Joseph Horwitz focuses on Biochemistry, Biophysics, Crystallin, Chaperone and Protein structure. The study of Biochemistry is intertwined with the study of Molecular biology in a number of ways. His Biophysics research is multidisciplinary, incorporating perspectives in Melittin, Random coil, Lens protein, Function and Alpha-crystallin.
The various areas that Joseph Horwitz examines in his Crystallin study include Immunoprecipitation, Normal lens, Lens Fiber, Alpha-Crystallin A Chain and Gap junction. His work carried out in the field of Chaperone brings together such families of science as Heat shock protein and Protein aggregation. In his study, which falls under the umbrella issue of Protein structure, Crystallography, Protein family and Förster resonance energy transfer is strongly linked to Protein subunit.
His scientific interests lie mostly in Crystallin, Biochemistry, Circular dichroism, Molecular biology and Biophysics. His Crystallin research includes elements of Lens, Alpha-Crystallin A Chain and Chaperone, Cell biology. Joseph Horwitz combines subjects such as Heat shock protein, Protein structure, Protein aggregation and Mutant with his study of Chaperone.
His work in Biochemistry tackles topics such as Lens which are related to areas like Gap junction and Fiber cell. His Circular dichroism research integrates issues from Size-exclusion chromatography, Chromophore and Absorption spectroscopy. The concepts of his Biophysics study are interwoven with issues in Membrane and Alpha-crystallin.
Joseph Horwitz mostly deals with Crystallin, Biophysics, Cell biology, Chaperone and Alpha-Crystallin A Chain. His Crystallin study is concerned with the field of Biochemistry as a whole. The Structural protein, Alpha B-Crystallin, Protein family and Alpha-crystallin research he does as part of his general Biochemistry study is frequently linked to other disciplines of science, such as Homogeneous, therefore creating a link between diverse domains of science.
His Biophysics research is multidisciplinary, relying on both Nuclear magnetic resonance spectroscopy, Fluorescence spectroscopy, Dissociation and Mass spectrometry. The Cell biology study combines topics in areas such as Danio and Zebrafish. His study in Chaperone is interdisciplinary in nature, drawing from both Crystallography, Mutant protein, Mutant and Protein aggregation.
His primary scientific interests are in Crystallography, Chaperone, Heat shock protein, Population and Circular dichroism. His research in Chaperone intersects with topics in In vitro, Nucleus, Alpha-Crystallin A Chain, Mutant and Crystallin. The study incorporates disciplines such as Antiparallel, Protein aggregation and Beta sheet in addition to Alpha-Crystallin A Chain.
His Crystallin study is concerned with the larger field of Biochemistry. His studies in Heat shock protein integrate themes in fields like Nuclear magnetic resonance spectroscopy, Mutant protein, Dissociation, Cell biology and In vivo. His work investigates the relationship between Alpha-crystallin and topics such as Protein quaternary structure that intersect with problems in Conformational change, Fluorescence spectroscopy and Biophysics.
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Alpha-crystallin can function as a molecular chaperone
Proceedings of the National Academy of Sciences of the United States of America (1992)
The major intrinsic protein (MIP) of the bovine lens fiber membrane : characterization and structure based on cDNA cloning
Michael B. Gorin;S.Barbara Yancey;Janice Cline;Jean-Paul Revel.
Disruption of α3 connexin gene leads to proteolysis and cataractogenesis in mice
Xiaohua Gong;En Li;George Klier;Qingling Huang.
Mutation R120G in αB-crystallin, which is linked to a desmin-related myopathy, results in an irregular structure and defective chaperone-like function
Michael P. Bova;Orna Yaron;Qingling Huang;Linlin Ding.
Proceedings of the National Academy of Sciences of the United States of America (1999)
Subunit exchange of alphaA-crystallin.
Michael P. Bova;Lin-Lin Ding;Joseph Horwitz;Bernard K.-K. Fung.
Journal of Biological Chemistry (1997)
The small heat-shock protein, αb-crystallin, has a variable quaternary structure
Dana A Haley;Joseph Horwitz;Phoebe L Stewart.
Journal of Molecular Biology (1998)
Crystal structures of truncated alphaA and alphaB crystallins reveal structural mechanisms of polydispersity important for eye lens function.
Arthur Laganowsky;Justin L. P. Benesch;Justin L. P. Benesch;Meytal Landau;Meytal Landau;Linlin Ding.
Protein Science (2010)
Fine structure in the near-ultraviolet circular dichroism and absorption spectra of tryptophan derivatives and chymotrypsinogen A at 77 degrees K.
Strickland Eh;Horwitz J;Billups C.
Lens alpha-crystallin: chaperone-like properties.
Joseph Horwitz;Qing-Ling Huang;Linlin Ding;Michael P. Bova.
Methods in Enzymology (1998)
Primary and secondary structure of bovine retinal S antigen (48-kDa protein)
T Shinohara;B Dietzschold;C M Craft;G Wistow.
Proceedings of the National Academy of Sciences of the United States of America (1987)
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