Edward E. Melnikov - Concepedia

Author

Edward E. Melnikov

Institute of Bioorganic Chemistry

Also Known As

E E Mel'nikov, E. E. Mel'nikov, E. E. Melnikov, E. E. Mel’nikov, E.E. Melnikov, Edward E Melnikov, Edward E. Melnikov

Publications

762

Citations

H-Index

Concepts

All Affiliations

Institute of Bioorganic Chemistry Frederick National Laboratory for Cancer Research National Cancer Institute Science Applications International Corporation (United States)National Institute of Diabetes and Digestive and Kidney Diseases

About

Edward E. Melnikov is an author at Institute of Bioorganic Chemistry specializing in structural biology, molecular biology, and biochemistry.

Top Concepts

#	Concept	H-Index	Publications	Citations
1	Natural Sciences	4	4	149
2	Biochemistry	4	4	149
3	Molecular Biology	4	4	149
4	Structural Biology	4	4	149
5	Medicine	2	2	44

Edward E. Melnikov

Publications

505

Citations

H-Index

Page 1

	Year	Citations
The Catalytic Domain of Escherichia coli Lon Protease Has a Unique Fold and a Ser-Lys Dyad in the Active Site Istvan Botos, Edward E. Melnikov, Scott Cherry, Journal of Biological Chemistry	2004	192
Classification of ATP‐dependent proteases Lon and comparison of the active sites of their proteolytic domains Edward E. Melnikov, Anna G. Khalatova, O.V. Makhovskaya, European Journal of Biochemistry	2004	102
Crystal structure of the N‐terminal domain of <i>E. coli</i> Lon protease Mi Li, Fatima Rasulova, Edward E. Melnikov, Protein Science Crystal StructureBiochemistryBiomolecular Structure PredictionNatural SciencesStructural Bioinformatics	2005	55
Atomic-resolution Crystal Structure of the Proteolytic Domain of Archaeoglobus fulgidus Lon Reveals the Conformational Variability in the Active Sites of Lon Proteases Istvan Botos, Edward E. Melnikov, Scott Cherry, Journal of Molecular Biology Atomic-resolution Crystal StructureBiochemistryProtein AssemblyNatural SciencesLon Proteases	2005	50
Structure of the N-terminal fragment of<i>Escherichia coli</i>Lon protease Mi Li, Alla Gustchina, Fatima Rasulova, Acta Crystallographica Section D Biological Crystallography	2010	36
The isolated proteolytic domain of <i>Escherichia coli</i> ATP‐dependent protease Lon exhibits the peptidase activity Fatima Rasulova, Natalie N Starkova, Edward E. Melnikov, FEBS Letters	1998	26
Limited proteolysis of E. coli ATP-dependent protease Lon - a unified view of the subunit architecture and characterization of isolated enzyme fragments. Edward E. Melnikov, A.D. Morozkin, Anton A. Stepnov, PubMed Protein AssemblyProteasomeMolecular BiologyEscherichia ColiProtein Folding	2008	23
Limited proteolysis of E. coli ATP-dependent protease Lon - a unified view of the subunit architecture and characterization of isolated enzyme fragments. Edward E. Melnikov, A.D. Morozkin, Anton A. Stepnov, Acta Biochimica Polonica Protein AssemblyProteasomeMolecular BiologyEscherichia ColiProtein Folding	2008	21

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