David I. Kreimer - Concepedia

Author

David I. Kreimer

Weizmann Institute of Science

Also Known As

D I Kreimer, D. Kreimer, D.I. Kreimer, David I. Kreimer, David Kreimer

Publications

340

Citations

H-Index

Concepts

All Affiliations

Weizmann Institute of Science Universidad de Salamanca University of California, Berkeley

About

David I. Kreimer is an author at Weizmann Institute of Science specializing in biochemistry, protein folding, and natural sciences.

Top Concepts

#	Concept	H-Index	Publications	Citations
1	Biochemistry	6	6	177
2	Medicine	4	4	102
3	Natural Sciences	4	4	102
4	Molecular Biology	4	4	102
5	Microbiology	1	1	23

David I. Kreimer

Publications

324

Citations

H-Index

Page 1

	Year	Citations
Oxidative Stress Transforms Acetylcholinesterase to a Molten Globule-like State Lev Weiner, David I. Kreimer, Esther Roth, Biochemical and Biophysical Research Communications Molten Globule-like StateBiochemistryProtein FoldingEnzyme CatalysisStructure-function Enzyme Kinetics	1994	59
Irreversible thermal denaturation of<i>Torpedo californica</i>acetylcholinesterase David I. Kreimer, Valery L. Shnyrov, Enrique Villar, Protein Science	1995	50
Cadmium‐induced crystallization of proteins: II. Crystallization of the Salmonella typhimuri histidine‐binding protein in complex with L‐histidine, L‐arginine, or L‐lysine Giovanna Ferro‐Luzzi Ames, David I. Kreimer, S. Trakhanov, Protein Science	1998	34
Membrane-promoted unfolding of acetylcholinesterase: A possible mechanism for insertion into the lipid bilayer Irina Shin, David I. Kreimer, Israel Silman, Proceedings of the National Academy of Sciences Membrane-promoted UnfoldingProteinlipid InteractionChemical ModificationMolecular BiologyLipid Movement	1997	33
Nonequivalence of the Nucleotide-Binding Subunits of an ABC Transporter, the Histidine Permease, and Conformational Changes in the Membrane Complex David I. Kreimer, Giovanna Ferro‐Luzzi Ames Biochemistry Proteinlipid InteractionVarious Thiol-specific ReagentsNucleotide-binding SubunitsTraffic AtpaseBiochemistry	2000	28
A Metastable State of Torpedo californica Acetylcholinesterase Generated by Modification with Organomercurials David I. Kreimer, Elena A. Dolginova, Mia L. Raves, Biochemistry	1994	25
Thermodynamics and dynamics of histidine‐binding protein, the water‐soluble receptor of histidine permease David I. Kreimer, H. Malak, Joseph R. Lakowicz, European Journal of Biochemistry Closed ConformationMolecular BiologyIntrinsic Hisj FluorescenceProtein FoldingMembrane Transport	2000	23
A “molten globule” of Torpedo acetylcholinesterase undergoes thiol-disulfide exchange. Jerry Eichler, David I. Kreimer, Larry E. Varon, Journal of Biological Chemistry	1994	21
Two-state transition between molten globule and unfolded states of acetylcholinesterase as monitored by electron paramagnetic resonance spectroscopy. David I. Kreimer, Reuven Szosenfogel, D. Goldfarb, Proceedings of the National Academy of Sciences Magnetic ResonanceMolecular BiologyEnzymatic ModificationProtein FoldingElectron Paramagnetic Resonance	1994	18
Two partially unfolded states of<i>torpedo californica</i>acetylcholinesterase David I. Kreimer, Irina Shin, Israel Silman, Protein Science	1996	17

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