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  • 1
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    Science over politics (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-04-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lanza, R P -- Arrow, K J -- Axelrod, J -- Baltimore, D -- Benacerraf, B -- Bloch, K E -- Bloembergen, N -- Brown, H C -- Brown, M S -- Cibelli, J B -- Cohen, S -- Cooper, L N -- Corey, E J -- Dulbecco, R -- Fischer, E H -- Fitch, V L -- Friedmen, M -- Friedman, M -- Furchgott, R F -- Gell-Mann, M -- Glaser, D A -- Glashow, S L -- Gilbert, W -- Goldstein, J L -- Wilson, R W -- New York, N.Y. -- Science. 1999 Mar 19;283(5409):1849-50.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10206888" target="_blank"〉PubMed〈/a〉
    Keywords: *Bioethics ; Biomedical Research ; *Embryo Research ; Embryo, Mammalian/*cytology ; Federal Government ; Government Regulation ; Humans ; Politics ; Research/*legislation & jurisprudence ; Research Support as Topic/legislation & jurisprudence ; *Risk Assessment ; *Stem Cells ; United States ; United States Dept. of Health and Human Services
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    Molecular medicine. The cholesterol quartet (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-05-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Goldstein, J L -- Brown, M S -- New York, N.Y. -- Science. 2001 May 18;292(5520):1310-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Genetics, University of Texas Southwestern Medical Center, Dallas, TX 75390-9046, USA. jgolds@mednet.swmed.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11360986" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Carrier Proteins/chemistry/*genetics/metabolism ; Cholesterol/blood/*metabolism ; Chromosome Mapping ; Humans ; Hypercholesterolemia/blood/*genetics/*metabolism ; Hyperlipoproteinemia Type II/blood/genetics/metabolism ; Lipoproteins, LDL/blood/metabolism ; Mutation/*genetics ; Protein Binding ; Receptors, LDL/genetics/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    Diet-induced hypercholesterolemia in mice: prevention by overexpression of LDL receptors (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-11-30
    Description: The current studies were designed to determine whether chronic overexpression of low density lipoprotein (LDL) receptors in the liver would protect mice from the increase in plasma LDL-cholesterol that is induced by high-fat diets. A line of transgenic mice was studied that express the human LDL receptor gene in the liver under control of the transferrin promoter. When fed a diet containing cholesterol, saturated fat, and bile acids for 3 weeks, the transgenic mice, in contrast to normal mice, did not develop a detectable increase in plasma LDL. The current data indicate that unregulated overexpression of LDL receptors can protect against diet-induced hypercholesterolemia in mice.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yokode, M -- Hammer, R E -- Ishibashi, S -- Brown, M S -- Goldstein, J L -- HL 20948/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1990 Nov 30;250(4985):1273-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Genetics, University of Texas, Southwestern Medical Center, Dallas 75235.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2244210" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cholesterol, Dietary/adverse effects ; Cholesterol, LDL/*blood ; Dietary Fats/*adverse effects ; Exons ; *Gene Expression ; Humans ; Hypercholesterolemia/etiology/*prevention & control ; Introns ; Lipoproteins/blood ; Lipoproteins, HDL/blood ; Lipoproteins, IDL ; Lipoproteins, VLDL/blood ; Liver/metabolism ; Mice ; Mice, Inbred C57BL ; Mice, Transgenic ; Nucleic Acid Hybridization ; Promoter Regions, Genetic/genetics ; RNA, Messenger/genetics ; Receptors, LDL/*genetics ; Transferrin/genetics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    Structure of the LDL receptor extracellular domain at endosomal pH (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-12-03
    Description: The low-density lipoprotein receptor mediates cholesterol homeostasis through endocytosis of lipoproteins. It discharges its ligand in the endosome at pH 〈 6. In the crystal structure at pH = 5.3, the ligand-binding domain (modules R2 to R7) folds back as an arc over the epidermal growth factor precursor homology domain (the modules A, B, beta propeller, and C). The modules R4 and R5, which are critical for lipoprotein binding, associate with the beta propeller via their calcium-binding loop. We propose a mechanism for lipoprotein release in the endosome whereby the beta propeller functions as an alternate substrate for the ligand-binding domain, binding in a calcium-dependent way and promoting lipoprotein release.