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KENNETH HAMPEL, PH.D.
PH.D.
Laboratory Management Specialist/Technologist
NPI: 1821962333Individual
Specialties, Licenses & Credentials
Laboratory Management Specialist/TechnologistPrimary
Specialist/Technologist, Pathology — Laboratory Management
Code: 246QL0900X
Research & Publications (16)
Phosphopeptide ligands of the SHP-1 N-SH2 domain: effects on binding and stimulation of phosphatase activity.
PMID 16902940·ChemMedChem·2006
8-other
A rate-limiting conformational step in the catalytic pathway of the glmS ribozyme.
PMID 19449899·Biochemistry·2009
8-other
An ontological knowledge framework for adaptive medical workflow.
PMID 18602872·J Biomed Inform·2008
8-other
Monitoring phosphatase reactions of multiple phosphorylated substrates by reversed-phase HPLC.
PMID 17416557·J Chromatogr B Analyt Technol Biomed Life Sci·2007
8-other
Inheritance of mitochondrial DNA recombinants in double-heteroplasmic families: potential implications for phylogenetic analysis.
PMID 17236134·Am J Hum Genet·2007
8-other
Evidence for preorganization of the glmS ribozyme ligand binding pocket.
PMID 16784238·Biochemistry·2006
8-other
Design and biological evaluation of linear and cyclic phosphopeptide ligands of the N-terminal SH2 domain of protein tyrosine phosphatase SHP-1.
PMID 15743195·J Med Chem·2005
8-other
Synthesis of linear and cyclic phosphopeptides as ligands for the N-terminal SH2-domain of protein tyrosine phosphatase SHP-1.
PMID 15635669·J Pept Sci·2005
8-other
In vitro selection of second site revertants analysis of the hairpin ribozyme active site.
PMID 14555657·J Biol Chem·2003
8-other
Solvent protection of the hammerhead ribozyme in the ground state: evidence for a cation-assisted conformational change leading to catalysis.
PMID 12693938·Biochemistry·2003
8-other
Functional involvement of G8 in the hairpin ribozyme cleavage mechanism.
PMID 11707414·EMBO J·2001
8-other
A base change in the catalytic core of the hairpin ribozyme perturbs function but not domain docking.
PMID 11327881·Biochemistry·2001
8-other
A conformational change in the "loop E-like" motif of the hairpin ribozyme is coincidental with domain docking and is essential for catalysis.
PMID 11297441·Biochemistry·2001
8-other
Time-resolved hydroxyl-radical footprinting of RNA using Fe(II)-EDTA.
PMID 11243836·Methods·2001
8-other
The hairpin ribozyme substrate binding-domain: a highly constrained D-shaped conformation.
PMID 11243803·J Mol Biol·2001
8-other
Data courtesy of the U.S. National Library of Medicine (NLM). Ltrl is not affiliated with or endorsed by NLM.
Contact & Hours
- Address
- 251 E HURON ST
CHICAGO, IL 60611 - Phone
- (312) 926-2000
Quick Facts
- NPI
- 1821962333
- Entity Type
- Individual
- Gender
- Male
- Medicare
- Not confirmed
- Specialties
- 1
- Locations
- 1
- Publications
- 16
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