Physician

Ophthalmology

John A. Carver, MD practices Ophthalmology. He went to University of California San Francisco School of Medicine. University of California San Francisco School of Medicine is one of the top medical schools in the US. University of California San Francisco School of Medicine is ranked 3/3 in Research/PrimaryCare. He over the years received 2 awards: "CMS Meaningful Use Stage 1 Certification" and "Fellow (FAAO)". John A. Carver, MD is also a published physician. He has 101 publication published. The most recent publication is: The mammalian small heat-shock protein Hsp20 forms dimers and is a poor chaperone. He is registered with Medicare and accepts Medicare payments.

Publications

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• Binding of the Molecular Chaperone ?B-Crystallin to A? Amyloid Fibrils Inhibits Fibril Elongation.
• Dynamism in Molecular Chaperones.
• The chaperone action of bovine milk α(S1)- and α(S2)-caseins and their associated form α(S)-casein.
• NMR spectroscopy of 14-3-3ζ reveals a flexible C-terminal extension: differentiation of the chaperone and phosphoserine-binding activities of 14-3-3ζ.
• Enhanced molecular chaperone activity of the small heat-shock protein αB-crystallin following covalent immobilization onto a solid-phase support.
• The quaternary organization and dynamics of the molecular chaperone HSP26 are thermally regulated.
• Age-related Macular degeneration and hyperbaric oxygen.
• Small heat-shock proteins interact with a flanking domain to suppress polyglutamine aggregation.
• The interaction of alphaB-crystallin with mature alpha-synuclein amyloid fibrils inhibits their elongation.
• The interaction of unfolding α-lactalbumin and malate dehydrogenase with the molecular chaperone αB-crystallin: a light and X-ray scatterin...
• Model for amorphous aggregation processes.
• Dephosphorylation of alpha(s)- and beta-caseins and its effect on chaperone activity: a structural and functional investigation.
• Analysis of Glaucoma-related mortality in the United States using death certificate data.
• Dissociation from the oligomeric state is the rate-limiting step in fibril formation by kappa-casein.
• Amyloid fibril formation by bovine milk alpha s2-casein occurs under physiological conditions yet is prevented by its natural counterpart, alpha s1-casein.
• Site-directed mutations in the C-terminal extension of human alphaB-crystallin affect chaperone function and block amyloid fibril formation.
• Amyloid fibril formation by bovine milk kappa-casein and its inhibition by the molecular chaperones alphaS- and beta-casein.
• Casein proteins as molecular chaperones.
• Host-defence peptides of Australian anurans: structure, mechanism of action and evolutionary significance.
• Investigating the importance of the flexible hinge in caerin 1.1: solution structures and activity of two synthetically modified caerin peptides.
• Amyloid fibril formation by Lens crystallin proteins and its implications for cataract formation.
• The selective inhibition of serpin aggregation by the molecular chaperone, alpha-crystallin, indicates a nucleation-dependent specificity.
• The solution structure of frenatin 3, a neuronal nitric oxide synthase inhibitor from the Giant tree frog, Litoria infrafrenata.
• The solution structures and activity of caerin 1.1 and caerin 1.4 in aqueous trifluoroethanol and dodecylphosphocholine miCelles.
• Mildly acidic pH activates the extraCellular molecular chaperone clusterin.
• Decreased heat stability and increased chaperone requirement of modified human betaB1-crystallins.
• Structural investigation of the hedamycin:d(ACCGGT)2 complex by NMR and restrained molecular dynamics.
• Evidence that clusterin has discrete chaperone and ligand binding sites.
• αB-Crystallin inhibits the Cell toxicity associated with amyloid fibril formation by κ-casein and the amyloid-β peptide.
• A quantitative NMR spectroscopic examination of the flexibility of the C-terminal extensions of the molecular chaperones, αA- and αB-crystallin.
• The dissociated form of kappa-casein is the precursor to its amyloid fibril formation.
• Crystallin proteins and amyloid fibrils.
• Glutamic acid residues in the C-terminal extension of small heat shock protein 25 are critical for structural and functional integrity.
• (-)-epigallocatechin-3-gallate (EGCG) maintains kappa-casein in its pre-fibrillar state without redirecting its aggregation pathway.