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rudenko, Gabby -- Henry, Lisa -- Henderson, Keith -- Ichtchenko, Konstantin -- Brown, Michael S -- Goldstein, Joseph L -- Deisenhofer, Johann -- HL20948/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 2002 Dec 20;298(5602):2353-8. Epub 2002 Nov 29.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard Y4-206, Dallas, TX 75390, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12459547" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites ; Calcium/metabolism ; Crystallization ; Crystallography, X-Ray ; Endosomes/*metabolism ; Epidermal Growth Factor/chemistry ; Humans ; Hydrogen-Ion Concentration ; Hydrophobic and Hydrophilic Interactions ; Ligands ; Lipoproteins, LDL/*metabolism ; Models, Biological ; Models, Molecular ; Mutation ; Protein Binding ; Protein Conformation ; Protein Folding ; Protein Precursors/chemistry ; Protein Structure, Secondary ; *Protein Structure, Tertiary ; Receptors, LDL/*chemistry/genetics/*metabolism ; Repetitive Sequences, Amino Acid
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    Heart attacks: gone with the century? (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-05-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brown, M S -- Goldstein, J L -- New York, N.Y. -- Science. 1996 May 3;272(5262):629.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8614809" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anticholesteremic Agents/*therapeutic use ; Cholesterol/blood ; Clinical Trials as Topic ; Coronary Artery Disease/*drug therapy/etiology ; Disease Susceptibility ; Humans ; *Hydroxymethylglutaryl-CoA Reductase Inhibitors ; Hypolipidemic Agents/*therapeutic use ; Lipoproteins, LDL/blood ; Myocardial Infarction/etiology/*prevention & control
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
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    Retinal degeneration in choroideremia: deficiency of rab geranylgeranyl transferase (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-01-15
    Description: Rab geranylgeranyl transferase (GG transferase) is a two-component enzyme that attaches 20-carbon isoprenoid groups to cysteine residues in Rab proteins, a family of guanosine triphosphate-binding proteins that regulate vesicular traffic. The mutant gene in human choroideremia, an X-linked form of retinal degeneration, encodes a protein that resembles component A of rat Rab GG transferase. Lymphoblasts from choroideremia subjects showed a marked deficiency in the activity of component A, but not component B, of Rab GG transferase. The deficiency was more pronounced when the substrate was Rab3A, a synaptic vesicle protein, than it was when the substrate was Rab1A, a protein of the endoplasmic reticulum. The data imply the existence of multiple component A proteins, one of which is missing in choroideremia.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Seabra, M C -- Brown, M S -- Goldstein, J L -- HL 20948/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1993 Jan 15;259(5093):377-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Genetics, University of Texas Southwestern Medical Center, Dallas 75235.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8380507" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; *Alkyl and Aryl Transferases ; Cell Line, Transformed ; Cells, Cultured ; Choroid/chemistry ; Choroideremia/*genetics ; Female ; GTP-Binding Proteins/analysis/*metabolism ; Gene Expression Regulation, Enzymologic ; Humans ; Lymphocyte Activation ; Male ; Middle Aged ; Mutation ; Nerve Tissue Proteins/analysis/*metabolism ; Photoreceptor Cells/chemistry ; Pigment Epithelium of Eye/chemistry ; Protein Prenylation ; Retina/chemistry ; Substrate Specificity ; Transferases/*deficiency/genetics ; rab1 GTP-Binding Proteins ; rab3 GTP-Binding Proteins
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
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    Biomedicine. Lowering LDL--not only how low, but how long? (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-03-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brown, Michael S -- Goldstein, Joseph L -- New York, N.Y. -- Science. 2006 Mar 24;311(5768):1721-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Genetics, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390-9046, USA. mike.brown@utsouthwestern.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16556829" target="_blank"〉PubMed〈/a〉
    Keywords: African Americans/genetics ; Animals ; Anticholesteremic Agents/*therapeutic use ; Cholesterol, LDL/*blood ; Codon, Nonsense ; Coronary Disease/epidemiology/genetics/*prevention & control ; Diet, Fat-Restricted ; European Continental Ancestry Group/genetics ; Humans ; Hydroxymethylglutaryl-CoA Reductase Inhibitors/therapeutic use ; Incidence ; Lipoproteins, LDL/*blood ; Mice ; Mutation, Missense ; Proprotein Convertases ; Serine Endopeptidases/*genetics/*metabolism ; Time Factors
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
