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Conference Paper: Recent progress in the study of the intracellular functions of diadenosine polyphosphates

TitleRecent progress in the study of the intracellular functions of diadenosine polyphosphates
Authors
KeywordsAp4a
Diphosphoinositol
Fhit
Stress
Issue Date2001
PublisherJohn Wiley & Sons, Inc. The Journal's web site is located at http://www3.interscience.wiley.com/cgi-bin/jhome/34597
Citation
The PURINES 2000 Meeting, Madrid, Spain, 9-13 July 2000. In Drug Development Research, 2001, v. 52 n. 1-2, p. 249-259 How to Cite?
AbstractRecent developments in the effort to understand the metabolism and function of the intracellular dinucleoside polyphosphates were described by nine speakers from some of the world's leading laboratories in this field in a workshop at the Purines 2000 International Symposium on Nucleosides and Nucleotides held in Madrid in July, 2000. Topics were wide-ranging and included phenotypic analyses of yeast mutants defective in enzymes of dinucleoside polyphosphate degradation, virally encoded catabolic enzymes, the structure and function of the Fhit tumor suppressor and Fhit-nitrilase fusion proteins and the relationship of Fhit to human diadenosine triphosphate hydrolase, site-directed mutagenesis of diadenosine tetraphosphate hydrolase, novel nucleotide analogs for studying hydrolase function, the synthesis of dinucleoside polyphosphates by ligases, and the possible roles of diadenosine tri- and tetraphosphates in insulin function and of diadenosine tetraphosphate in the heat-shock response of Escherichia coli. The results presented and the ensuing discussions showed that, while considerable progress is being made in the field, it still has the capacity to tease and frustrate and produce the unexpected result. © 2001 Wiley-Liss, Inc.
DescriptionThese journal issues entitled: Special Issue: PURINES 2000 Meeting: Biochemical, Pharmacological and Clinical Perspectives
Conference Theme: Biochemical, Pharmacological and Clinical Perspectives
Persistent Identifierhttp://hdl.handle.net/10722/148704
ISSN
2021 Impact Factor: 5.004
2020 SCImago Journal Rankings: 0.582
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorMclennan, AGen_US
dc.contributor.authorBarnes, LDen_US
dc.contributor.authorBlackburn, GMen_US
dc.contributor.authorBrenner, Cen_US
dc.contributor.authorGuranowski, Aen_US
dc.contributor.authorMiller, ADen_US
dc.contributor.authorRovira, JMen_US
dc.contributor.authorRotllán, Pen_US
dc.contributor.authorSoria, Ben_US
dc.contributor.authorTanner, JAen_US
dc.contributor.authorSillero, Aen_US
dc.date.accessioned2012-05-29T06:17:25Z-
dc.date.available2012-05-29T06:17:25Z-
dc.date.issued2001en_US
dc.identifier.citationThe PURINES 2000 Meeting, Madrid, Spain, 9-13 July 2000. In Drug Development Research, 2001, v. 52 n. 1-2, p. 249-259en_US
dc.identifier.issn0272-4391en_US
dc.identifier.urihttp://hdl.handle.net/10722/148704-
dc.descriptionThese journal issues entitled: Special Issue: PURINES 2000 Meeting: Biochemical, Pharmacological and Clinical Perspectives-
dc.descriptionConference Theme: Biochemical, Pharmacological and Clinical Perspectives-
dc.description.abstractRecent developments in the effort to understand the metabolism and function of the intracellular dinucleoside polyphosphates were described by nine speakers from some of the world's leading laboratories in this field in a workshop at the Purines 2000 International Symposium on Nucleosides and Nucleotides held in Madrid in July, 2000. Topics were wide-ranging and included phenotypic analyses of yeast mutants defective in enzymes of dinucleoside polyphosphate degradation, virally encoded catabolic enzymes, the structure and function of the Fhit tumor suppressor and Fhit-nitrilase fusion proteins and the relationship of Fhit to human diadenosine triphosphate hydrolase, site-directed mutagenesis of diadenosine tetraphosphate hydrolase, novel nucleotide analogs for studying hydrolase function, the synthesis of dinucleoside polyphosphates by ligases, and the possible roles of diadenosine tri- and tetraphosphates in insulin function and of diadenosine tetraphosphate in the heat-shock response of Escherichia coli. The results presented and the ensuing discussions showed that, while considerable progress is being made in the field, it still has the capacity to tease and frustrate and produce the unexpected result. © 2001 Wiley-Liss, Inc.en_US
dc.languageengen_US
dc.publisherJohn Wiley & Sons, Inc. The Journal's web site is located at http://www3.interscience.wiley.com/cgi-bin/jhome/34597en_US
dc.relation.ispartofDrug Development Researchen_US
dc.subjectAp4aen_US
dc.subjectDiphosphoinositolen_US
dc.subjectFhiten_US
dc.subjectStressen_US
dc.titleRecent progress in the study of the intracellular functions of diadenosine polyphosphatesen_US
dc.typeConference_Paperen_US
dc.identifier.emailTanner, JA:jatanner@hku.hken_US
dc.identifier.authorityTanner, JA=rp00495en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1002/ddr.1122en_US
dc.identifier.scopuseid_2-s2.0-0035042508en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0035042508&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume52en_US
dc.identifier.issue1-2en_US
dc.identifier.spage249en_US
dc.identifier.epage259en_US
dc.identifier.isiWOS:000168532400031-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridMcLennan, AG=7004499238en_US
dc.identifier.scopusauthoridBarnes, LD=7103076976en_US
dc.identifier.scopusauthoridBlackburn, GM=7201722732en_US
dc.identifier.scopusauthoridBrenner, C=7102383525en_US
dc.identifier.scopusauthoridGuranowski, A=7003631810en_US
dc.identifier.scopusauthoridMiller, AD=7406230808en_US
dc.identifier.scopusauthoridRovira, JM=36891329600en_US
dc.identifier.scopusauthoridRotllán, P=6701457772en_US
dc.identifier.scopusauthoridSoria, B=7006173693en_US
dc.identifier.scopusauthoridTanner, JA=35513993000en_US
dc.identifier.scopusauthoridSillero, A=7006367269en_US
dc.customcontrol.immutablesml 170406 amended-
dc.identifier.issnl0272-4391-

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