• The thioflavin T fluorescence assay for amyloid fibril detection can be biased by the presence of exogenous compounds.
• Carboxymethylated-kappa-casein: a convenient tool for the identification of polyphenolic inhibitors of amyloid fibril formation.
• Unraveling the mysteries of protein folding and misfolding.
• Monitoring the prevention of amyloid fibril formation by alpha-crystallin. Temperature dependence and the nature of the aggregating species.
• The effect of small molecules in modulating the chaperone activity of alphaB-crystallin against ordered and disordered protein aggregation.
• Mimicking phosphorylation of alphaB-crystallin affects its chaperone activity.
• The effect of dextran on subunit exchange of the molecular chaperone alphaA-crystallin.
• Characterisation of amyloid fibril formation by small heat-shock chaperone proteins human alphaA-, alphaB- and R120G alphaB-crystallins.
• Interaction of the molecular chaperone alphaB-crystallin with alpha-synuclein: effects on amyloid fibril formation and chaperone activity.
• R120G alphaB-crystallin promotes the unfolding of reduced alpha-lactalbumin and is inherently unstable.
• nNOS inhibition, antimicrobial and anticancer activity of the amphibian skin peptide, citropin 1.1 and synthetic modifications. The solution structure of a modified ci...
• Small heat-shock proteins and clusterin: intra- and extraCellular molecular chaperones with a common mechanism of action and function?
• Clusterin is an extraCellular chaperone that specifically interacts with slowly aggregating proteins on their off-folding pathway.
• The eye Lens protein alphaA-crystallin of the blind mole rat Spalax ehrenbergi: effects of altered functional constraints.
• The interaction of the molecular chaperone alpha-crystallin with unfolding alpha-lactalbumin: a structural and kinetic spectroscopic study.
• Mouse Hsp25, a small shock protein. The role of its C-terminal extension in oligomerization and chaperone action.
• The molecular chaperone alpha-crystallin is in kinetic competition with aggregation to stabilize a monomeric molten-globule form of alpha-lactalbumin.
• Structural alterations of alpha-crystallin during its chaperone action.
• Formation of betaA3/betaB2-crystallin mixed complexes: involvement of N- and C-terminal extensions.
• The mammalian small heat-shock protein Hsp20 forms dimers and is a poor chaperone.
• Clusterin has chaperone-like activity similar to that of small heat shock proteins.
• Host defence peptides from the skin glands of the Australian blue mountains tree-frog Litoria citropa. Solution structure of the antibacterial peptide citropin 1.1.
• The antibiotic and anticancer active aurein peptides from the Australian Bell Frogs Litoria aurea and Litoria raniformis the solution structure of aurein 1.2.
• The small heat-shock chaperone protein, alpha-crystallin, does not recognize stable molten globule states of cytosolic proteins.
• Clusterin is an ATP-independent chaperone with very broad substrate specificity that stabilizes stressed proteins in a folding-competent state.
• Immobilization of the C-terminal extension of bovine alphaA-crystallin reduces chaperone-like activity.
• The interaction of the molecular chaperone, alpha-crystallin, with molten globule states of bovine alpha-lactalbumin.
• Investigation of gammaE-crystallin target protein binding to bovine Lens alpha-crystallin by small-angle neutron scattering.
• Identification by 1H NMR spectroscopy of flexible C-terminal extensions in bovine Lens alpha-crystallin.
• The molecular chaperone, alpha-crystallin, inhibits amyloid formation by apolipoprotein C-II.
• Secondary structure determination of 15N-labelled human Long-[Arg-3]-insulin-like growth factor 1 by multidimensional NMR spectroscopy.
• Solution structure and backbone dynamics of long-[Arg(3)]insulin-like growth factor-I.
• Non-oxidative modification of Lens crystallins by kynurenine: a novel post-translational protein modification with possible relevance to ageing and cataract.
• Maculatin 1.1, an anti-microbial peptide from the Australian tree frog, Litoria genimaculata solution structure and biological activity.
• Supramolecular order within the Lens: 1H NMR spectroscopic evidence for specific crystallin-crystallin interactions.
• Age-related changes in bovine alpha-crystallin and High-molecular-weight protein.
• Alpha-crystallin: molecular chaperone and protein surfactant.
• Oxidation products of 3-hydroxykynurenine bind to Lens proteins: relevance for nuclear cataract.
