Русская Википедия:Браун, Майкл Стюарт

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Майкл Стюарт Браун (Шаблон:Lang-en; род. 13 апреля, 1941, Бруклин, Нью-Йорк, США) — американский Шаблон:Врач2 и Шаблон:Биохимик. За исследования наследственной гиперхолестеринемии и открытие рецептора липопротеинов низкой плотности вместе с Джозефом Голдштейном получил Нобелевскую премию по медицине и физиологии в 1985 году.

Член Национальной академии наук США (1980), иностранный член Лондонского королевского общества (1991).

Биография

Майкл Браун окончил Университет Пенсильвании в 1962 году и медицинскую школу этого же университета в 1966 году. С тех пор работает в Юго-Западном медицинском центре (Университет Техаса) в области метаболизма холестерина. Автор множества статей в ведущих мировых биологических и медицинских журналах. В 1985 году получил Нобелевскую премию за открытие рецептора липопротеинов низкой плотности.

Награды

• Шаблон:Нп5 (1976)
• Шаблон:Нп5 (1976)
• Шаблон:Нп5 (1978)
• Шаблон:Нп5 (1979)
• Международная премия Гайрднера (1981)
• Премия Луизы Гросс Хорвиц (1984)
• Премия Альберта Ласкера за фундаментальные медицинские исследования (1985)
• Шаблон:Нп5 (1985)
• Нобелевская премия по физиологии и медицине (1985)
• Шаблон:Нп5 (1987)
• Национальная научная медаль США (1988)
• Шаблон:Нп5 (1999)
• Шаблон:Нп5 (2002)
• Премия медицинского центра Олбани (2003)
• Шаблон:Нп5 (2005)
• Шаблон:Нп5 (2010)

Библиография

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[16] Independent pathways for secretion of cholesterol and apolipoprotein E by macrophages. Science. 1983 Feb 18;219(4586):871-3.

[17] Recycling receptors: the round-trip itinerary of migrant membrane proteins. Cell. 1983 Mar;32(3):663-7

[18] The LDL receptor locus in familial hypercholesterolemia: multiple mutations disrupt transport and processing of a membrane receptor. Cell. 1983 Mar;32(3):941-51.

[19] Depletion of intracellular potassium arrests coated pit formation and receptor-mediated endocytosis in fibroblasts. Cell. 1983 May;33(1):273-85

[20] Increase in membrane cholesterol: a possible trigger for degradation of HMG CoA reductase and crystalloid endoplasmic reticulum in UT-1 cells. Cell. 1984 Apr;36(4):835-45.

[21] Nucleotide sequence of 3-hydroxy-3-methyl-glutaryl coenzyme A reductase, a glycoprotein of endoplasmic reticulum. Nature. 1984 Apr 12-18;308(5960):613-7.

[22] Domain map of the LDL receptor: sequence homology with the epidermal growth factor precursor. Cell. 1984 Jun;37(2):577-85.

[23] HMG CoA reductase: a negatively regulated gene with unusual promoter and 5' untranslated regions. Cell. 1984 Aug;38(1):275-85.

[24] The human LDL receptor: a cysteine-rich protein with multiple Alu sequences in its mRNA. Cell. 1984 Nov;39(1):27-38

[25] Mutation in LDL receptor: Alu-Alu recombination deletes exons encoding transmembrane and cytoplasmic domains. Science. 1985 Jan 11;227(4683):140-6.

[26] The LDL receptor gene: a mosaic of exons shared with different proteins. Science. 1985 May 17;228(4701):815-22.

[27] Cassette of eight exons shared by genes for LDL receptor and EGF precursor. Science. 1985 May 17;228(4701):893-895

[28] Membrane-bound domain of HMG CoA reductase is required for sterol-enhanced degradation of the enzyme. Cell. 1985 May;41(1):249-58.

[29] Internalization-defective LDL receptors produced by genes with nonsense and frameshift mutations that truncate the cytoplasmic domain. Cell. 1985 Jul;41(3):735-43.

[30] 5' end of HMG CoA reductase gene contains sequences responsible for cholesterol-mediated inhibition of transcription. Cell. 1985 Aug;42(1):203-12.

[31] Scavenger cell receptor shared. Nature. 1985 Aug 22-28;316(6030):680-1.

