

R. Portugal, I. Polikarpov, A. Zaha, 2006, Biophysical journal.

Nuclear magnetic resonance investigation of water accessibility in cellulose of pretreated sugarcane bagasse

M. N. d'Eurydice, I. Polikarpov, T. Bonagamba, 2014, Biotechnology for Biofuels.

Analysis of agonist and antagonist effects on thyroid hormone receptor conformation by hydrogen/deuterium exchange.

L. Martínez, J. Baxter, P. Webb, 2011, Molecular endocrinology.

Low Resolution Structures of the Retinoid X Receptor DNA-binding and Ligand-binding Domains Revealed by Synchrotron X-ray Solution Scattering*

S. Dias, F. A. Neves, J. Baxter, 2003, The Journal of Biological Chemistry.

Structure-Based Approach for the Study of Estrogen Receptor Binding Affinity and Subtype Selectivity

Adriano D. Andricopulo, Igor Polikarpov, Lívia Barros Salum, 2008, J. Chem. Inf. Model..

Conformation by Hydrogen / Deuterium Exchange Analysis of Agonist and Antagonist Effects on Thyroid Hormone Receptor

L. Martínez, J. Baxter, P. Webb, 2010 .

Structural and chemical basis for enhanced affinity and potency for a large series of estrogen receptor ligands: 2D and 3D QSAR studies.

Adriano D Andricopulo, Igor Polikarpov, I. Polikarpov, 2007, Journal of molecular graphics & modelling.

Ligand dissociation from estrogen receptor is mediated by receptor dimerization: evidence from molecular dynamics simulations.

Leandro Martínez, Igor Polikarpov, Paul Webb, 2008, Molecular endocrinology.

Molecular dynamics simulations reveal multiple pathways of ligand dissociation from thyroid hormone receptors.

Leandro Martínez, Igor Polikarpov, Paul Webb, 2005, Biophysical journal.

Human thyroid receptor forms tetramers in solution, which dissociate into dimers upon ligand binding

S. Dias, F. A. Neves, L. A. Simeoni, 2007, Cell Biochemistry and Biophysics.

Role of Halogen Bonds in Thyroid Hormone Receptor Selectivity: Pharmacophore-Based 3D-QSSR Studies

Adriano D. Andricopulo, Lívia B. Salum, Napoleão Fonseca Valadares, 2009, J. Chem. Inf. Model..

Cellulose fiber size defines efficiency of enzymatic hydrolysis and impacts degree of synergy between endo- and exoglucanases

I. Polikarpov, C. A. Rezende, V. Pellegrini, 2018, Cellulose.

Novel Zn2+-binding Sites in Human Transthyretin

I. Polikarpov, D. Foguel, L. Lima, 2010, The Journal of Biological Chemistry.

Sets of Covariant Residues Modulate the Activity and Thermal Stability of GH1 β-Glucosidases

S. R. Marana, I. Polikarpov, F. Tamaki, 2014, PloS one.

Enzymes in Bioenergy

I. Polikarpov, V. Serpa, 2011 .

A novel thermostable GH5 β-xylosidase from Thermogemmatispora sp. T81.

I. Polikarpov, R. Sparling, D. Levin, 2019, New biotechnology.

A simple enzymatic assay for the quantification of C1-specific cellulose oxidation by lytic polysaccharide monooxygenases

I. Polikarpov, C. Felby, R. Singh, 2019, Biotechnology Letters.

Gaining ligand selectivity in thyroid hormone receptors via entropy

Leandro Martínez, Igor Polikarpov, Phuong Nguyen, 2009, Proceedings of the National Academy of Sciences.

Low-resolution molecular shape, biochemical characterization and emulsification properties of a halotolerant esterase from Bacillus licheniformis

I. Polikarpov, E. A. de Araújo, V. Pellegrini, 2020, European Biophysics Journal.

Small-angle X-ray scattering and structural modeling of full-length: cellobiohydrolase I from Trichoderma harzianum

L. Martínez, I. Polikarpov, F. R. Rosseto, 2013, Cellulose.

Crystal structure of exo-inulinase from Aspergillus awamori in spacegroup P212121

I. Polikarpov, A. Rojas, A. Golubev, 2004 .

Comparative analysis of two recombinant LPMOs from Aspergillus fumigatus and their effects on sugarcane bagasse saccharification.