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    Medicine. HDL miR-ed down by SREBP introns (2010)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2010-06-19
    Description: 〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2936826/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2936826/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brown, Michael S -- Ye, Jin -- Goldstein, Joseph L -- HL20948/HL/NHLBI NIH HHS/ -- P01 HL020948/HL/NHLBI NIH HHS/ -- P01 HL020948-34/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 2010 Jun 18;328(5985):1495-6. doi: 10.1126/science.1192409.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Genetics, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA. mike.brown@utsouthwestern.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20558698" target="_blank"〉PubMed〈/a〉
    Keywords: ATP Binding Cassette Transporter 1 ; ATP-Binding Cassette Transporters/genetics ; Animals ; Cholesterol/biosynthesis/*metabolism ; Gene Expression Regulation ; Humans ; Hyperinsulinism/genetics/metabolism ; *Introns ; Lipoproteins, HDL/*blood ; Liver/metabolism ; Metabolic Syndrome X/genetics/metabolism ; MicroRNAs/antagonists & inhibitors/*genetics/*metabolism ; RNA, Messenger/genetics/metabolism ; Sterol Regulatory Element Binding Protein 1/*genetics/metabolism ; Sterol Regulatory Element Binding Protein 2/*genetics/metabolism ; Transcription, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 9
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    Regulation of plasma cholesterol by lipoprotein receptors (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-05-08
    Description: The lipoprotein transport system holds the key to understanding the mechanisms by which genes, diet, and hormones interact to regulate the plasma cholesterol level in man. Crucial components of this system are lipoprotein receptors in the liver and extrahepatic tissues that mediate the uptake and degradation of cholesterol-carrying lipoproteins. The number of lipoprotein receptors, and hence the efficiency of disposal of plasma cholesterol, can be increased by cholesterol-lowering drugs. Regulation of lipoprotein receptors can be exploited pharmacologically in the therapy of hypercholesterolemia and atherosclerosis is man.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brown, M S -- Kovanen, P T -- Goldstein, J L -- HL-20948/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1981 May 8;212(4495):628-35.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6261329" target="_blank"〉PubMed〈/a〉
    Keywords: Arteriosclerosis/metabolism ; Biological Transport ; Cholesterol/*blood ; Chylomicrons/metabolism ; Dietary Fats/metabolism ; Homeostasis ; Humans ; Hyperlipoproteinemia Type II/metabolism ; Lipoproteins/*metabolism ; Liver/*metabolism ; Receptors, Cell Surface/metabolism/*physiology ; Receptors, LDL ; Receptors, Lipoprotein ; Triglycerides/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
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    Deletion in cysteine-rich region of LDL receptor impedes transport to cell surface in WHHL rabbit (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-06-06
    Description: The Watanabe heritable hyperlipidemic (WHHL) rabbit, an animal with familial hypercholesterolemia, produces a mutant receptor for plasma low-density lipoprotein (LDL) that is not transported to the cell surface at a normal rate. Cloning and sequencing of complementary DNA's from normal and WHHL rabbits, shows that this defect arises from an in-frame deletion of 12 nucleotides that eliminates four amino acids from the cysteine-rich ligand binding domain of the LDL receptor. A similar mutation, detected by S1 nuclease mapping of LDL receptor messenger RNA, occurred in a patient with familial hypercholesterolemia whose receptor also fails to be transported to the cell surface. These findings suggest that animal cells may have fail-safe mechanisms that prevent the surface expression of improperly folded proteins with unpaired or improperly bonded cysteine residues.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4451858/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4451858/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yamamoto, T -- Bishop, R W -- Brown, M S -- Goldstein, J L -- Russell, D W -- HL 01287/HL/NHLBI NIH HHS/ -- HL 20948/HL/NHLBI NIH HHS/ -- HL 31346/HL/NHLBI NIH HHS/ -- P01 HL020948/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1986 Jun 6;232(4755):1230-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3010466" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Biological Transport ; *Chromosome Deletion ; Cloning, Molecular ; Cysteine/genetics ; Dna ; DNA Restriction Enzymes ; Genes ; Humans ; Hyperlipoproteinemia Type II/*genetics ; Mutation ; RNA, Messenger ; Rabbits ; Receptors, LDL/*genetics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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