E. Horjales

ORCID: 0000-0003-1022-5628
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Research Areas
  • Glycosylation and Glycoproteins Research
  • Enzyme Structure and Function
  • Biochemical and Molecular Research
  • Enzyme-mediated dye degradation
  • Protein Structure and Dynamics
  • Carbohydrate Chemistry and Synthesis
  • Venomous Animal Envenomation and Studies
  • Trypanosoma species research and implications
  • Pancreatic function and diabetes
  • Ion channel regulation and function
  • Enzyme Production and Characterization
  • Microbial Metabolism and Applications
  • Peptidase Inhibition and Analysis
  • Fungal and yeast genetics research
  • RNA and protein synthesis mechanisms
  • Dye analysis and toxicity
  • melanin and skin pigmentation
  • Hemoglobin structure and function
  • Research on Leishmaniasis Studies
  • Chemical Synthesis and Analysis
  • Computational Drug Discovery Methods
  • Monoclonal and Polyclonal Antibodies Research
  • Alcohol Consumption and Health Effects
  • Immune Cell Function and Interaction
  • Diet, Metabolism, and Disease

Universidade de São Paulo
1995-2018

Universidade Federal de São Carlos
1995-2018

Universidad Nacional Autónoma de México
1995-2008

Instituto de Biotecnología de León
2002

Bioénergétique et Ingénierie des Protéines
2002

Queen Elizabeth II Medical Centre
2002

The University of Western Australia
2002

Universidad de la República de Uruguay
1992

Swedish University of Agricultural Sciences
1984-1990

Uppsala University
1987

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTMolecular aspects of functional differences between alcohol and sorbitol dehydrogenasesHans Eklund, Eduardo Horjales, Hans Joernvall, Carl-Ivar Braenden, Jonathan JefferyCite this: Biochemistry 1985, 24, 27, 8005–8012Publication Date (Print):December 1, 1985Publication History Published online1 May 2002Published inissue 1 December 1985https://pubs.acs.org/doi/10.1021/bi00348a025https://doi.org/10.1021/bi00348a025research-articleACS...

10.1021/bi00348a025 article EN Biochemistry 1985-12-01

Conformational models of the three characterized classes mammalian liver alcohol dehydrogenase were constructed using computer graphics based on known three-dimensional structure E subunit horse enzyme (class I) and primary structures human classes. This correlates substrate-binding pockets class I subunits (alpha, beta gamma in enzyme) with those II III (pi chi, respectively) for enzymes that differ substrate specificity, inhibition pattern many other properties. The sites exhibit...

10.1111/j.1432-1033.1990.tb19337.x article EN European Journal of Biochemistry 1990-10-01

Three‐dimensional models of human alcohol dehydrogenase subunits have been constructed, based on the homologous horse enzyme, with computer graphics. All types class I (α, β, and γ) major allelic variants (β 1 /β 2 γ /γ ) studied. Residue differences between E‐type subunit enzyme any isozymes occur at 64 positions, about half which are isozyme‐specific. About two thirds substitutions surface all can be accommodated in highly conserved three‐dimensional structures. The model isozyme is most...

10.1111/j.1432-1033.1987.tb13322.x article EN European Journal of Biochemistry 1987-09-01

Abstract Mevalonate kinase (MVK) is an essential enzyme acting in early steps of sterol isoprenoids biosynthesis, such as cholesterol humans or ergosterol trypanosomatids. MVK conserved from bacteria to mammals and localizes glycosomes During the course T. cruzi characterization, we found that, addition glycosomes, this may be secreted modulate cell invasion. To evaluate role TcMVK parasite-host interactions, recombinant protein was produced anti-TcMVK antibodies were raised mice. detected...

10.1038/srep24610 article EN cc-by Scientific Reports 2016-04-26

10.1016/s0006-291x(02)00766-0 article EN Biochemical and Biophysical Research Communications 2002-07-01

Structural studies of proteins normally require large quantities pure material that can only be obtained through heterologous expression systems and recombinant technique. In these procedures, amounts expressed protein are often found in the insoluble fraction, making purification from soluble fraction inefficient, laborious costly. Usually, refolding is avoided due to a lack experimental assays validate correct folding compare conformational population fraction. Herein, we propose...

10.1038/srep04259 article EN cc-by-nc-nd Scientific Reports 2014-03-04

Model building and energy minimization procedures have been used to determine a productive substrate binding mode in liver alcohol dehydrogenase for secondary alcohols. These docking results compared some of the extensive amounts kinetic data available this enzyme. The indirect diamond lattice approach first suggested by Prelog (Prelog, V. (1964) Pure Appl. Chem. 9, 119-130) describe active site an enzyme has build direct from crystallographic model This was oriented positioned into using...

10.1016/s0021-9258(17)36274-9 article EN cc-by Journal of Biological Chemistry 1985-12-01

Glucosamine‐6‐phosphate deaminase (EC 3.5.99.6) is an allosteric enzyme that catalyzes the reversible conversion of D ‐glucosamine‐6‐phosphate into ‐fructose‐6‐phosphate and ammonium. Here we describe existence two mammalian glucosamine‐6‐phosphate enzymes. We present crystallographic structure one them, long human deaminase, at 1.75 Å resolution. Crystals belong to space group P2 1 2 a whole hexamer in asymmetric unit. The active‐site lid (residues 162–182) presented significant structural...

10.1016/s0014-5793(03)00896-2 article EN FEBS Letters 2003-08-27

Glossoscolex paulistus is a free-living earthworm encountered in south-east Brazil. Its oxygen transport requirements are undertaken by giant extracellular haemoglobin, or erythrocruorin (HbGp), which has an approximate molecular mass of 3.6 MDa and, analogy with its homologue from Lumbricus terrestris (HbLt), believed to be composed total 180 polypeptide chains. In the present work full particle cyanomet state was purified and crystallized using sodium citrate PEG8000 as precipitant. The...

10.1107/s090904951002772x article EN cc-by Journal of Synchrotron Radiation 2010-11-04

A new crystallographic structure of the free active-site R conformer allosteric enzyme glucosamine-6-phosphate deaminase from Escherichia coli, coupled with previously reported structures T and conformers, generates a detailed description heterotropic transition in which structural flexibility plays central role. The conformer's external zone [Horjales et al. (1999), Structure, 7, 527–536] presents higher B values than conformers. ligand-free (T conformer) undergoes an to upon binding...

10.1107/s0907444901016699 article EN Acta Crystallographica Section D Biological Crystallography 2001-12-21

The antibody BCF2 generated against the mammal-specific toxin Cn2 of scorpion Centruroides noxius Hoffmann neutralizes effect both and venom. We cloned sequenced genes coding for Fv fragment BCF2. A three-dimensional (3D) model was using a knowledge-based approach. Furthermore, 3D complex Cn2–BCF2 built nuclear magnetic resonance (NMR) structure experimental results on putative epitope region around N C termini. initial conformations were submitted to new refinement procedure rigid-body...

10.1002/(sici)1097-0134(19991001)37:1<130::aid-prot13>3.0.co;2-s article EN Proteins Structure Function and Bioinformatics 1999-10-01

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTAsymmetric allosteric activation of Escherichia coli glucosamine-6-phosphate deaminase produced by replacements Tyr 121Myriam M. Altamirano, Jacqueline A. Plumbridge, Eduardo Horjales, and Mario L. CalcagnoCite this: Biochemistry 1995, 34, 18, 6074–6082Publication Date (Print):May 9, 1995Publication History Published online1 May 2002Published inissue 9...

10.1021/bi00018a010 article EN Biochemistry 1995-05-09
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