Roy A. Quinlan mainly investigates Intermediate filament, Cell biology, Molecular biology, Biochemistry and Cytoskeleton. Roy A. Quinlan combines subjects such as Chaperone and Circular dichroism with his study of Intermediate filament. His Cell biology study combines topics from a wide range of disciplines, such as Heat shock protein, Cellular differentiation, Protein filament and Lens protein.
Roy A. Quinlan has researched Molecular biology in several fields, including Lamin, Lens Fiber, Peptide sequence, Cell nucleus and Human skin. His work in the fields of Biochemistry, such as Hsp27, Protein aggregation, ASK1 and MAP kinase kinase kinase, intersects with other areas such as Cytosol. The study incorporates disciplines such as Gel electrophoresis and Lens in addition to Cytoskeleton.
His primary areas of investigation include Cell biology, Intermediate filament, Molecular biology, Lens and Cytoskeleton. His study looks at the intersection of Cell biology and topics like Nuclear lamina with Chromatin. As a member of one scientific family, Roy A. Quinlan mostly works in the field of Intermediate filament, focusing on Chaperone and, on occasion, Protein aggregation.
His work carried out in the field of Molecular biology brings together such families of science as Lamin, Plasma protein binding, Mutant, Transfection and Desmin. His Lens research includes elements of Cataracts, BFSP2, Crystallin and Anatomy. His research integrates issues of Mutation and Actin in his study of Cytoskeleton.
His scientific interests lie mostly in Cell biology, Lens, Intermediate filament, Eye lens and Cataracts. The concepts of his Cell biology study are interwoven with issues in Heat shock protein, Molecular biology, Desmin and Cytoskeleton. His biological study spans a wide range of topics, including Mechanotransduction, Nuclear lamina and Myristoylation.
His Lens research includes themes of Crystallin, Anatomy and Regeneration. In general Intermediate filament, his work in BFSP2 is often linked to SILK linking many areas of study. His BFSP2 course of study focuses on Protein filament and Gene.
His primary areas of study are Cell biology, Cataracts, Eye lens, Lens and Crystallin. His studies deal with areas such as Mutation, Intermediate filament, Molecular biology, Protein structure and Hsp27 as well as Cell biology. Intermediate filament is a subfield of Cytoskeleton that Roy A. Quinlan tackles.
His Cataracts study combines topics in areas such as Optometry, Cataractous lens and Drug treatment. His Lens Fiber study, which is part of a larger body of work in Lens, is frequently linked to Perlecan, bridging the gap between disciplines. The various areas that Roy A. Quinlan examines in his Crystallin study include Crystallography and Chaperone.
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Patterns of Expression and Organization of Cytokeratin Intermediate Filaments
Roy A. Quinlan;Dorothea L. Schiller;Mechthild Hatzfeld;Thomas Achtstätter.
Annals of the New York Academy of Sciences (1985)
Chaperone activity of alpha-crystallins modulates intermediate filament assembly.
I D Nicholl;R A Quinlan.
The EMBO Journal (1994)
Intermediate filament interactions can be altered by HSP27 and alphaB-crystallin
M D Perng;Lindsay Susan Cairns;P van den IJssel;A Prescott.
Journal of Cell Science (1999)
Alpha-b crystallin gene (CRYAB) mutation causes dominant congenital posterior polar cataract in humans
Vanita Berry;Peter Francis;M. Ashwin Reddy;Dean Collyer.
American Journal of Human Genetics (2001)
Lamin A/C Binding Protein LAP2α Is Required for Nuclear Anchorage of Retinoblastoma Protein
Ewa Markiewicz;Thomas Dechat;Roland Foisner;Roy. A Quinlan.
Molecular Biology of the Cell (2002)
 Separation of cytokeratin polypeptides by gel electrophoretic and chromatographic techniques and their identification by immunoblotting
Thomas Achtstaetter;Mechthild Hatzfeld;Roy A. Quinlan;David C. Parmelee.
Methods in Enzymology (1986)
Identification of a distinct soluble subunit of an intermediate filament protein: tetrameric vimentin from living cells.
Peter Soellner;Roy A. Quinlan;Werner W. Franke.
Proceedings of the National Academy of Sciences of the United States of America (1985)
Glial fibrillary acidic protein mutations in infantile, juvenile, and adult forms of Alexander disease.
Rong Li;Anne B. Johnson;Gajja Salomons;James E. Goldman.
Annals of Neurology (2005)
Aniridia-associated translocations, DNase hypersensitivity, sequence comparison and transgenic analysis redefine the functional domain of PAX6
Dirk A. Kleinjan;Anne Seawright;Andreas Schedl;Roy A Quinlan.
Human Molecular Genetics (2001)
Heterotypic tetramer (A2D2) complexes of non-epidermal keratins isolated from cytoskeletons of rat hepatocytes and hepatoma cells.
Roy A. Quinlan;Jeffrey A. Cohlberg;Dorothea L. Schiller;Mechthtld Hatzfeld.
Journal of Molecular Biology (1984)
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