guest ::
| Home > Publications database > The crystal structures of eukaryotic phosphofructokinases from baker's yeast and rabbit skeletal muscle. > print |
| Home > Publications database > The crystal structures of eukaryotic phosphofructokinases from baker's yeast and rabbit skeletal muscle. > print |
| 001 | 95857 | ||
| 005 | 20250730164005.0 | ||
| 024 | 7 | _ | |a pmid:21241708 |2 pmid |
| 024 | 7 | _ | |a 10.1016/j.jmb.2011.01.019 |2 doi |
| 024 | 7 | _ | |a 1089-8638 |2 ISSN |
| 024 | 7 | _ | |a 0022-2836 |2 ISSN |
| 024 | 7 | _ | |a WOS:000288925100007 |2 WOS |
| 024 | 7 | _ | |a altmetric:3246537 |2 altmetric |
| 024 | 7 | _ | |a openalex:W1973813347 |2 openalex |
| 037 | _ | _ | |a PHPPUBDB-19271 |
| 041 | _ | _ | |a eng |
| 082 | _ | _ | |a 570 |
| 100 | 1 | _ | |a Banaszak, K. |
| 110 | 1 | _ | |a DESY |b European Molecular Biology Laboratory |
| 245 | _ | _ | |a The crystal structures of eukaryotic phosphofructokinases from baker's yeast and rabbit skeletal muscle. |
| 260 | _ | _ | |a Amsterdam [u.a.] |b Elsevier |c 2011 |
| 300 | _ | _ | |a 284-297 |
| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
| 336 | 7 | _ | |a article |2 DRIVER |
| 336 | 7 | _ | |a Journal Article |m journal |0 PUB:(DE-HGF)16 |2 PUB:(DE-HGF) |
| 440 | _ | 0 | |a J. Mol. Biol. |v 407 |x 0022-2836 |0 PERI:(DE-600)1355192-9 |
| 500 | _ | _ | |3 Converted on 2013-05-30 15:24 |
| 500 | _ | _ | |3 Converted on 2013-06-21 19:21 |
| 520 | _ | _ | |a Phosphofructokinase 1 (PFK) is a multisubunit allosteric enzyme that catalyzes the principal regulatory step in glycolysis-the phosphorylation of fructose 6-phosphate to fructose 1,6-bisphosphate by ATP. The activity of eukaryotic PFK is modulated by a number of effectors in response to the cell's needs for energy and building blocks for biosynthesis. The crystal structures of eukaryotic PFKs-from Saccharomyces cerevisiae and rabbit skeletal muscle-demonstrate how successive gene duplications and fusion are reflected in the protein structure and how they allowed the evolution of new functionalities. The basic framework inherited from prokaryotes is conserved, and additional levels of structural and functional complexity have evolved around it. Analysis of protein-ligand complexes has shown how PFK is activated by fructose 2,6-bisphosphate (a powerful PFK effector found only in eukaryotes) and reveals a novel nucleotide binding site. Crystallographic results have been used as the basis for structure-based effector design. |
| 536 | _ | _ | |0 G:(DE-H253)POF2-BW7-20130405 |f POF II |x 0 |c POF2-54G13 |a DORIS Beamline BW7 (POF2-54G13) |
| 588 | _ | _ | |a Dataset connected to Pubmed |
| 650 | _ | 2 | |2 MeSH |a Animals |
| 650 | _ | 2 | |2 MeSH |a Binding Sites: genetics |
| 650 | _ | 2 | |2 MeSH |a Crystallography |
| 650 | _ | 2 | |2 MeSH |a Eukaryota: enzymology |
| 650 | _ | 2 | |2 MeSH |a Fructosephosphates: metabolism |
| 650 | _ | 2 | |2 MeSH |a Glycolysis: genetics |
