Biography:Michael Stuart Brown
Michael Brown | |
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Born | Michael Stuart Brown April 13, 1941 Brooklyn, New York, U.S. |
Nationality | American |
Alma mater |
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Known for | Regulation of cholesterol metabolism |
Awards |
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Scientific career | |
Fields | Biology |
Website | profiles |
Michael Stuart Brown ForMemRS NAS AAA&S APS (born April 13, 1941) is an American geneticist and Nobel laureate. He was awarded the Nobel Prize in Physiology or Medicine with Joseph L. Goldstein in 1985 for describing the regulation of cholesterol metabolism.[2][3][4][5]
Education and early life
Brown was born in Brooklyn, New York, the son of Evelyn, a homemaker, and Harvey Brown, a textile salesman.[4][6] His family is Jewish.[7] He graduated from Cheltenham High School (Wyncote, Pennsylvania). Brown graduated from the University of Pennsylvania in 1962 and received his M.D. from the University of Pennsylvania School of Medicine in 1966.[citation needed]
Career and research
Moving to the University of Texas Michael liked vann Warner Health Science Center in Dallas, now the UT Southwestern Medical Center, Brown and colleague Joseph L. Goldstein researched cholesterol metabolism and discovered that human cells have low-density lipoprotein (LDL) receptors that extract cholesterol from the bloodstream. The lack of sufficient LDL receptors is implicated in familial hypercholesterolemia, which predisposes heavily for cholesterol-related diseases. In addition to explaining the underlying pathology of this disease, their work uncovered a fundamental aspect of cell biology - receptor-mediated endocytosis. Their findings led to the development of statin drugs, the cholesterol-lowering compounds that today are used by 16 million Americans and are the most widely prescribed medications in the United States.[citation needed] Their discoveries are improving more lives every year, both in the US and around the world.[citation needed] New federal cholesterol guidelines will triple the number of Americans taking statin drugs to lower their cholesterol, reducing the risk of heart disease and stroke for countless people. Following these important advances, their team of dedicated researchers elucidated the role of lipid modification of proteins (protein prenylation) in cancer. In 1984 he was awarded the Louisa Gross Horwitz Prize from Columbia University together with Joseph L. Goldstein (co-recipient of 1985 Nobel Prize in Physiology or Medicine). In 1988, Brown received the National Medal of Science for his contributions to medicine.
In 1993, their trainees Xiaodong Wang and Michael Briggs purified the sterol regulatory element binding proteins (SREBPs). Since 1993, Brown, Goldstein, and their colleagues have described the unexpectedly complex machinery by which cells maintain the necessary levels of fats and cholesterol in the face of varying environmental circumstances.
Brown holds the W. A. (Monty) Moncrief Distinguished Chair in Cholesterol and Arteriosclerosis Research; is a Regental Professor of the University of Texas; holds the Paul J. Thomas Chair in Medicine.[citation needed]
Brown is also on the Prix Galien USA Committee that "recognizes the technical, scientific and clinical research skills necessary to develop innovative medicines".[citation needed]
Awards and honors
Brown has won numerous awards and honors, including:
- 2016 - Keynote Speaker at the Congress of Future Medical Leaders
- 2011 - Stadtman Distinguished Scientist Award, American Society for Biochemistry and Molecular Biology[8]
- 2007 - Builders of Science Award, Research!America[9]
- 2005 - Woodrow Wilson Award for Public Service[10]
- 2005 - Herbert Tabor Award, American Society for Biochemistry and Molecular Biology[11]
- 2003 - Albany Medical Center Prize[12]
- 2002 - Kober Medal, Association of American Physicians[13]
- 1999 - Warren Alpert Foundation Prize, Harvard Medical School[14]
- 1991 - Elected a Foreign Member of the Royal Society (ForMemRS)[1]
- 1987 - Elected member of the American Philosophical Society[15]
- 1986 - Golden Plate Award of the American Academy of Achievement[16]
- 1985 - Nobel Prize for physiology and medicine[17]
- 1985 - Albert Lasker Award for Basic Medical Research[18]
- 1985 - William Allan Award, American Society of Human Genetics[19]
- 1984 - Louisa Gross Horwitz Prize[20]
- 1981 - Gairdner Foundation International Award[21]
- 1981 - Elected member of the American Academy of Arts and Sciences[22]
- 1980 - elected member of the National Academy of Sciences[23]
- 1979 - Lounsbery Award, U.S. National Academy of Sciences[24]
- 1978 - Passano Award, Johns Hopkins University[25]
- 1976 - Pfizer Award in Enzyme Chemistry, American Chemical Society[26]
- 1974 - Heinrich Wieland Prize[27]
Bibliography
- "Expression of the familial hypercholesterolemia gene in heterozygotes: mechanism for a dominant disorder in man". Science 185 (4145): 61–3. Jul 1974. doi:10.1126/science.185.4145.61. PMID 4366052. Bibcode: 1974Sci...185...61B.
