S. Gover - Concepedia

Concepedia

Author

S. Gover

University of Oxford

Also Known As

S Gover, S. Gover, SHEILA GOVER, Sheila Gover

32

Publications

1.2K

Citations

14

H-Index

14

Concepts

All Affiliations

University of Oxford MRC Laboratory of Molecular Biology University of Hong Kong Syracuse University

SG

About

S. Gover is an author at University of Oxford specializing in natural sciences, molecular biology, and biochemistry.

Top Concepts

#	Concept	H-Index	Publications	Citations
1	Natural Sciences	9	9	824
2	Biochemistry	9	9	748
3	Medicine	7	7	679
4	Metabolism	3	3	361
5	Microbiology	1	1	55

S. Gover

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13

Publications

1.2K

Citations

13

H-Index

	Year	Citations
Human glucose-6-phosphate dehydrogenase: the crystal structure reveals a structural NADP + molecule and provides insights into enzyme deficiency Shannon WN Au, S. Gover, Veronica Lam, Structure Crystal StructureCellular EnzymologyBiochemistryNatural SciencesEnzyme Deficiency	2000	281
Structural studies of glucose-6-phosphate and NADP<sup>+</sup>binding to human glucose-6-phosphate dehydrogenase Masayo Kotaka, S. Gover, Lucy Vandeputte-Rutten, Acta Crystallographica Section D Biological Crystallography	2005	173
The three–dimensional structure of glucose 6–phosphate dehydrogenase from Leuconostoc mesenteroides refined at 2.0 Å resolution Paul Rowland, Ajit K. Basak, S. Gover, Structure Aldo-keto ReductaseCellular EnzymologyBiochemistryBioenergeticsNatural Sciences	1994	132
Millisecond X-ray diffraction and the first electron density map from Laue photographs of a protein crystal János Hajdu, P. A. Machin, John W. Campbell, Nature X-ray CrystallographyCrystal StructureMillisecond X-ray DiffractionProtein FoldingNatural Sciences	1987	131
Crystallographic study of coenzyme, coenzyme analogue and substrate binding in 6-phosphogluconate dehydrogenase: implications for NADP specificity and the enzyme mechanism Margaret Adams, Grant H Ellis, S. Gover, Structure Nadp SpecificityEnzyme MechanismBiochemistryNatural SciencesMolecular Biology	1994	100
Glucose 6-phosphate dehydrogenase mutations causing enzyme deficiency in a model of the tertiary structure of the human enzyme CE Naylor, Paul Rowland, A. K. Basak, Blood	1996	83
A 2.8 Å resolution structure of 6-phosphogluconate dehydrogenase from the protozoan parasite Trypanosoma brucei : comparison with the sheep enzyme accounts for differences in activity with coenzyme and substrate analogues 1 1Edited by R. Huber Christopher Phillips, Jan Dohnálek, S. Gover, Journal of Molecular Biology Cellular EnzymologyBiochemistryParasitic ProtozoaAfrican TrypanosomiasisR. Huber	1998	55
An Examination of the Role of Asp-177 in the His-Asp Catalytic Dyad of <i>Leuconostoc mesenteroides</i> Glucose 6-Phosphate Dehydrogenase: X-ray Structure and pH Dependence of Kinetic Parameters of the D177N Mutant Enzyme<sup>,</sup> Michael S. Cosgrove, S. Gover, C.E. Naylor, Biochemistry Cellular EnzymologyBiochemistryNormal Enzyme ActivityCatalytic DyadNatural Sciences	2000	51
Solution of the structure of tetrameric human glucose 6-phosphate dehydrogenase by molecular replacement Shannon Wing‐Ngor Au, C.E. Naylor, S. Gover, Acta Crystallographica Section D Biological Crystallography Molecular ReplacementAldehyde DehydrogenaseCellular EnzymologyBiochemistryBiomolecular Structure Prediction	1999	49
NADP<sup>+</sup>and NAD<sup>+</sup>binding to the dual coenzyme specific enzyme<i>Leuconostoc mesenteroides</i>glucose 6-phosphate dehydrogenase: different interdomain hinge angles are seen in different binary and ternary complexes C.E. Naylor, S. Gover, Ajit K. Basak, Acta Crystallographica Section D Biological Crystallography	2001	39

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