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2vom
From Proteopedia
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===STRUCTURAL BASIS OF HUMAN TRIOSEPHOSPHATE ISOMERASE DEFICIENCY. MUTATION E104D AND CORRELATION TO SOLVENT PERTURBATION.=== | ===STRUCTURAL BASIS OF HUMAN TRIOSEPHOSPHATE ISOMERASE DEFICIENCY. MUTATION E104D AND CORRELATION TO SOLVENT PERTURBATION.=== | ||
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| + | The line below this paragraph, {{ABSTRACT_PUBMED_18562316}}, adds the Publication Abstract to the page | ||
| + | (as it appears on PubMed at http://www.pubmed.gov), where 18562316 is the PubMed ID number. | ||
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| + | {{ABSTRACT_PUBMED_18562316}} | ||
==About this Structure== | ==About this Structure== | ||
2VOM is a 4 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VOM OCA]. | 2VOM is a 4 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VOM OCA]. | ||
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| + | ==Reference== | ||
| + | <ref group="xtra">PMID:18562316</ref><references group="xtra"/> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Triose-phosphate isomerase]] | [[Category: Triose-phosphate isomerase]] | ||
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[[Category: Polymorphism]] | [[Category: Polymorphism]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jan 18 09:24:31 2010'' |
Revision as of 07:24, 18 January 2010
STRUCTURAL BASIS OF HUMAN TRIOSEPHOSPHATE ISOMERASE DEFICIENCY. MUTATION E104D AND CORRELATION TO SOLVENT PERTURBATION.
Template:ABSTRACT PUBMED 18562316
About this Structure
2VOM is a 4 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Rodriguez-Almazan C, Arreola R, Rodriguez-Larrea D, Aguirre-Lopez B, de Gomez-Puyou MT, Perez-Montfort R, Costas M, Gomez-Puyou A, Torres-Larios A. Structural basis of human triosephosphate isomerase deficiency: mutation E104D is related to alterations of a conserved water network at the dimer interface. J Biol Chem. 2008 Aug 22;283(34):23254-63. Epub 2008 Jun 18. PMID:18562316 doi:10.1074/jbc.M802145200
Page seeded by OCA on Mon Jan 18 09:24:31 2010
Categories: Homo sapiens | Triose-phosphate isomerase | Aguirre-Lopez, B. | Arreola-Alemon, R. | Costas, M. | Gomez-Puyou, A. | Gomez-Puyou, M T.De. | Perez-Montfort, R. | Rodriguez-Almazan, C. | Rodriguez-Larrea, D. | Torres-Larios, A. | Acetylation | Alternative splicing | Disease mutation | Fatty acid biosynthesis | Gluconeogenesis | Glycolysis | Isomerase | Lipid synthesis | Pentose shunt | Phosphoprotein | Polymorphism