• A 1H NMR spectroscopic comparison of gamma S- and gamma B-crystallins.
• An investigation into the stability of alpha-crystallin by NMR spectroscopy; evidence for a two-domain structure.
• NMR spectroscopy of alpha-crystallin. Insights into the structure, interactions and chaperone action of small heat-shock proteins.
• The solution structure and activity of caerin 1.1, an antimicrobial peptide from the Australian green tree frog, Litoria splendida.
• Structure/function studies of dogfish alpha-crystallin, comparison with bovine alpha-crystallin.
• 1H NMR spectroscopy reveals that mouse Hsp25 has a flexible C-terminal extension of 18 amino acids.
• 1H-NMR spectroscopy of beta B2-crystallin from bovine eye Lens. Conformation of the N- and C-terminal extensions.
• Identification of glutathionyl-3-hydroxykynurenine glucoside as a novel fluorophore associated with aging of the human Lens.
• The solution structure of uperin 3.6, an antibiotic peptide from the granular dorsal glands of the Australian toadlet, Uperoleia mjobergii.
• Polypeptide modification and cross-linking by oxidized 3-hydroxykynurenine.
• The elusive role of the N-terminal extension of beta A3- and beta A1-crystallin.
• A possible chaperone-like quaternary structure for alpha-crystallin.
• 1H-NMR spectroscopy of bovine Lens beta-crystallin. The role of the beta B2-crystallin C-terminal extension in aggregation.
• Elucidation of a novel polypeptide cross-link involving 3-hydroxykynurenine.
• On the interaction of alpha-crystallin with unfolded proteins.
• Loss of the C-terminal serine residue from bovine beta B2-crystallin.
• A two dimensional 1H NMR study of the solution conformation of gastrin releasing peptide.
• The conformation of bombesin in solution as determined by two-dimensional 1H-NMR techniques.
• A spectroscopic study of glycated bovine alpha-crystallin: investigation of flexibility of the C-terminal extension, chaperone activity and evidence for diglycation.
• Solution conformation of bovine Lens alpha- and betaB2-crystallin terminal extensions.
• Probing the structure and interactions of crystallin proteins by NMR spectroscopy.
• Inactivation of chicken liver pyruvate carboxylase by 1,10-phenanthroline.
• NMR identification of a partial helical conformation for bombesin in solution.
• Structural comparison between retro-inverso and parent peptides: molecular basis for the biological activity of a retro-inverso analogue of the immunodominant fragment...
• A High resolution 1H NMR study of the solution structure of human epidermal growth factor.
• Conformational differences between various myoglobin ligated states as monitored by 1H NMR spectroscopy.
• High-resolution 1H NMR study of the solution structure of alamethicin.
• Bioprospecting keratinous materials.

Schools

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• University of California At San Francisco

• University of Washington

• Moorfields Eye Hospital

• University Of Virginia Health System

Procedures Preformed

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• Cataract Removal Surgery
• Destruction of Lesion of Retina and Choroid
• Drainage of Conjunctival Cyst
• Enucleation of Eye
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Conditions Treated

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• Aphakia and Other Disorders of Lens
• Bell's Palsy
• Blindness
• Cataract
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Doctors Specialties

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• Ophthalmology

Accepted Insurances

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Awards

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• CMS Meaningful Use Stage 1 Certification
• Fellow (FAAO)

Education

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• University of Washington
• University of California San Francisco School of Medicine

Drug Facts

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NPI NUMBER		1669435160
NPPES Provider LastName		CARVER
NPPES Provider FirstName		JOHN
NPPES Provider ZIPCode		846043374
NPPES Provider State		UT
Specialty Description		Ophthalmology
Total Claim Count		369.0
Distinct Opioid Count		1.0
Opioid Claim Count		17.0
Percent Opioid Claims		4.61

Helpful Reviews

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Medicare Facts

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National Provider Identifier [NPI]	1669435160
Last Name Of The Provider	CARVER
First Name Of The Provider	JOHN
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