Mr. Victor L Schramm MD
Ear-Nose and Throat Doctor (ENT)
1601 E 19th Ave Suite 3100 Denver CO, 80218About
Dr. Victor Schramm is an ear, nose and throat (ENT) doctor, also known as an otolaryngologist, practicing in Denver, CO. Dr. Schramm specializes in diseases and disorders of the ear, nose and throat as well as other parts of the head and neck. Such structures an ENT may work on include the sinuses, larynx (voice box) and mouth in addition to the ear, nose and throat. There are seven areas of expertise that an ENT might specialize in, and these are: allergies; facial reconstructive surgery; head and neck; laryngology; otology/neurotology; pediatric otolaryngology; and rhinology.
Education and Training
University of Iowa Medical School MD
Board Certification
OtolaryngologyAmerican Board of OtolaryngologyABOto
Provider Details
Expert Publications
Data provided by the National Library of Medicine- Transition-state analogs as inhibitors of human and malarial hypoxanthine-guanine phosphoribosyltransferases.
- The 2.0 A structure of human hypoxanthine-guanine phosphoribosyltransferase in complex with a transition-state analog inhibitor.
- Nucleoside hydrolase from Leishmania major. Cloning, expression, catalytic properties, transition state inhibitors, and the 2.5-å crystal structure.
- The 2.0 A structure of malarial purine phosphoribosyltransferase in complex with a transition-state analogue inhibitor.
- Enzymatic transition-state analysis and transition-state analogs.
- Iminoribitol transition state analogue inhibitors of protozoan nucleoside hydrolases.
- Prediction of inhibitor binding free energies by quantum neural networks. Nucleoside analogues binding to trypanosomal nucleoside hydrolase.
- Transition state analogue inhibitors of protozoan nucleoside hydrolases.
- Radiation-associated disease: disease incidence and cost effectiveness of follow-up.
- Radiation-associated disease: disease incidence and cost effectiveness of follow-up.
- Crystal structures of Giardia lamblia guanine phosphoribosyltransferase at 1.75 A(,).
- Immucillin-H binding to purine nucleoside phosphorylase reduces dynamic solvent exchange.
- 5'-Deoxyadenosine contacts the substrate radical intermediate in the active site of ethanolamine ammonia-lyase: 2H and 13C electron nuclear double resonance studies.
- Transition state structure of purine nucleoside phosphorylase and principles of atomic motion in enzymatic catalysis.
- Immucillin H, a powerful transition-state analog inhibitor of purine nucleoside phosphorylase, selectively inhibits human T lymphocytes.
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