| 650 | _ | 2 | |2 MeSH |a Models, Molecular |
| 650 | _ | 2 | |2 MeSH |a Muscle, Skeletal: enzymology |
| 650 | _ | 2 | |2 MeSH |a Phosphofructokinase-1: chemistry |
| 650 | _ | 2 | |2 MeSH |a Phosphofructokinase-1: genetics |
| 650 | _ | 2 | |2 MeSH |a Phosphofructokinase-1: metabolism |
| 650 | _ | 2 | |2 MeSH |a Phosphofructokinases: chemistry |
| 650 | _ | 2 | |2 MeSH |a Phosphofructokinases: genetics |
| 650 | _ | 2 | |2 MeSH |a Phosphofructokinases: metabolism |
| 650 | _ | 2 | |2 MeSH |a Rabbits |
| 650 | _ | 2 | |2 MeSH |a Saccharomyces cerevisiae: enzymology |
| 650 | _ | 2 | |2 MeSH |a Saccharomyces cerevisiae: genetics |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Fructosephosphates |
| 650 | _ | 7 | |0 6814-87-5 |2 NLM Chemicals |a fructose-6-phosphate |
| 650 | _ | 7 | |0 EC 2.7.1 - |2 NLM Chemicals |a Phosphofructokinases |
| 650 | _ | 7 | |0 EC 2.7.1.11 |2 NLM Chemicals |a Phosphofructokinase-1 |
| 693 | _ | _ | |a DORIS III |f DORIS Beamline BW7 |1 EXP:(DE-H253)DORISIII-20150101 |0 EXP:(DE-H253)D-BW7-20150101 |6 EXP:(DE-H253)D-BW7-20150101 |x 0 |
| 700 | 1 | _ | |a Mechin, I. |
| 700 | 1 | _ | |a Obmolova, G. |
| 700 | 1 | _ | |a Oldham, M. |
| 700 | 1 | _ | |a Chang, S. H. |
| 700 | 1 | _ | |a Ruiz, T. |
| 700 | 1 | _ | |a Radermacher, M. |
| 700 | 1 | _ | |a Kopperschlaeger, G. |
| 700 | 1 | _ | |a Rypniewski, W. |
| 773 | _ | _ | |0 PERI:(DE-600)1355192-9 |a 10.1016/j.jmb.2011.01.019 |g Vol. 407, p. 284-297 |p 284-297 |q 407<284-297 |t Journal of molecular biology |v 407 |x 0022-2836 |y 2011 |
| 909 | C | O | |o oai:bib-pubdb1.desy.de:95857 |p VDB |
| 910 | 1 | _ | |0 I:(DE-HGF)0 |a Externes Institut |k Extern |
| 913 | 1 | _ | |0 G:(DE-HGF)POF2-54G13 |1 G:(DE-HGF)POF2-540 |2 G:(DE-HGF)POF2-500 |9 G:(DE-H253)POF2-BW7-20130405 |b Struktur der Materie |v DORIS III |x 0 |a DE-H253 |4 G:(DE-HGF)POF |3 G:(DE-HGF)POF2 |l Forschung mit Photonen, Neutronen, Ionen |
| 914 | 1 | _ | |a (c) Elsevier B.V. Post referee full-text in progress. |y 2011 |
| 915 | _ | _ | |a JCR/ISI refereed |0 StatID:(DE-HGF)0010 |2 StatID |
| 915 | _ | _ | |a JCR |0 StatID:(DE-HGF)0100 |2 StatID |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)0150 |2 StatID |b Web of Science Core Collection |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)0199 |2 StatID |b Thomson Reuters Master Journal List |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)0300 |2 StatID |b Medline |
| 915 | _ | _ | |a No Author Disambiguation |0 StatID:(DE-HGF)1 |2 StatID |
| 920 | _ | 1 | |k EMBL |i European Molecular Biology Laboratory |
| 920 | 1 | _ | |0 I:(DE-H253)EMBL_-2012_-20130307 |k EMBL |l European Molecular Biology Laboratory |x 0 |
| 920 | _ | _ | |k 001 |
| 980 | _ | _ | |a PHPPUBDB |
| 980 | _ | _ | |a VDB |
| 980 | _ | _ | |a UNRESTRICTED |
| 980 | _ | _ | |a journal |
| 980 | _ | _ | |a I:(DE-H253)EMBL_-2012_-20130307 |
| 980 | _ | _ | |a ConvertedRecord |
| Library | Collection | CLSMajor | CLSMinor | Language | Author |
|---|