Physician
Anesthesiology
Dr. George W. Farr Jr., MD
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George Farr is an expert in the field of Anesthesiology. He attended University of Alabama Medical Center. University of Alabama Medical Center is ranked 37 in research and 17 in primary care medicine George W. Farr Jr., MD is also published. He has 19 publications published. The lastest publication: "Yeast Gis2 and its human ortholog CNBP are novel components of stress-induced RNP granules.' Doctor George W. Farr Jr., MD is registered with Medicare.
Publications
- Yeast Gis2 and its human ortholog CNBP are novel components of stress-induced RNP granules.
- Hydrogen-deuterium exchange in vivo to measure turnover of an ALS-associated mutant SOD1 protein in spinal cord of mice.
- Progressive aggregation despite chaperone associations of a mutant SOD1-YFP in transgenic mice that develop ALS.
- An ALS-linked mutant SOD1 produces a locomotor defect associated with aggregation and synaptic dysfunction when expressed in neurons of Caenorhabditis elegans.
- Requirement for binding multiple ATPs to convert a GroEL ring to the folding-active state.
- Multiple states of a nucleotide-bound group 2 chaperonin.
- Topologies of a substrate protein bound to the chaperonin GroEL.
- Perturbed ATPase activity and not "close confinement" of substrate in the cis cavity affects rates of folding by tail-multiplied GroEL.
- Two families of chaperonin: physiology and mechanism.
- Global aggregation of newly translated proteins in an Escherichia coli strain deficient of the chaperonin GroEL.
- GroEL-GroES-mediated protein folding.
- Allosteric signaling of ATP hydrolysis in GroEL-GroES complexes.
- Loops in the central channel of ClpA chaperone mediate protein binding, unfolding, and translocation.
- A mutant chaperonin with rearranged inter-ring electrostatic contacts and temperature-sensitive dissociation.
- Substrate polypeptide presents a load on the apical domains of the chaperonin GroEL.
- Folding with and without encapsulation by cis- and trans-only GroEL-GroES complexes.
- Role of the gamma-phosphate of ATP in triggering protein folding by GroEL-GroES: function, structure and energetics.
- A small molecule inhibitor selective for a variant ATP-binding site of the chaperonin GroEL.
Schools
University Of Tennessee Health Science Center College Of Medicine
Chatt Unit UtcomEr
University Of Alabama Birmingham
Doctors Specialties
- Anesthesiology
Accepted Insurances
Education
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University of Alabama Medical Center -
University of Tennessee College of Medicine
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