Professor, Neurology, University Massachusetts Medical School

Neurology

Lawrence Hayward is an expert in the field of Neurology. He went to Baylor College of Medicine. Lawrence J. Hayward, MD is also published. He has 36 publications published. The lastest publication: "Missense mutation in the mtDNA cytochrome b gene in a patient with myopathy.' Doctor Lawrence J. Hayward, MD accepts Medicare payments and is registered with Medicare.gov.

Publications

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• Genome wide array analysis indicates that an amyotrophic lateral Sclerosis mutation of FUS causes an early increase of CAMK2N2 in vitro.
• Na+,K+-pump stimulation improves contractility in isolated muscles of mice with hyperkalemic periodic paralysis.
• A Yeast Model of FUS/TLS-Dependent CytoToxicity.
• A common property of amyotrophic lateral Sclerosis-associated variants: destabilization of the copper/zinc superoxide dismutase electrostatic loop.
• Metal deficiency increases aberrant hydrophobicity of mutant superoxide dismutases that cause amyotrophic lateral Sclerosis.
• Sensitive and specific identification of wild type and variant proteins from 8 to 669 kDa using top-down mass spectrometry.
• Interaction of amyotrophic lateral sclerosis (ALS)-related mutant copper-zinc superoxide dismutase with the dynein-dynactin complex contributes to inclusion formation.
• Structures of the G85R variant of SOD1 in familial amyotrophic lateral Sclerosis.
• Targeted mutation of mouse skeletal muscle sodium channel produces myotonia and potassium-sensitive weakness.
• Detergent-insoluble aggregates associated with amyotrophic lateral Sclerosis in transgenic mice contain primarily full-length, unmodified superoxide dismutase-1.
• Interaction between familial amyotrophic lateral Sclerosis (ALS)-linked SOD1 mutants and the dynein complex.
• Increased affinity for copper mediated by cysteine 111 in forms of mutant superoxide dismutase 1 linked to amyotrophic lateral Sclerosis.
• Aberrantly increased hydrophobicity shared by mutants of Cu,Zn-superoxide dismutase in familial amyotrophic lateral Sclerosis.
• Destabilization of apoprotein is insufficient to explain Cu,Zn-superoxide dismutase-linked ALS pathogenesis.
• Inhibition of chaperone activity is a shared property of several Cu,Zn-superoxide dismutase mutants that cause amyotrophic lateral Sclerosis.
• Structural consequences of the familial amyotrophic lateral Sclerosis SOD1 mutant His46Arg.
• Structural basis of heteromeric smad protein assembly in TGF-beta signaling.
• Dimer destabilization in superoxide dismutase may result in Disease-causing properties: structures of motor neuron Disease mutants.
• An alternative mechanism of bicarbonate-mediated peroxidation by copper-zinc superoxide dismutase: rates enhanced via proposed enzyme-associated peroxycarbonate interm...
• Amyloid-like filaments and water-filled nanotubes formed by SOD1 mutant proteins linked to familial ALS.
• Familial amyotrophic lateral Sclerosis mutants of copper/zinc superoxide dismutase are susceptible to disulfide reduction.
• Decreased metallation and activity in subsets of mutant superoxide dismutases associated with familial amyotrophic lateral Sclerosis.
• Familial amyotrophic lateral Sclerosis-associated mutations decrease the thermal stability of distinctly metallated species of human copper/zinc superoxide dismutase.
• Defective slow inactivation of sodium channels contributes to familial periodic paralysis.
• Missense mutation in the mtDNA cytochrome b gene in a patient with myopathy.
• A proposed mutation, Val781Ile, associated with hyperkalemic periodic paralysis and cardiac dysrhythmia is a benign polymorphism.
• Axonal transport defects in neurodegenerative Diseases.
• Slow inactivation differs among mutant Na channels associated with myotonia and periodic paralysis.
• Sodium channel inactivation is impaired in equine hyperkalemic periodic paralysis.
• Three novel mutations and two variants in the gene for Cu/Zn superoxide dismutase in familial amyotrophic lateral Sclerosis.
• Inactivation defects caused by myotonia-associated mutations in the sodium channel III-IV linker.
• The structure of holo and metal-deficient wild-type human Cu, Zn superoxide dismutase and its relevance to familial amyotrophic lateral Sclerosis.
• Mutant SOD1 instability: implications for Toxicity in amyotrophic lateral sclerosis.
• Retrograde axonal transport and motor neuron Disease.
• Mutant FUS proteins that cause amyotrophic lateral Sclerosis incorporate into stress granules.

Schools

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• Baylor University

• Baylor Affiliated Hosps Tx

• Mass General Hospital Ma

Procedures Preformed

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• EEG (Electroencephalogram)
• EMG (Electromyography)

Conditions Treated

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• Alzheimer's Disease
• Anterior Horn Disease
• Ataxia
• Autonomic Disorders
• View All

Doctors Specialties

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• Neurology

Accepted Insurances

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Education

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• Massachusetts General Hospital
• Baylor College of Medicine

Hospital

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• UMass Memorial Medical Center

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