Zobrazeno 1 - 10 of 17 pro vyhledávání: '"Aaron J. Morris"'
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Akademický článek
Investigational Assay for Haplotype Phasing of the Huntingtin Gene
Autor: Nenad Svrzikapa, Kenneth A. Longo, Nripesh Prasad, Ramakrishna Boyanapalli, Jeffrey M. Brown, Daniel Dorset, Scott Yourstone, Jason Powers, Shawn E. Levy, Aaron J. Morris, Chandra Vargeese, Jaya Goyal
Publikováno v: Molecular Therapy: Methods & Clinical Development, Vol 19, Iss , Pp 162-173 (2020)
Novel treatments for Huntington’s disease (HD), a progressive neurodegenerative disorder, include selective targeting of the mutant allele of the huntingtin gene (mHTT) carrying the abnormally expanded disease-causing cytosine-adenine-guanine (CAG)
Externí odkaz: https://doaj.org/article/65d1f0e1bbb64c3b9d640e8783a84fb1
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2
Investigational Assay for Haplotype Phasing of the Huntingtin Gene
Autor: Daniel Dorset, Ramakrishna Boyanapalli, Kenneth Longo, Jeffrey M. Brown, Aaron J. Morris, Nripesh Prasad, Scott Yourstone, Shawn Levy, Chandra Vargeese, Nenad Svrzikapa, Jaya Goyal, Jason Powers
Publikováno v: Molecular Therapy. Methods & Clinical Development
Molecular Therapy: Methods & Clinical Development, Vol 19, Iss, Pp 162-173 (2020)
Novel treatments for Huntington’s disease (HD), a progressive neurodegenerative disorder, include selective targeting of the mutant allele of the huntingtin gene (mHTT) carrying the abnormally expanded disease-causing cytosine-adenine-guanine (CAG)
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b6a876e8e2835d79e2bba28b9a1adca6
http://europepmc.org/articles/PMC7648085
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5
Structure of a Fructose-1,6-bis(phosphate) Aldolase Liganded to Its Natural Substrate in a Cleavage-Defective Mutant at 2.3 Å
Autor: Aaron J. Morris, Didier Utheza, Karen N. Allen, Dean R. Tolan, Kyung H. Choi, Andrew S. Mazurkie
Publikováno v: Biochemistry. 38:12655-12664
Class I fructose-1,6-bis(phosphate) aldolase is a glycolytic enzyme that catalyzes the cleavage of fructose 1,6-bis(phosphate) through a covalent Schiff base intermediate. Although the atomic structure of this enzyme is known, assigning catalytic rol
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::97cfad972be47f9b30305dbce8f6fb40
https://doi.org/10.1021/bi9828371
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6
Association of the Insulin Receptor with Phospholipase C-γ (PLCγ) in 3T3-L1 Adipocytes Suggests a Role for PLCγ in Metabolic Signaling by Insulin
Autor: Ayse G. Kayali, Jens Eichhorn, Tetsuro Haruta, Nicholas J. G. Webster, Jerrold M. Olefsky, Aaron J. Morris, James G. Nelson, Peter Vollenweider
Publikováno v: Journal of Biological Chemistry. 273:13808-13818
Phospholipase C-gamma (PLCgamma) is the isozyme of PLC phosphorylated by multiple tyrosine kinases including epidermal growth factor, platelet-derived growth factor, nerve growth factor receptors, and nonreceptor tyrosine kinases. In this paper, we p
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::81c63241373cddff0baa68ea7a1c1f40
https://doi.org/10.1074/jbc.273.22.13808
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7
Ligand-Independent GLUT4 Translocation Induced by Guanosine 5′-O-(3-Thiotriphosphate) Involves Tyrosine Phosphorylation*
Autor: David W. Rose, M. Mueckler, Tetsuro Haruta, Aaron J. Morris, James G. Nelson, Jerrold M. Olefsky, Peter Vollenweider
Publikováno v: Endocrinology. 139:358-364
To delineate the signaling pathway leading to glucose transport protein (GLUT4) translocation, we examined the effect of microinjection of the nonhydrolyzable GTP analog, guanosine 5′-O-(3-thiotriphosphate) (GTPγS), into 3T3-L1 adipocytes. Thirty
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3049f1a6e6fdcc3a62e73f73a92bbde8
https://doi.org/10.1210/endo.139.1.5698
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8
The Molecular Nature of the F-actin Binding Activity of Aldolase Revealed with Site-directed Mutants
Autor: Jian Wang, Len Pagliaro, Dean R. Tolan, Aaron J. Morris
Publikováno v: Journal of Biological Chemistry. 271:6861-6865
We used site-directed mutagenesis of rabbit muscle aldolase, falling ball viscometry, co-sedimentation binding assays, and negative stain electron microscopy, to identify specific residues involved in the aldolase-actin interaction. Three mutants, R4
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::a9f16ad64c6adf202d600385ec805690
https://doi.org/10.1074/jbc.271.12.6861
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9
A lysine to arginine substitution at position 146 of rabbit aldolase A changes the rate-determining step to Schiff base formation
Autor: Dean R. Tolan, Aaron J. Morris, Robert C. Davenport
Publikováno v: "Protein Engineering, Design and Selection". 9:61-67
Lys146 of rabbit aldolase A [D-fructose-1,6-bis(phosphate): D-glyceraldehyde-3-phosphate lyase, EC 4.1.2.13] was changed to arginine by site-directed mutagenesis. The kcat of the resulting mutant protein, K146R, was 500 times slower than wild-type in
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::215d2dc00464616dda1e0210a1e91923
https://doi.org/10.1093/protein/9.1.61
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10
Site-directed mutagenesis identifies aspartate 33 as a previously unidentified critical residue in the catalytic mechanism of rabbit aldolase A
Autor: Aaron J. Morris, Dean R. Tolan
Publikováno v: Journal of Biological Chemistry. 268:1095-1100
The expression and purification of the rabbit muscle aldolase A (D-fructose 1,6-bisphosphate:D-glyceraldehyde-3-phosphate lyase, EC 4.1.2.13) from an expression plasmid in bacteria is described. The enzyme is produced in bacteria at a level of 300 mg
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::13d1ee8587fa7a1cf26168aad0373345
https://doi.org/10.1016/s0021-9258(18)54046-1
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