Robert W. Mahley

ORCID: 0000-0003-3543-9278
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About
Contact & Profiles
Research Areas
  • Diabetes, Cardiovascular Risks, and Lipoproteins
  • Lipoproteins and Cardiovascular Health
  • Cancer, Lipids, and Metabolism
  • Alzheimer's disease research and treatments
  • Cholesterol and Lipid Metabolism
  • Peroxisome Proliferator-Activated Receptors
  • Lipid metabolism and disorders
  • Lipid metabolism and biosynthesis
  • Nuclear Receptors and Signaling
  • Glycosylation and Glycoproteins Research
  • Protease and Inhibitor Mechanisms
  • Ubiquitin and proteasome pathways
  • Adipokines, Inflammation, and Metabolic Diseases
  • Mitochondrial Function and Pathology
  • Liver Disease Diagnosis and Treatment
  • Retinoids in leukemia and cellular processes
  • Atherosclerosis and Cardiovascular Diseases
  • Computational Drug Discovery Methods
  • RNA and protein synthesis mechanisms
  • Advanced Proteomics Techniques and Applications
  • Cellular transport and secretion
  • Antioxidant Activity and Oxidative Stress
  • Fatty Acid Research and Health
  • Genetic Associations and Epidemiology
  • S100 Proteins and Annexins

Gladstone Institutes
2010-2024

University of California, San Francisco
2009-2024

Marymount University
2016

National Institutes of Health
1974-2010

Amerikan Hastanesi
1993-2010

The University of Texas Southwestern Medical Center
1993-2010

University of Ottawa
2010

Medical Research Council
2010

GlaxoSmithKline (United Kingdom)
2010

University of Cambridge
2010

Iosif Lazaridis Nick Patterson Alissa Mittnik Gabriel Renaud Swapan Mallick and 95 more Karola Kirsanow Peter H. Sudmant Joshua G. Schraiber Sergi Castellano Mark Lipson Bonnie Berger Christos Economou Ruth Bollongino Qiaomei Fu Kirsten I. Bos Susanne Nordenfelt Heng Li Cesare de Filippo Kay Prüfer Susanna Sawyer Cosimo Posth Wolfgang Haak Fredrik Hallgren Elin Fornander Nadin Rohland Dominique Delsate Michael Francken Jean-Michel Guinet Joachim Wahl George Ayodo Hamza A. Babiker Graciela Bailliet Elena Balanovska Oleg Balanovsky Ramiro Barrantes Gabriel Bedoya Haim Ben‐Ami Judit Bene Fouad Berrada Cláudio M. Bravi Francesca Brisighelli George B. J. Busby Francesco Calı̀ Mikhail Churnosov David E.C. Cole Daniel Corach Larissa Damba George van Driem Stanislav Dryomov Jean-Michel Dugoujon С.А. Федорова Irene Gallego Romero Marina Gubina Michael F. Hammer Brenna M. Henn Tor Hervig Uğur Hodoglugil Aashish R. Jha Sena Karachanak-Yankova Р. И. Хусаинова Э. К. Хуснутдинова Rick A. Kittles Toomas Kivisild William Klitz Vaidutis Kučinskas Alena Kushniarevich Leila Laredj Sergey Litvinov Theologos Loukidis Robert W. Mahley Béla Melegh Ene Metspalu Julio Molina Joanna L. Mountain Klemetti Näkkäläjärvi Desislava Nesheva Thomas Nyambo L. P. Osipova Jüri Parik Федор Алексеевич Платонов Olga L. Posukh Valentino Romano Francisco Rothhammer Igor Rudan Ruslan Ruizbakiev Hovhannes Sahakyan Antti Sajantila Antonio Salas Elena B. Starikovskaya Ayele Tarekegn Драга Тончева Shahlo Turdikulova Ingrida Uktverytė Olga Utevska René Vásquez Mercedes Villena М. И. Воевода Cheryl A. Winkler Levon Yepiskoposyan Pierre Zalloua

10.1038/nature13673 article EN Nature 2014-09-01

Abaract Plasma lipoprotein metabolism is regulated and controlled by the specific apolipoprotein (apo-) constituents of various classes.The major apolipoproteins include apoE, apoB, apoA-I, apoA-11, apoA-IV, apoC-I, apoC-11, apoC-Ill.Specific function in regulation through their involvement transport redistribution lipids among cells tissues, role as cofactors for enzymes lipid metabolism, or maintenance structure particles.The primary structures most are now known, functional domains these...

10.1016/s0022-2275(20)34443-6 article EN cc-by Journal of Lipid Research 1984-12-01

Apolipoprotein E4 (apoE4), one of the three common isoforms apoE, has been implicated in Alzheimer's disease. The effects apoE on neuronal growth were determined cultures dorsal root ganglion neurons. In presence β-migrating very low density lipoproteins (β-VLDL), apoE3 increased neurite outgrowth, whereas apoE4 decreased outgrowth. or β-VLDL prevented by incubation with a monoclonal antibody to reductive methylation both which block ability interact lipoprotein receptors. data suggest that...

10.1126/science.8171342 article EN Science 1994-05-06

The plasma protein apolipoprotein (apo) E is an important determinant of lipid transport and metabolism in mammals. In the present study, immunocytochemistry has been used to identify apo specific cells central peripheral nervous systems rat. Light microscopic examination revealed that all astrocytes, including specialized astrocytic (Bergmann glia cerebellum, tanycytes third ventricle, pituicytes neurohypophysis, Müller retina), possessed significant concentrations E. major subdivisions...

