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Topic Area: Life Sciences Research
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Displaying records 221 to 230 of 271 records.
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221. Stressing-Out DNA? The Contribution of Serine-Phosphodiester Interactions in Catalysis by Uracil DNA Glycosylase
Topic: Life Sciences Research
Published: 10/17/2000
Authors: R M. Werner, Y. L. Jiang, R. G. Gordley, J. Jagadeesh, Jane E Ladner, G Xiao, M Tordova, G L. Gilliland, J T. Stivers
Abstract: The DNA repair enzyme uracil DNA glycosylase (UDG) pinches the phosphodiester backbone of damaged DNA using the hydroxyl side chains of a conserved trio of serine residues, resulting in flipping of the deoxyuridine from the DNA helix into the enzyme ...
http://www.nist.gov/manuscript-publication-search.cfm?pub_id=830180

222. Structural analysis of heparin by Raman spectroscopy
Topic: Life Sciences Research
Published: 1/1/1996
Authors: Donald H Atha, Adolfas Kastytis Gaigalas, Vytautas Reipa
http://www.nist.gov/manuscript-publication-search.cfm?pub_id=906420

223. Structure (1.3 Å) and Charge States of a Ribonuclease A-Uridine Vanadate Complex: Implications for the Phosphate Ester Hydrolysis Mechanism
Topic: Life Sciences Research
Published: 6/10/1998
Authors: B Wladkowski, L A Svensson, L Sjolin, Jane E Ladner, G L. Gilliland
http://www.nist.gov/manuscript-publication-search.cfm?pub_id=901659

224. Structure and Function of the Xenobiotic Substrate Binding Site and Location of a Potential Non-Substrate Binding Site in a Class Pi Glutathione S-Transferase
Topic: Life Sciences Research
Published: 8/12/1997
Authors: X Ji, M. Tordova, R O'Donnell, J F Parsons, J B Hayden, G L. Gilliland, P Zimniak
http://www.nist.gov/manuscript-publication-search.cfm?pub_id=100240

225. Structure and Reaction in the Active Site of Mammalian Adenylyl Cyclase
Topic: Life Sciences Research
Published: 4/8/2004
Authors: Y. S. Lee, Morris Krauss
Abstract: The reaction path for the catalytic conversion of adenosine triphosphate (ATP) to cyclic adenosine monophosphate (cAMP) by the enzyme mammalian adenylyl cyclase has been calculated theoretically using the Hartree-Fock method. The crystal structure of ...
http://www.nist.gov/manuscript-publication-search.cfm?pub_id=830386

226. Substrate Specificity and Excision Kinetics of Escherichia Coli Endonuclease VIII (Nei) for Modified Bases in DNA Damaged by Free Radicals
Topic: Life Sciences Research
Published: 10/9/2001
Author: M. Dizdaroglu
Abstract: Endonuclease VIII (Nei) is one of three enzymes in Escherichia coli that are involved in base-excision repair of oxidative damage to DNA. We investigated the substrate specificity and excision kinetics of this DNA glycosylase for bases in DNA that ha ...
http://www.nist.gov/manuscript-publication-search.cfm?pub_id=830248

227. Substrate Specificity of Schizosaccharomyces pombe Nth Protein for Products of Oxidative DNA Damage
Topic: Life Sciences Research
Published: 1/13/1998
Authors: B. Karahalil, T. Roldan-Arjona, M Miral Dizdar
http://www.nist.gov/manuscript-publication-search.cfm?pub_id=903718

228. Substrate Specificity of the Ntg1 and Ntg2 Proteins of Saccharomyces cerevisiae for Modified Bases in Oxidatively Damaged DNA
Topic: Life Sciences Research
Published: 12/1/1998
Authors: S. Senturker, P Auffret van der kemp, H -J You, P W Doetsch, M. Dizdaroglu, B Boiteux
http://www.nist.gov/manuscript-publication-search.cfm?pub_id=100609

229. Substrate binding and the presence of ferredoxin affect the redox properties of the soluble plant Delta(9)-18:0-acyl carrier protein desaturase
Topic: Life Sciences Research
Published: 9/23/2004
Authors: Vytautas Reipa, J Shanklin, V L. Vilker
http://www.nist.gov/manuscript-publication-search.cfm?pub_id=903192

230. Substrate specificities and excision kinetics of DNA glycosylases involved in base-excision repair of oxidative DNA damage
Topic: Life Sciences Research
Published: 10/29/2003
Author: M Miral Dizdar
http://www.nist.gov/manuscript-publication-search.cfm?pub_id=903147



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