Physician
Anesthesiology
Dr. Christopher Dobson, MD
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Christopher Dobson works in the field of Anesthesiology. He researched medicine at Baylor College of Medicine. Christopher Dobson is also a published doctor. He has 101 publication published. The most recent publication is: Direct observation of the three regions in -synuclein that determine its membrane-bound behaviour.
Publications
- Higher Order Amyloid Fibril Structure by MAS NMR and DNP Spectroscopy.
- Widespread aggregation and neurodegenerative diseases are associated with supersaturated proteins.
- Direct observation of the three regions in α-synuclein that determine its membrane-bound behaviour.
- Targeting the Intrinsically Disordered Structural Ensemble of α-Synuclein by Small Molecules as a Potential Therapeutic Strategy for Parkinson's Disease.
- Mutations in the MMAA gene in patients with the cblA disorder of vitamin B12 metabolism.
- Lactobacillus casei, Lactobacillus rhamnosus, and Lactobacillus zeae isolates identified by sequence signature and immunoblot phenotype.
- Identification of the gene responsible for the cblA complementation group of vitamin B12-responsive methylmalonic acidemia based on analysis of prokaryotic gene arrang...
- Identification of the gene responsible for methylmalonic aciduria and homocystinuria, cblC type.
- Genome-wide analysis of signaling networks regulating fatty acid-induced gene expression and organelle biogenesis.
- Reclassification of Pediococcus dextrinicus (Coster and White 1964) back 1978 (Approved Lists 1980) as Lactobacillus dextrinicus comb. nov., and emended description of...
- Identification of the gene responsible for the cblB complementation group of vitamin B12-dependent methylmalonic aciduria.
- Phylogenetic analysis of the genus Pediococcus, including Pediococcus claussenii sp. nov., a novel lactic acid bacterium isolated from beer.
- Mutation and biochemical analysis of patients belonging to the cblB complementation class of vitamin B12-dependent methylmalonic aciduria.
- Homozygous nonsense mutation in the MCEE gene and siRNA suppression of methylmalonyl-CoA epimerase expression: a novel cause of mild methylmalonic aciduria.
- Impact of cblB mutations on the function of ATP:cob(I)alamin adenosyltransferase in disorders of vitamin B12 metabolism.
- Structure of the regulatory apparatus of a calcium-dependent protein kinase (CDPK): a novel mode of calmodulin-target recognition.
- Folding and fibril formation of the cell cycle protein Cks1.
- Expanding to fill the gap: a possible role for inert biopolymers in regulating the extent of the ''macromolecular crowding'' effect.
- Protein aggregation and its consequences for human disease.
- Cytochrome display on amyloid fibrils.
- Impact of the native-state stability of human lysozyme variants on protein secretion by Pichia pastoris.
- Enthalpic and entropic contributions mediate the role of disulfide bonds on the conformational stability of interleukin-4.
- Probing the mechanism of amyloidogenesis through a tandem repeat of the PI3-SH3 domain suggests a generic model for protein aggregation and fibril formation.
- Amyloid fibril formation by bovine milk kappa-casein and its inhibition by the molecular chaperones alphaS- and beta-casein.
- The importance of sequence diversity in the aggregation and evolution of proteins.
- Probing the pressure-temperature stability of amyloid fibrils provides new insights into their molecular properties.
- Molecular conformation of a peptide fragment of transthyretin in an amyloid fibril.
- De novo designed peptide-based amyloid fibrils.
- Competition between folding, native-state dimerisation and amyloid aggregation in beta-lactoglobulin.
- Self-templated nucleation in peptide and protein aggregation.
- Amyloid formation by globular proteins under native conditions.
- alpha2-Macroglobulin and haptoglobin suppress amyloid formation by interacting with prefibrillar protein species.
- A generic mechanism of emergence of amyloid protofilaments from disordered oligomeric aggregates.
- Recombinant amyloid beta-peptide production by coexpression with an affibody ligand.
- Engineering a camelid antibody fragment that binds to the active site of human lysozyme and inhibits its conversion into amyloid fibrils.
- Mutational analysis of the aggregation-prone and disaggregation-prone regions of acylphosphatase.
- Direct characterization of amyloidogenic oligomers by single-molecule fluorescence.
- Structure and dynamics of a partially folded protein are decoupled from its mechanism of aggregation.
- Immunological features of alpha-synuclein in Parkinson''s disease.
- Characterizing the first steps of amyloid formation for the ccbeta peptide.
- Prediction of aggregation-prone regions in structured proteins.
- Calculation of the free energy barriers in the oligomerisation of Abeta peptide fragments.
- A coupled equilibrium shift mechanism in calmodulin-mediated signal transduction.
- Molecular determinants of the aggregation behavior of alpha- and beta-synuclein.
- Measurement of amyloid fibril length distributions by inclusion of rotational motion in solution NMR diffusion measurements.
- Conservation of mechanism, variation of rate: folding kinetics of three homologous four-helix bundle proteins.
- Characterization of folding the four-helix bundle protein Rop by real-time NMR.
- Protein misfolding and disease: from the test tube to the organism.
- Determination of the transition state ensemble for the folding of ubiquitin from a combination of Phi and Psi analyses.