[32] A receptor-mediated pathway for cholesterol homeostasis. Science. 1986 Apr 4;232(4746):34-47.

[33] The J.D. mutation in familial hypercholesterolemia: amino acid substitution in cytoplasmic domain impedes internalization of LDL receptors Cell. 1986 Apr 11;45(1):15-24.

[34] Deletion in cysteine-rich region of LDL receptor impedes transport to cell surface in WHHL rabbit. Science. 1986 Jun 6;232(4755):1230-7.

[35] Duplication of seven exons in LDL receptor gene caused by Alu-Alu recombination in a subject with familial hypercholesterolemia. Cell. 1987 Mar 13;48(5):827-35.

[36] 42 bp element from LDL receptor gene confers end-product repression by sterols when inserted into viral TK promoter. Cell. 1987 Mar 27;48(6):1061-9.

[37] Acid-dependent ligand dissociation and recycling of LDL receptor mediated by growth factor homology region. Nature. 1987 Apr 23-29;326(6115):760-765

[38] Overexpression of low density lipoprotein (LDL) receptor eliminates LDL from plasma in transgenic mice. Science. 1988 Mar 11;239(4845):1277-81.

[39] Inhibition of purified p21ras farnesyl: protein transferase by Cys-AAX tetrapeptides. Cell. 1990 Jul 13;62(1):81-8.

[40] Diet-induced hypercholesterolemia in mice: prevention by overexpression of LDL receptors. Science. 1990 Nov 30;250(4985):1273-5

[41] Protein farnesyltransferase and geranylgeranyltransferase share a common alpha subunit. Cell. 1991 May 3;65(3):429-34.

[42] cDNA cloning and expression of the peptide-binding beta subunit of rat p21ras farnesyltransferase, the counterpart of yeast DPR1/RAM1. Cell. 1991 Jul 26;66(2):327-34.

[43] Purification of component A of Rab geranylgeranyl transferase: possible identity with the choroideremia gene product. Cell. 1992 Sep 18;70(6):1049-57.

[44] Koch’s postulates for cholesterol. Cell. 1992 Oct 16;71(2):187-8.

[45] cDNA cloning of component A of Rab geranylgeranyl transferase and demonstration of its role as a Rab escort protein. Cell. 1993 Jun 18;73(6):1091-9

[46] SREBP-1, a basic-helix-loop-helix-leucine zipper protein that controls transcription of the low density lipoprotein receptor gene. Cell. 1993 Oct 8;75(1):187-97.

[47] Molecular characterization of a membrane transporter for lactate, pyruvate, and other monocarboxylates: implications for the Cori cycle. Cell. 1994 Mar 11;76(5):865-73.

[48] SREBP-1, a membrane-bound transcription factor released by sterol-regulated proteolysis. Cell. 1994 Apr 8;77(1):53-62

[49] Sterol-regulated release of SREBP-2 from cell membranes requires two sequential cleavages, one within a transmembrane segment. Cell. 1996 Jun 28;85(7):1037-46

[50] Sterol resistance in CHO cells traced to point mutation in SREBP cleavage-activating protein. Cell. 1996 Nov 1;87(3):415-26.

[51] The SREBP pathway: regulation of cholesterol metabolism by proteolysis of a membrane-bound transcription factor. Cell. 1997 May 2;89(3):331-40.

[52] Transport-dependent proteolysis of SREBP: relocation of site-1 protease from Golgi to ER obviates the need for SREBP transport to Golgi. Cell. 1999 Dec 23;99(7):703-12.

[53] Regulated intramembrane proteolysis: a control mechanism conserved from bacteria to humans. Cell. 2000 Feb 18;100(4):391-8.

[54] Regulated step in cholesterol feedback localized to budding of SCAP from ER membranes. Cell. 2000 Aug 4;102(3):315-23.

[55] Crucial step in cholesterol homeostasis: sterols promote binding of SCAP to INSIG-1, a membrane protein that facilitates retention of SREBPs in ER. Cell. 2002 Aug 23;110(4):489-500. Шаблон:Конец скрытого блока

Ссылки

• Юго-западный медицинский центр при Университете Техаса. Шаблон:Wayback Шаблон:Ref-en
• Сайт Департамента молекулярной генетики Брауна и Гольдштейна в Университете Техаса. Шаблон:Wayback