10.1172/jci112130 article EN Journal of Clinical Investigation 1985-10-01

The abbreviations used are: apo-E, E apoprotein; VLDL, very low density lipoproteins; isoforms, E-1, E-2, E-3, and E-4, using the onedimensional gel nomenclature established by Utermann et al. (17).Equivalency of Zannis Breslow (20) with system: p-11 pattern, E-4/E-4 genotype; p-111 E-3/E-3 D-IV E-2/E-2 a-I1 E-4/E-3 a-111 E-3/E-2 a-IV E-4/E-2 genotype.and several different animals (5-10).Metabolically, this Mr ' Expressed as residues per mole, assuming Ala = 1.0 (2 determinations).Converted...

10.1016/s0021-9258(19)52510-8 article EN cc-by Journal of Biological Chemistry 1981-09-01

The amino acid sequence of human apolipoprotein E (apo-E) has been determined.Apo-E2, one the major isoforms E, is a polypeptide 299 acids having calculated molecular weight 34,145.The isoform apo-E3 differs from apo-E2 by single substitution arginine for cysteine at residue 158 (italicized).The sequqnce...

10.1016/s0021-9258(18)34702-1 article EN cc-by Journal of Biological Chemistry 1982-04-01

In summary, the model of chylomicron remnant clearance via LDL receptors, HSPG-LRP pathway, and HSPG alone appears to be valid (Fig. 1). Apolipoprotein E serves as major ligand facilitating lipoprotein catabolism. The in space Disse may well serve a reservoir allow apoE accumulate thereby participate sequestration capture lipoproteins. addition, receptor, either or part complex, responsible for endocytosis by hepatocytes. Along with receptor function an alternate pathway. Hepatic lipase...

10.1016/s0022-2275(20)33334-4 article EN cc-by Journal of Lipid Research 1999-01-01

Human apolipoprotein E, a blood plasma protein, mediates the transport and uptake of cholesterol lipid by way its high affinity interaction with different cellular receptors, including low-density lipoprotein (LDL) receptor. The three-dimensional structure LDL receptor-binding domain apoE has been determined at 2.5 angstrom resolution x-ray crystallography. protein forms an unusually elongated (65 angstroms) four-helix bundle, helices apparently stabilized tightly packed hydrophobic core...

10.1126/science.2063194 article EN Science 1991-06-28

The low density lipoprotein (LDL) cell surface receptors on human fibroblasts grown in culture bind specific plasma lipoproteins, initiating a series of events which regulate intracellular cholesterol metabolism. Specificity for the interaction with resides protein moieties specifically B and E apoproteins LDL certain high lipoproteins (HDLc HDLl), respectively. It was previously established that amino acid arginine is functionally significant residue or near recognition sites modification...

10.1016/s0021-9258(17)34284-9 article EN cc-by Journal of Biological Chemistry 1978-12-01

A 37-kDa glycoprotein has been described recently, whose synthesis is dramatically increased after injury of the rat sciatic and optic nerves. Cells in nerve sheath, distal to site injury, produce secrete large amounts this protein, so that by 3 weeks it represents 2-5% total soluble extracellular protein regenerating although fails accumulate damaged nerve. Results presented here reveal extensive homology between injury-induced a well-studied serum apolipoprotein E (apoE), involved lipid...

10.1073/pnas.83.4.1125 article EN Proceedings of the National Academy of Sciences 1986-02-01

Recent work has demonstrated that apo E secretion and accumulation increase in the regenerating peripheral nerve. The fact apoE, conjunction with apoA-I LDL receptors, participates a well-established lipid transfer system raised possibility apoE is also involved transport injured In present study of crushed rat sciatic nerve, combination techniques was used to trace cellular associations apoA-I, receptor during nerve repair determine distribution at each stage. After crush injury, as axons...

10.1172/jci113943 article EN Journal of Clinical Investigation 1989-03-01

Apolipoprotein (apo) E has roles beyond lipoprotein metabolism. The detrimental effects of apoE4 in cardiovascular, neurological, and infectious diseases correlate with its structural features (e.g., domain interaction) that distinguish it from apoE3 apoE2. Structure/function studies revealed apoE2 is severely defective LDL receptor binding because a difference alters the region helped unravel mechanism type III hyperlipoproteinemia. ApoE4 major genetic risk factor for Alzheimer's disease...

10.1194/jlr.r800069-jlr200 article EN cc-by Journal of Lipid Research 2008-12-23

The relative amount of apolipoprotein (apo-) E mRNA in 12 different tissues the rat and marmoset was examined by dot blot hybridization using cloned cDNA probes. As expected, it found to be most abundant liver. However, substantial amounts apo-E were brain adrenals at levels about one-third that Significant quantities detected all other peripheral as well. these 2-10% liver 10-30% marmoset. Apo-E also human each species examined; distributed throughout major areas this organ. In contrast,...

10.1073/pnas.82.1.203 article EN Proceedings of the National Academy of Sciences 1985-01-01

Previous in vivo turnover studies suggested that retarded clearance of low density lipoproteins (LDL) from the plasma some hypercholesterolemic patients is due to LDL with defective receptor binding. The present study examined this postulate directly by binding experiments. a patient (G.R.) displayed reduced ability bind receptors on normal human fibroblasts. G.R. possessed 32% activity (approximately equal 9.3 micrograms per ml were required displace 50% 125I-labeled LDL, vs. approximately...

10.1073/pnas.84.19.6919 article EN Proceedings of the National Academy of Sciences 1987-10-01
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