- Functionalised amyloid fibrils for roles in cell adhesion.
- Role of intermolecular forces in defining material properties of protein nanofibrils.
- Importance of metastable states in the free energy landscapes of polypeptide chains.
- Systematic in vivo analysis of the intrinsic determinants of amyloid Beta pathogenicity.
- Structural reorganisation and potential toxicity of oligomeric species formed during the assembly of amyloid fibrils.
- Structure and dynamics of a ribosome-bound nascent chain by NMR spectroscopy.
- Chemical biology: More charges against aggregation.
- Contribution of rotational diffusion to pulsed field gradient diffusion measurements.
- Characterisation of amyloid fibril formation by small heat-shock chaperone proteins human alphaA-, alphaB- and R120G alphaB-crystallins.
- Kinetics and thermodynamics of amyloid formation from direct measurements of fluctuations in fibril mass.
- Protein structure determination from NMR chemical shifts.
- Similarities in the thermodynamics and kinetics of aggregation of disease-related Abeta(1-40) peptides.
- Life on the edge: a link between gene expression levels and aggregation rates of human proteins.
- The extracellular chaperone clusterin influences amyloid formation and toxicity by interacting with prefibrillar structures.
- The extracellular chaperone clusterin potently inhibits human lysozyme amyloid formation by interacting with prefibrillar species.
- Geometry, energetics, and dynamics of hydrogen bonds in proteins: structural information derived from NMR scalar couplings.
- Recombinant amyloidogenic domain of ApoA-I: analysis of its fibrillogenic potential.
- Nature and significance of the interactions between amyloid fibrils and biological polyelectrolytes.
- Characterization of the nanoscale properties of individual amyloid fibrils.
- Protein unfolding, amyloid fibril formation and configurational energy landscapes under high pressure conditions.
- Normal and aberrant biological self-assembly: Insights from studies of human lysozyme and its amyloidogenic variants.
- Structural biology. Dynamic visions of enzymatic reactions.
- X-ray scattering study of the effect of hydration on the cross-beta structure of amyloid fibrils.
- Prefibrillar amyloid aggregates could be generic toxins in higher organisms.
- Identification of the core structure of lysozyme amyloid fibrils by proteolysis.
- Spatial persistence of angular correlations in amyloid fibrils.
- The component polypeptide chains of bovine insulin nucleate or inhibit aggregation of the parent protein in a conformation-dependent manner.
- Protein misfolding, functional amyloid, and human disease.
- An accidental breach of a protein's natural defenses.
- Apomyoglobin reveals a random-nucleation mechanism in amyloid protofibril formation.
- The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-?(1-40) peptide.
- Experimental free energy surfaces reveal the mechanisms of maintenance of protein solubility.
- Hydrophobicity and conformational change as mechanistic determinants for nonspecific modulators of amyloid ? self-assembly.
- Inversion of the balance between hydrophobic and hydrogen bonding interactions in protein folding and aggregation.
- Nucleated polymerisation in the presence of pre-formed seed filaments.
- Probing small molecule binding to amyloid fibrils.
- Disease-related amyloidogenic variants of human lysozyme trigger the unfolded protein response and disturb eye development in Drosophila melanogaster.
- Binding of the Molecular Chaperone ?B-Crystallin to A? Amyloid Fibrils Inhibits Fibril Elongation.
- Observation of spatial propagation of amyloid assembly from single nuclei.
- Nucleated polymerization with secondary pathways. III. Equilibrium behavior and oligomer populations.
- Nucleated polymerization with secondary pathways. II. Determination of self-consistent solutions to growth processes described by non-linear master equations.
- Nucleated polymerization with secondary pathways. I. Time evolution of the principal moments.
- Label-free detection of amyloid growth with microcantilever sensors.
- Protein solubility and protein homeostasis: a generic view of protein misfolding disorders.
- Native-state stability determines the extent of degradation relative to secretion of protein variants from Pichia pastoris.
- In situ measurements of the formation and morphology of intracellular ?-amyloid fibrils by super-resolution fluorescence imaging.
- Intermolecular structure determination of amyloid fibrils with magic-angle spinning and dynamic nuclear polarization NMR.
- Probing protein aggregation with quartz crystal microbalances.
- Solution-state nuclear magnetic resonance spectroscopy and protein folding.
- The iFly tracking system for an automated locomotor and behavioural analysis of Drosophila melanogaster.
- Conserved C-terminal charge exerts a profound influence on the aggregation rate of α-synuclein.
Schools
Oxford University MedSchool
Baylor College Med
Bowman Gray School Med
Doctors Specialties
- Anesthesiology
- Pediatric Anesthesiology
Accepted Insurances
- Amerigroup (Wellpoint)
- Cigna
- Commercial Insurance Company
- Harvard Pilgrim Health Care PPO
- Medicare Advantage PFFS
- Humana
- Medicare MCR
- Medico
- POMCO Group
- United Healthcare
Education
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Wake Forest University -
Baylor College of Medicine
Helpful Reviews
Medicare Facts
| National Provider Identifier [NPI] | 1720074008 |
| Last Name Of The Provider | DOBSON |
| First Name Of The Provider | CHRISTOPHER |
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