I. Polikarpov, Josman Velasco, F. Segato, 2021, Enzyme and microbial technology.

Fluorescence spectroscopy as a tool to detect and evaluate glucocorticoid-induced skin atrophy

C. Kurachi, I. Polikarpov, W. Correr, 2012, Lasers in Medical Science.

Family 1 carbohydrate binding-modules enhance saccharification rates

I. Polikarpov, B. L. Mello, 2014, AMB Express.

Target analysis of microbial lignocellulytic secretomes: a new approach to enzyme discovery

I. Polikarpov, 2016 .

Purification, and biochemical and biophysical characterization of cellobiohydrolase I from Trichoderma harzianum IOC 3844.

I. Polikarpov, A. Golubev, Francieli Colussi, 2011, Journal of microbiology and biotechnology.

Purification, crystallization and preliminary crystallographic analysis of the catalytic domain of the extracellular cellulase CBHI from Trichoderma harzianum.

I. Polikarpov, Francieli Colussi, R. N. Maeda, 2010, Acta crystallographica. Section F, Structural biology and crystallization communications.

X-ray Structure and Molecular Dynamics Simulations of Endoglucanase 3 from Trichoderma harzianum: Structural Organization and Substrate Recognition by Endoglucanases That Lack Cellulose Binding Module

Rodrigo L. Silveira, I. Polikarpov, E. Prates, 2013, PloS one.

Joint X‐ray crystallographic and molecular dynamics study of cellobiohydrolase I from Trichoderma harzianum: deciphering the structural features of cellobiohydrolase catalytic activity

Igor Polikarpov, Rodrigo L. Silveira, Nei Pereira, 2013, The FEBS journal.

Differences in Gluco and Galacto Substrate-Binding Interactions in a Dual 6Pβ-Glucosidase/6Pβ-Galactosidase Glycoside Hydrolase 1 Enzyme from Bacillus licheniformis

S. R. Marana, I. Polikarpov, Ö. T. Bishop, 2021, J. Chem. Inf. Model..

X-ray Structure, Bioinformatics Analysis, and Substrate Specificity of a 6-Phospho-β-glucosidase Glycoside Hydrolase 1 Enzyme from Bacillus licheniformis

S. R. Marana, I. Polikarpov, Ö. T. Bishop, 2020, J. Chem. Inf. Model..

Inhibition of Human Transthyretin Aggregation by Non-Steroidal Anti-Inflammatory Compounds: A Structural and Thermodynamic Analysis

I. Polikarpov, D. Foguel, C. Braga, 2013, International journal of molecular sciences.

Bovine beta-lactoglobulin at 1.8 A resolution--still an enigmatic lipocalin.

D R Flower, J. M. Morais Cabral, A. North, 1997, Structure.

A linker of the proline-threonine repeating motif sequence is bimodal

I. Polikarpov, M. Skaf, Ivana M. Stanković, 2020, Journal of Molecular Modeling.

2D QSAR studies on thyroid hormone receptor ligands.

Igor Polikarpov, I. Polikarpov, M. Castilho, 2007, Bioorganic & medicinal chemistry.

Enhanced hydrolysis of hydrothermally and autohydrolytically treated sugarcane bagasse and understanding the structural changes leading to improved saccharification

E. deAzevedo, I. Polikarpov, B. S. Chadha, 2020 .

Structural characterization of B and non-B subtypes of HIV-protease: insights into the natural susceptibility to drug resistance development.

A. Wlodawer, A. Gustchina, I. Polikarpov, 2007, Journal of molecular biology.

Getting the most out of X-ray home sources.

I. Polikarpov, A. Rojas, A. Golubev, 2005, Acta crystallographica. Section D, Biological crystallography.

Production of prebiotic xylooligosaccharides from arabino- and glucuronoxylan using a two-domain Jonesia denitrificans xylanase from GH10 family.

I. Polikarpov, V. Pellegrini, Milena Moreira Vacilotto, 2021, Enzyme and microbial technology.

Crystal structure and statistical coupling analysis of highly glycosylated peroxidase from royal palm tree (Roystonea regia).

