Physician

Otolaryngology (ENT)

Dr. Thomas R. Schneider practices Otolaryngology (ENT). He went to medical school at Georgetown University School of Medicine. Georgetown University School of Medicine is ranked 49 in research and 84 in primary care medicine He received awards:"Fellow (FACS)". Thomas Schneider has written publications. He has 39 publications published with PubMed. The lastest paper is: 'Influence of internal dynamics on accuracy of protein NMR structures: derivation of realistic model distance data from a long molecular dynamics trajectory.'

Publications

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• Substructure determination in isomorphous replacement and anomalous diffraction experiments.
• Crystal structure of the ubiquitin binding domains of rabex-5 reveals two modes of interaction with ubiquitin.
• Mechanism of Aurora B activation by INCENP and inhibition by hesperadin.
• Structural basis for the autoinhibition and STI-571 inhibition of c-Kit tyrosine kinase.
• Ultrahigh resolution drug design. II. Atomic resolution structures of human aldose reductase holoenzyme complexed with Fidarestat and Minalrestat: implications for the...
• Molecular basis for redox-Bohr and cooperative effects in cytochrome c3 from Desulfovibrio desulfuricans ATCC 27774: crystallographic and modeling studies of oxidized ...
• Evolution of feedback-inhibited beta /alpha barrel isoenzymes by gene duplication and a single mutation.
• Automatic solution of heavy-atom substructures.
• Structural information content at high resolution: MAD versus native.
• Crystal structure of the endosomal SNARE complex reveals common structural principles of all SNAREs.
• Crystal structure of domain A of Thermus flavus 5S rRNA and the contribution of water molecules to its structure.
• Loop closure and intersubunit communication in tryptophan synthase.
• Contribution of the intramolecular disulfide bridge to the folding stability of REIv, the variable domain of a human immunoglobulin kappa light chain.
• X-ray snapshots of serine protease catalysis reveal a tetrahedral intermediate.
• Influence of internal dynamics on accuracy of protein NMR structures: derivation of realistic model distance data from a long molecular dynamics trajectory.
• SHELXL: high-resolution refinement.
• Crystal structure of vancomycin.
• Comparison of different X-ray data-collection systems using the crystal structure of octreotide.
• Refinement of triclinic hen egg-white lysozyme at atomic resolution.
• 1.7 A structure of the stabilized REIv mutant T39K. Application of local NCS restraints.
• Objective comparison of protein structures: error-scaled difference distance matrices.
• Ab initio structure determination of the lantibiotic mersacidin.
• Structure of balhimycin and its complex with solvent molecules.
• Ultrahigh resolution drug design I: details of interactions in human aldose reductase-inhibitor complex at 0.66 A.
• X-ray crystallography reveals stringent conservation of protein fold after removal of the only disulfide bridge from a stabilized immunoglobulin variable domain.
• Crystallization and preliminary X-ray analysis of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase (tyrosine inhibitable) from Saccharomyces cerevisiae.
• Optimization of selenium substructures as obtained from SHELXD.
• Structure of the alpha-amylase inhibitor tendamistat at 0.93 A.
• Use of multiple anomalous dispersion to phase highly merohedrally twinned crystals of interleukin-1beta.
• Substrate and metal complexes of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Saccharomyces cerevisiae provide new insights into the catalytic mechanism.
• Substructure solution with SHELXD.
• A genetic algorithm for the identification of conformationally invariant regions in protein molecules.
• Domain identification by iterative analysis of error-scaled difference distance matrices.
• RAPIDO: a web server for the alignment of protein structures in the presence of conformational changes.
• The atomic resolution structure of human aldose reductase reveals that rearrangement of a bound ligand allows the opening of the safety-belt loop.
• Synchrotron radiation: micrometer-sized x-ray beams as fine tools for macromolecular crystallography.
• Alignment of protein structures in the presence of domain motions.
• Structure of Ecballium elaterium trypsin inhibitor II (EETI-II): a rigid molecular scaffold.

Schools

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• Georgetown University

• Nat39l Naval Med Center

• Naval Hospital

Conditions Treated

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• Gastroesophageal Reflux Disease (GERD)
• Headache
• Vertigo

Doctors Specialties

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• Ear, Nose, and Throat
• Family Medicine
• Otolaryngology (ENT)

Accepted Insurances

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• Aetna
• Blue Cross Blue Shield
• Cigna
• Commercial Insurance Company
• Medicare MCR
• Tricare
• United Healthcare

Awards

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• Fellow (FACS)

Education

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• National Capital Consortium
• Georgetown University School of Medicine

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