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Items: 25


An All-Inclusive and Straightway Laboratory Activity to Solve the Three-Dimensional Crystal Structure of a Protein.

Klinke S, Rinaldi J, Goldbaum FA, Suarez S, Otero LH.

Biochem Mol Biol Educ. 2019 Nov;47(6):700-707. doi: 10.1002/bmb.21296. Epub 2019 Aug 24.


The Reaction Mechanism of Metallo-β-Lactamases Is Tuned by the Conformation of an Active-Site Mobile Loop.

Palacios AR, Mojica MF, Giannini E, Taracila MA, Bethel CR, Alzari PM, Otero LH, Klinke S, Llarrull LI, Bonomo RA, Vila AJ.

Antimicrob Agents Chemother. 2018 Dec 21;63(1). pii: e01754-18. doi: 10.1128/AAC.01754-18. Print 2019 Jan.


Engineering a bifunctional copper site in the cupredoxin fold by loop-directed mutagenesis.

Espinoza-Cara A, Zitare U, Alvarez-Paggi D, Klinke S, Otero LH, Murgida DH, Vila AJ.

Chem Sci. 2018 Jun 28;9(32):6692-6702. doi: 10.1039/c8sc01444b. eCollection 2018 Aug 28.


Draft Genome Sequence of Methylobacterium sp. Strain V23, Isolated from Accretion Ice of the Antarctic Subglacial Lake Vostok.

Sapp A, Huguet-Tapia JC, Sánchez-Lamas M, Antelo GT, Primo ED, Rinaldi J, Klinke S, Goldbaum FA, Bonomi HR, Christner BC, Otero LH.

Genome Announc. 2018 Mar 8;6(10). pii: e00145-18. doi: 10.1128/genomeA.00145-18.


The disruptive effect of lysozyme on the bacterial cell wall explored by an in-silico structural outlook.

Primo ED, Otero LH, Ruiz F, Klinke S, Giordano W.

Biochem Mol Biol Educ. 2018 Jan;46(1):83-90. doi: 10.1002/bmb.21092. Epub 2017 Nov 13.


Structural and mutational analyses of the Leptospira interrogans virulence-related heme oxygenase provide insights into its catalytic mechanism.

Soldano A, Klinke S, Otero LH, Rivera M, Catalano-Dupuy DL, Ceccarelli EA.

PLoS One. 2017 Aug 3;12(8):e0182535. doi: 10.1371/journal.pone.0182535. eCollection 2017.


Structural and functional characterization of a cold adapted TPM-domain with ATPase/ADPase activity.

Cerutti ML, Otero LH, Smal C, Pellizza L, Goldbaum FA, Klinke S, Aran M.

J Struct Biol. 2017 Mar;197(3):201-209. doi: 10.1016/j.jsb.2016.10.010. Epub 2016 Nov 1.


Structure of the Full-Length Bacteriophytochrome from the Plant Pathogen Xanthomonas campestris Provides Clues to its Long-Range Signaling Mechanism.

Otero LH, Klinke S, Rinaldi J, Velázquez-Escobar F, Mroginski MA, Fernández López M, Malamud F, Vojnov AA, Hildebrandt P, Goldbaum FA, Bonomi HR.

J Mol Biol. 2016 Sep 25;428(19):3702-20. doi: 10.1016/j.jmb.2016.04.012. Epub 2016 Apr 20.


Snapshots of Conformational Changes Shed Light into the NtrX Receiver Domain Signal Transduction Mechanism.

Fernández I, Otero LH, Klinke S, Carrica MDC, Goldbaum FA.

J Mol Biol. 2015 Oct 9;427(20):3258-3272. doi: 10.1016/j.jmb.2015.06.010. Epub 2015 Jun 23.


Discovery of antibiotic (E)-3-(3-carboxyphenyl)-2-(4-cyanostyryl)quinazolin-4(3H)-one.

Bouley R, Kumarasiri M, Peng Z, Otero LH, Song W, Suckow MA, Schroeder VA, Wolter WR, Lastochkin E, Antunes NT, Pi H, Vakulenko S, Hermoso JA, Chang M, Mobashery S.

J Am Chem Soc. 2015 Feb 11;137(5):1738-41. doi: 10.1021/jacs.5b00056. Epub 2015 Feb 2.


Crystallization and preliminary X-ray characterization of the full-length bacteriophytochrome from the plant pathogen Xanthomonas campestris pv. campestris.

Klinke S, Otero LH, Rinaldi J, Sosa S, Guimarães BG, Shepard WE, Goldbaum FA, Bonomi HR.

Acta Crystallogr F Struct Biol Commun. 2014 Dec 1;70(Pt 12):1636-9. doi: 10.1107/S2053230X14023243. Epub 2014 Nov 14.


Solution and crystal structure of BA42, a protein from the Antarctic bacterium Bizionia argentinensis comprised of a stand-alone TPM domain.

Aran M, Smal C, Pellizza L, Gallo M, Otero LH, Klinke S, Goldbaum FA, Ithurralde ER, Bercovich A, Mac Cormack WP, Turjanski AG, Cicero DO.