V. Shnyrov, J. Calvete, L. Sanz, 2010, Journal of structural biology.

Ionic diodes based on regenerated α-cellulose films deposited asymmetrically onto a microhole

Neil B. McKeown, Lian Fan, Igor Polikarpov, 2017 .

Structural rearrangements in the thyroid hormone receptor hinge domain and their putative role in the receptor function.

Lucas Bleicher, Igor Polikarpov, Paul Webb, 2006, Journal of molecular biology.

Transformation of xylan into value-added biocommodities using Thermobacillus composti GH10 xylanase.

I. Polikarpov, E. A. de Araújo, V. Pellegrini, 2020, Carbohydrate polymers.

Crystallographic structure and molecular dynamics simulations of the major endoglucanase from Xanthomonas campestris pv. campestris shed light on its oligosaccharide products release pattern.

F. Squina, I. Polikarpov, E. Prates, 2019, International journal of biological macromolecules.

Molecular dynamics simulations of ligand dissociation from thyroid hormone receptors: evidence of the likeliest escape pathway and its implications for the design of novel ligands.

Leandro Martínez, Igor Polikarpov, Paul Webb, 2006, Journal of medicinal chemistry.

Crystallization of a non-B and a B mutant HIV protease.

A. Tanuri, I. Polikarpov, O. Antunes, 2004, Acta crystallographica. Section D, Biological crystallography.

Thermal adaptation strategies of the extremophile bacterium Thermus filiformis based on multi-omics analysis

F. Squina, M. B. Couger, I. Polikarpov, 2017, Extremophiles.

SAXSMoW 3.0: New advances in the determination of the molecular weight of proteins in dilute solutions from SAXS intensity data on a relative scale

I. Polikarpov, A. Craievich, Mario de Oliveira Neto, 2021, Protein science : a publication of the Protein Society.

A Novel Carbohydrate-binding Module from Sugar Cane Soil Metagenome Featuring Unique Structural and Carbohydrate Affinity Properties*

F. Squina, I. Polikarpov, H. Gilbert, 2016, The Journal of Biological Chemistry.

Xanthomonas campestris expansin-like X domain is a structurally disordered beta-sheet macromolecule capable of synergistically enhancing enzymatic efficiency of cellulose hydrolysis

I. Polikarpov, M. Oliveira Neto, A. T. Júnior, 2015, Biotechnology Letters.

Cellulose ionics: switching ionic diode responses by surface charge in reconstituted cellulose films.

F. Marken, I. Polikarpov, J. Scott, 2017, The Analyst.

Nanostructured sensors containing immobilized nuclear receptors for thyroid hormone detection.

V. Zucolotto, I. Polikarpov, A. Figueira, 2014, Journal of biomedical nanotechnology.

Structural insights into the beta-mannosidase from T. reesei obtained by synchrotron small-angle X-ray solution scattering enhanced by X-ray crystallography.

R. Aparício, I. Polikarpov, H. Fischer, 2002, Biochemistry.

Structural and molecular dynamics investigations of ligand stabilization via secondary binding site interactions in Paenibacillus xylanivorans GH11 xylanase

I. Polikarpov, A. S. Nascimento, S. Ghio, 2021, Computational and structural biotechnology journal.

Cloning, purification, crystallization and preliminary X-ray studies of a carbohydrate-binding module from family 64 (StX).

F. Squina, I. Polikarpov, A. Zeri, 2015, Acta crystallographica. Section F, Structural biology communications.

Two- and Three-Dimensional Quantitative Structure-Activity Relationships Studies on a Series of Liver X Receptor Ligands

Adriano D Andricopulo, Igor Polikarpov, Lívia B Salum, 2008, The open medicinal chemistry journal.

RXR agonist modulates TR: corepressor dissociation upon 9-cis retinoic acid treatment.

I. Polikarpov, J. Xavier-Neto, Juliana Fattori, 2015, Molecular endocrinology.

Low-resolution structures of thyroid hormone receptor dimers and tetramers in solution.

S. Dias, J. Baxter, P. Webb, 2007, Biochemistry.