M K Sardana - Concepedia

Concepedia

Author

M K Sardana

United States Military Academy

Also Known As

M K Sardana, M SARDANA, M Sardana, M. K. Sardana, M. SARDANA, M. Sardana, M.K. Sardana, Madhur Sardana, Mishika Sardana, Muskan Sardana

26

Publications

1.3K

Citations

16

H-Index

72

Concepts

All Affiliations

United States Military Academy Rockefeller University Hospital Merck & Co., Inc., Rahway, NJ, USA (United States)Institute of Molecular Biology and Pathology

MK

About

M K Sardana is an author at United States Military Academy specializing in medicine, biochemistry, and pharmacology.

Top Concepts

#	Concept	H-Index	Publications	Citations
1	Medicine	11	12	858
2	Natural Sciences	8	8	558
3	Health Sciences	3	3	264
4	Engineering	2	2	104
5	Public Health	1	1	10

M K Sardana

×

18

Publications

1.3K

Citations

16

H-Index

	Year	Citations
Echistatin is a potent inhibitor of bone resorption in culture. Masahiko Sato, M K Sardana, W A Grasser, The Journal of Cell Biology SclerostinBone ResorptionAntibody LocalizationOsteoporosisBone Morphogenic Protein	1990	200
Dual control mechanism for heme oxygenase: tin(IV)-protoporphyrin potently inhibits enzyme activity while markedly increasing content of enzyme protein in liver. M K Sardana, A Kappas Proceedings of the National Academy of Sciences Molecular BiologyChemical BiologyRedox BiologyOxidative StressEnzyme Protein	1987	168
Antistasin, a Leech-derived Inhibitor of Factor Xa Christopher T. Dunwiddie, Nancy A. Thornberry, Herbert G. Bull, Journal of Biological Chemistry	1989	156
Activity of purified hepatitis C virus protease NS3 on peptide substrates Christian Steinkühler, Andrea Urbani, Licia Tomei, Journal of Virology	1996	142
Characterization of recombinant tick anticoagulant peptide. A highly selective inhibitor of blood coagulation factor Xa. Michael P. Neeper, Lloyd Waxman, Donna Smith, Journal of Biological Chemistry Tick Anticoagulant PeptideProtein SecretionImmunologyMolecular BiologyThrombosis	1990	105
Molecular model of the specificity pocket of the hepatitis C virus protease: implications for substrate recognition. Elisabetta Pizzi, Anna Tramontano, Licia Tomei, Proceedings of the National Academy of Sciences Structural BioinformaticsMolecular BiologyViral Structural ProteinVirus StructureViral Hepatitis	1994	93
Aspartyl beta-hydroxylase: in vitro hydroxylation of a synthetic peptide based on the structure of the first growth factor-like domain of human factor IX. Robert S. Gronke, William J. VanDusen, V M Garsky, Proceedings of the National Academy of Sciences Aspartic AcidEngineeringAldo-keto ReductaseHuman GrowthPeptide Engineering	1989	82
A fully active catalytic domain of bovine aspartyl (asparaginyl) beta-hydroxylase expressed in Escherichia coli: characterization and evidence for the identification of an active-site region in vertebrate alpha-ketoglutarate-dependent dioxygenases. Steve Jia, Kathleen A. McGinnis, William J. VanDusen, Proceedings of the National Academy of Sciences Alanine ResidueAldo-keto ReductaseActive Catalytic DomainBiochemistryCellular Enzymology	1994	56
Partial purification and characterization of bovine liver aspartyl beta-hydroxylase. Robert S. Gronke, D. Welsch, William J. VanDusen, Journal of Biological Chemistry Additional DetergentAldehyde DehydrogenaseCellular EnzymologyBiochemistryVitro Hydroxylation	1990	51
Metal ion-mediated regulation of heme oxygenase induction in cultured avian liver cells. M K Sardana, Shigeru Sassa, Attallah Kappas Journal of Biological Chemistry Iron MetabolismMetal Ion-mediated RegulationRedox BiologyOxidative StressToxicology	1982	48

Page 1