A. McCLUSKEY

McLean Hospital

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Document Type

Co-Authors

Lawrence K. Duffy

University of Alaska Fairbanks

Carmela R. Abraham

Boston University

Dennis J. Selkoe

Harvard University

D. J. Selkoe

Harvard University

Kenneth S. Kosik

University of California, Santa Barbara

C. G. Rasool

CNS Research (United States)

Greg G. Hillebrand

University of Cincinnati Medical Center

Katherine A. Abbott

Baylor College of Medicine

MM Dowling

The University of Texas Southwestern Medical Center

Francis X. Walsh

Marymount University

Cooperative Institutions

Harvard University

Brigham and Women's Hospital

McLean Hospital

Baylor College of Medicine

United States Department of Veterans Affairs

University of California, Santa Barbara

Massachusetts General Hospital

The University of Texas Southwestern Medical Center

Columbia University

Scripps Research Institute

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Research Field

Misincorporation during DNA synthesis, analyzed by gel electrophoresis

Nucleic Acids Research (1984)

Greg G. Hillebrand A. McCLUSKEY Katherine A. Abbott Galina G. Revich Kenneth L. Beattie

A method has been developed for simultaneous comparison of the propensity of a DNA polymerase to misincorporate at different points on a natural template–primer. In this method elongation of a [5′–12P]primer, annealed to a bacteriophage template strand, is carried out in the presence of only three dNTPs (highly purified by HPLC). Under these corditions the rate of primer elongation (monitored by gel electrophoresis/autoradiography) is limited by the rate of misincorporation at template positions complementary to the missing dNTP. Variations in the rate of elongation (revealed by antoradiographic banding patterns) reflect variations in the propensity for misincorporation at different positions along the template. The effect on primer elongation produced by addition of a chemically modified dNTP to ‘minus’ reactions reveals the mispairing potential of the modified nucleotide during DNA synthesis. By use of this electrophoretic assay of misincorporation we have demonstrated that the fidelity of E. coli DNA polymerase I varies greatly at different positions along a natural template, and that BrdUTP and IodUTP can be incorporated in place of dCTP during chain elongation catalyzed by this enzyme.

Primer (cosmetics)

Elongation

Primer extension

10.1093/nar/12.7.3155

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Citations (40)

161 MONOCLONAL ANTIBODIES TO ALZHEIMER PAIRED HELICAL FILAMENTS PRODUCED BY RAT-MOUSE HYBRIDOMAS

Journal of Neuropathology & Experimental Neurology (1984)

D. J. Selkoe Carmela R. Abraham C. G. Rasool A. McCLUSKEY Lawrence K. Duffy

10.1097/00005072-198405000-00167

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Citations (2)

Microtubule-associated protein 2: monoclonal antibodies demonstrate the selective incorporation of certain epitopes into Alzheimer neurofibrillary tangles

Alzheimer Disease & Associated Disorders (1987)

KS Kosik LK Duffy MM Dowling Carmela R. Abraham A. McCLUSKEY

Abstract Neurofibrillary tangles (NFT) are the principal structural alteration of neuronal cell bodies in Alzheimer disease as well as in normal aging of the human brain. While the ultrastructure of these intraneuronal lesions has been extensively studied, the biochemical composition of the fibers comprising the NFT is unknown. We report the production of three monoclonal antibodies against the microtubule-associated protein 2 (MAP-2), one of which intensely labels Alzheimer NFT. All three antibodies specifically recognize MAP-2 on immunoblots and stain brain tissue in a characteristic dendritic pattern. The three antibodies are directed against at least two different antigenic sites on the MAP-2 molecule, and one appears to recognize a phosphorylation site on MAP-2. That only one of the three antibodies immunolabels NFT suggests that the formation of the tangle involves some modification of the MAP-2 molecule. Our findings suggest that one aspect of Alzheimer-type neurofibrillary pathology is an aggregation of MAP-2 or MAP-2 fragments with altered neurofilamentous elements present in NFT. Normal interactive function, which putatively occurs between neurofilaments and MAP-2, may thus be disrupted in Alzheimer disease.

Neurofilament

Microtubule-associated protein

Neurofibrillary tangle

Tau protein

Amyloid (mycology)

10.1097/00002093-198701040-00018

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Citations (2)

Studies on the Analysis of Brain Structural Proteins by Chromatofocusing

Protides of the biological fluids (1985)

Lawrence K. Duffy A. McCLUSKEY Kenneth S. Kosik Dennis J. Selkoe

Chromatofocusing

10.1016/b978-0-08-033215-4.50136-9

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Citations (0)

Axonal transport of cytoskeletal proteins in aluminum toxicity

Neurochemical Pathology (1983)

Kenneth S. Kosik A. McCLUSKEY Francis X. Walsh Dennis J. Selkoe

Neurofilament

Axoplasmic transport

10.1007/bf02834283

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Citations (14)

Microtubule-associated protein 2: monoclonal antibodies demonstrate the selective incorporation of certain epitopes into Alzheimer neurofibrillary tangles.

Proceedings of the National Academy of Sciences (1984)

K S Kosik Lawrence K. Duffy Michael M. Dowling Carmela R. Abraham A. McCLUSKEY

Neurofibrillary tangles (NFT) are the principal structural alteration of neuronal cell bodies in Alzheimer disease as well as in normal aging of the human brain. While the ultrastructure of these intraneuronal lesions has been extensively studied, the biochemical composition of the fibers comprising the NFT is unknown. We report the production of three monoclonal antibodies against the microtubule-associated protein 2 (MAP-2), one of which intensely labels Alzheimer NFT. All three antibodies specifically recognize MAP-2 on immunoblots and stain brain tissue in a characteristic dendritic pattern. The three antibodies are directed against at least two different antigenic sites on the MAP-2 molecule, and one appears to recognize a phosphorylation site on MAP-2. That only one of the three antibodies immunolabels NFT suggests that the formation of the tangle involves some modification of the MAP-2 molecule. Our findings suggest that one aspect of Alzheimer-type neurofibrillary pathology is an aggregation of MAP-2 or MAP-2 fragments with altered neurofilamentous elements present in NFT. Normal interactive function, which putatively occurs between neurofilaments and MAP-2, may thus be disrupted in Alzheimer disease.

Neurofilament

Microtubule-associated protein

Neurofibrillary tangle

Tau protein

10.1073/pnas.81.24.7941

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Citations (227)

Paired Helical Filaments in Human Neurons: Relationship to Neurofilaments

Annals of the New York Academy of Sciences (1985)

Dennis J. Selkoe Carmela R. Abraham C. G. Rasool A. McCLUSKEY Kenneth S. Kosik

Neuropathology

Center (category theory)