About: Single mutation at the intersubunit interface confers extra efficiency to Cu,Zn superoxide dismutase

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scientific article published on 01 October 2000

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rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в жовтні 2000 (uk) im Oktober 2000 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu n'ochobre de 2000 (ast) scientific article published on 01 October 2000 (en)
publication date	wds:Q56877680-78905C64-7733-4337-A549-EF0475530CE1
publication date	2000-10-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q56877680-11CBF604-0C16-4C0F-BA1F-672B65772C55
language of work or name	English
cites work	wds:Q56877680-103A7B57-FF6F-4DF3-9FE2-472979E4D02E wds:Q56877680-1A468B73-DA81-475B-910C-BB128A2D8FD0 wds:Q56877680-2DAB3A88-B086-4D5B-81AB-6107F018A9A0 wds:Q56877680-33E36701-8DDD-41E2-879F-8FB07B39EB34 wds:Q56877680-3B9A67A4-E51B-4B9C-AE89-346764E29AB6 wds:Q56877680-5D8B5E13-48BB-417F-9118-91C16F16BECB wds:Q56877680-62437ACB-6375-4D34-896D-70EB3A8D09E1 wds:Q56877680-63BCAB54-5E18-421E-B050-1356F8BD7B00 wds:Q56877680-6A45F0AB-52D3-4E6A-96B2-9673BD2D2A18 wds:Q56877680-6D5D339E-AA52-403F-B0A7-FD7F1434A3C4 wds:Q56877680-6FE25800-6686-4B57-B2DB-5E085AD83C58 wds:Q56877680-83C568AC-6208-4A63-B712-032995AA1100 wds:Q56877680-872237D1-DD9D-4419-B357-5E81864C7AED wds:Q56877680-884390C3-9EB5-45CF-8CB2-37D9D41244E6 wds:Q56877680-8E51A9F9-65B3-4C5F-8334-3DA3AD91AA69 wds:Q56877680-8E8DBEA0-4019-46F8-84F6-AC29C0166382 wds:Q56877680-9399CEA3-03DF-48C1-A376-C1FB1972CD3B wds:Q56877680-A9FA8E7E-70E8-4D10-BFBB-12F80E244DED wds:Q56877680-B0116EA8-A797-4255-8146-852465FF2D99 wds:Q56877680-C4D25BC9-1A0A-45F8-850B-0C98AE57794E wds:Q56877680-CD98DFB6-7174-494D-849D-B5D294525A14 wds:Q56877680-D33C589D-531C-45FC-B409-C3FF5BD668C8 wds:Q56877680-F09272A8-E176-4B6D-B508-246025002F24
cites work	PROCHECK: a program to check the stereochemical quality of protein structures MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures Calculation of the total electrostatic energy of a macromolecular system: solvation energies, binding energies, and conformational analysis Improved methods for building protein models in electron density maps and the location of errors in these models Processing of X-ray diffraction data collected in oscillation mode Novel dimeric interface and electrostatic recognition in bacterial Cu,Zn superoxide dismutase Evolutionary constraints for dimer formation in prokaryotic Cu,Zn superoxide dismutase The essential dynamics of Cu, Zn superoxide dismutase: suggestion of intersubunit communication The effects of pH and various salts upon the activity of a series of superoxide dismutases Evolutionary conservativeness of electric field in the Cu,Zn superoxide dismutase active site. Evidence for co-ordinated mutation of charged amino acid residues. Spectroscopic characterization of recombinant Cu,Zn superoxide dismutase from Photobacterium leiognathi expressed in Escherichia coli: evidence for a novel catalytic copper binding site Toward the engineering of a super efficient enzyme Aspects of the Structure, Function, and Applications of Superoxide Dismutas Solution structure of reduced monomeric Q133M2 copper, zinc superoxide dismutase (SOD). Why is SOD a dimeric enzyme? Faster superoxide dismutase mutants designed by enhancing electrostatic guidance A general method for rapid site-directed mutagenesis using the polymerase chain reaction. Accurate bond and angle parameters for X-ray protein structure refinement Unique structural features of the monomeric Cu,Zn superoxide dismutase from Escherichia coli, revealed by X-ray crystallography Electrostatic recognition between superoxide and copper, zinc superoxide dismutase. Mechanism of action of superoxide dismutase from pulse radiolysis and electron paramagnetic resonance. Evidence that only half the active sites function in catalysis Conserved Enzyme-Substrate Electrostatic Attraction in Prokaryotic Cu,Zn Superoxide Dismutases Cu,Zn superoxide dismutase from Photobacterium leiognathi is an hyperefficient enzyme Modulation of the catalytic rate of Cu,Zn superoxide dismutase in single and double mutants of conserved positively and negatively charged residues.
author name string	wds:Q56877680-668A26E5-F961-4593-A697-CF1A1344AA59 wds:Q56877680-ED276022-4C27-427E-8628-B98950B5DB73 wds:Q56877680-F96C1513-9A28-44AF-AF11-377FCF292FE0
author name string	A Pesce P O'Neill M E Stroppolo
rdfs:label	Single mutation at the intersubunit interface confers extra efficiency to Cu,Zn superoxide dismutase (en) Single mutation at the intersubunit interface confers extra efficiency to Cu,Zn superoxide dismutase (nl)
skos:prefLabel	Single mutation at the intersubunit interface confers extra efficiency to Cu,Zn superoxide dismutase (en) Single mutation at the intersubunit interface confers extra efficiency to Cu,Zn superoxide dismutase (nl)
name	Single mutation at the intersubunit interface confers extra efficiency to Cu,Zn superoxide dismutase (en) Single mutation at the intersubunit interface confers extra efficiency to Cu,Zn superoxide dismutase (nl)
author	wds:Q56877680-46076989-4361-4085-86F1-1132A9019BB9 wds:Q56877680-4DD3E3CE-BBA7-424A-9C9C-DEB1A9DCB830 wds:Q56877680-C9F7F9D5-F288-4108-8696-D3F29E03B06F
author	Alessandro Desideri Martino Bolognesi Mattia Falconi
title	wds:Q56877680-0B7C764E-98BC-4952-BF4B-0E71C0A616A0
title	Single mutation at the intersubunit interface confers extra efficiency to Cu,Zn superoxide dismutase (en)
page(s)	wds:Q56877680-EAEAD0C4-C6C9-45BE-B75F-D145C886F7AA
page(s)	17-20
instance of	wds:Q56877680-0E9E04F7-C172-462C-88F7-6EE22721533D
instance of	scholarly article
main subject	wds:Q56877680-98876259-948B-482C-8883-B0572BEB5BBD wds:Q56877680-A00DC15B-56F7-4218-95DB-22AAA491608E wds:Q56877680-D4753361-8205-4ABE-936B-92D8A62A5E1C wds:Q56877680-D82FD05F-8600-45C6-8986-4A21400B7363
main subject	cell biology biophysics molecular biology structural biology
PubMed ID	wds:Q56877680-D516857A-1344-4A62-8492-F58780CE066F
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/11033348
PubMed ID	11033348
published in	wds:Q56877680-5E0E5628-D5B1-40BF-B18E-8B7929B98851
published in	FEBS Letters
issue	wds:Q56877680-A675E411-52E4-426B-A316-4E70D5B51DBE
volume	wds:Q56877680-666B0529-E202-473B-BE23-0DD2F5705079
issue	1
volume	483
DOI	wds:Q56877680-8791682E-6CD7-4796-9422-FE48C9588EBB
DOI	http://dx.doi.org/10.1016/S0014-5793(00)01967-0
DOI	10.1016/S0014-5793(00)01967-0

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