Proteins. 2014 Nov;82(11):3062-78. doi: 10.1002/prot.24667. Epub 2014 Sep 3.


Disruption of allosteric response as an unprecedented mechanism of resistance to antibiotics.

Fishovitz J, Rojas-Altuve A, Otero LH, Dawley M, Carrasco-López C, Chang M, Hermoso JA, Mobashery S.

J Am Chem Soc. 2014 Jul 16;136(28):9814-7. doi: 10.1021/ja5030657. Epub 2014 Jul 2.


Structural basis for the broad specificity of a new family of amino-acid racemases.

Espaillat A, Carrasco-López C, Bernardo-García N, Pietrosemoli N, Otero LH, Álvarez L, de Pedro MA, Pazos F, Davis BM, Waldor MK, Hermoso JA, Cava F.

Acta Crystallogr D Biol Crystallogr. 2014 Jan;70(Pt 1):79-90. doi: 10.1107/S1399004713024838. Epub 2013 Dec 24.


How allosteric control of Staphylococcus aureus penicillin binding protein 2a enables methicillin resistance and physiological function.

Otero LH, Rojas-Altuve A, Llarrull LI, Carrasco-López C, Kumarasiri M, Lastochkin E, Fishovitz J, Dawley M, Hesek D, Lee M, Johnson JW, Fisher JF, Chang M, Mobashery S, Hermoso JA.

Proc Natl Acad Sci U S A. 2013 Oct 15;110(42):16808-13. doi: 10.1073/pnas.1300118110. Epub 2013 Oct 1.


The structural domains of Pseudomonas aeruginosa phosphorylcholine phosphatase cooperate in substrate hydrolysis: 3D structure and enzymatic mechanism.

Infantes L, Otero LH, Beassoni PR, Boetsch C, Lisa AT, Domenech CE, Albert A.

J Mol Biol. 2012 Nov 2;423(4):503-14. doi: 10.1016/j.jmb.2012.07.024. Epub 2012 Aug 21.


A Pseudomonas aeruginosa PAO1 acetylcholinesterase is encoded by the PA4921 gene and belongs to the SGNH hydrolase family.

Sánchez DG, Otero LH, Hernández CM, Serra AL, Encarnación S, Domenech CE, Lisa AT.

Microbiol Res. 2012 Jun 20;167(6):317-25. doi: 10.1016/j.micres.2011.11.005. Epub 2011 Dec 20.


Phosphorylcholine Phosphatase: A Peculiar Enzyme of Pseudomonas aeruginosa.

Domenech CE, Otero LH, Beassoni PR, Lisa AT.

Enzyme Res. 2011;2011:561841. doi: 10.4061/2011/561841. Epub 2011 Sep 11.


Different Effects of Mg and Zn on the Two Sites for Alkylammonium Compounds in Pseudomonas aeruginosa Phosphorylcholine Phosphatase.

Otero LH, Beassoni PR, Boetsch C, Lisa AT, Domenech CE.

Enzyme Res. 2011;2011:918283. doi: 10.4061/2011/918283. Epub 2011 May 14.


Site-directed mutations and kinetic studies show key residues involved in alkylammonium interactions and reveal two sites for phosphorylcholine in Pseudomonas aeruginosa phosphorylcholine phosphatase.

Beassoni PR, Otero LH, Boetsch C, Domenech CE, González-Nilo FD, Lisa AT.

Biochim Biophys Acta. 2011 Jul;1814(7):858-63. doi: 10.1016/j.bbapap.2011.04.003. Epub 2011 Apr 15.


Crystallization and preliminary X-ray diffraction analysis of Pseudomonas aeruginosa phosphorylcholine phosphatase.

Otero LH, Beassoni PR, Domenech CE, Lisa AT, Albert A.

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Aug 1;66(Pt 8):957-60. doi: 10.1107/S1744309110024061. Epub 2010 Jul 29.


Transition from octahedral to tetrahedral geometry causes the activation or inhibition by Znf2+ of Pseudomonas aeruginosa phosphorylcholine phosphatase.

Otero LH, Beassoni PR, Lisa AT, Domenech CE.

Biometals. 2010 Apr;23(2):307-14. doi: 10.1007/s10534-010-9289-1. Epub 2010 Feb 5.


Preparation and biophysical characterization of recombinant Pseudomonas aeruginosa phosphorylcholine phosphatase.

Beassoni PR, Berti FP, Otero LH, Risso VA, Ferreyra RG, Lisa AT, Domenech CE, Ermácora MR.

Protein Expr Purif. 2010 Jun;71(2):153-9. doi: 10.1016/j.pep.2010.01.006. Epub 2010 Jan 11.


Using a molecular model and kinetic experiments in the presence of divalent cations to study the active site and catalysis of Pseudomonas aeruginosa phosphorylcholine phosphatase.

Beassoni PR, Otero LH, Lisa AT, Domenech CE.

Biochim Biophys Acta. 2008 Dec;1784(12):2038-44. doi: 10.1016/j.bbapap.2008.08.014. Epub 2008 Aug 29.


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