- "Regulation of the activity of the low density lipoprotein receptor in human fibroblasts". Cell 6 (3): 307–16. Nov 1975. doi:10.1016/0092-8674(75)90182-8. PMID 212203.
- "Release of low density lipoprotein from its cell surface receptor by sulfated glycosaminoglycans". Cell 7 (1): 85–95. Jan 1976. doi:10.1016/0092-8674(76)90258-0. PMID 181140.
- "Receptor-mediated control of cholesterol metabolism". Science 191 (4223): 150–4. Jan 1976. doi:10.1126/science.174194. PMID 174194. Bibcode: 1976Sci...191..150B.
- "Heterozygous familial hypercholesterolemia: failure of normal allele to compensate for mutant allele at a regulated genetic locus". Cell 9 (2): 195–203. Oct 1976. doi:10.1016/0092-8674(76)90110-0. PMID 184960.
- "Analysis of a mutant strain of human fibroblasts with a defect in the internalization of receptor-bound low density lipoprotein". Cell 9 (4 PT 2): 663–74. Dec 1976. doi:10.1016/0092-8674(76)90130-6. PMID 189940.
- "Role of the coated endocytic vesicle in the uptake of receptor-bound low density lipoprotein in human fibroblasts". Cell 10 (3): 351–64. Mar 1977. doi:10.1016/0092-8674(77)90022-8. PMID 191195.
- "Genetics of the LDL receptor: evidence that the mutations affecting binding and internalization are allelic". Cell 12 (3): 629–41. Nov 1977. doi:10.1016/0092-8674(77)90263-X. PMID 200368.
- "A mutation that impairs the ability of lipoprotein receptors to localise in coated pits on the cell surface of human fibroblasts". Nature 270 (5639): 695–9. 1977. doi:10.1038/270695a0. PMID 201867. Bibcode: 1977Natur.270..695A.
- "Immunocytochemical visualization of coated pits and vesicles in human fibroblasts: relation to low density lipoprotein receptor distribution". Cell 15 (3): 919–33. Nov 1978. doi:10.1016/0092-8674(78)90276-3. PMID 215316.
- "Coated pits, coated vesicles, and receptor-mediated endocytosis". Nature 279 (5715): 679–85. Jun 1979. doi:10.1038/279679a0. PMID 221835. Bibcode: 1979Natur.279..679G.
- "LDL receptors in coated vesicles isolated from bovine adrenal cortex: binding sites unmasked by detergent treatment". Cell 20 (3): 829–37. Jul 1980. doi:10.1016/0092-8674(80)90329-3. PMID 6251975.
- "Regulation of plasma cholesterol by lipoprotein receptors". Science 212 (4495): 628–35. May 1981. doi:10.1126/science.6261329. PMID 6261329. Bibcode: 1981Sci...212..628B.
- "Monensin interrupts the recycling of low density lipoprotein receptors in human fibroblasts". Cell 24 (2): 493–502. May 1981. doi:10.1016/0092-8674(81)90340-8. PMID 6263497.
- "Posttranslational processing of the LDL receptor and its genetic disruption in familial hypercholesterolemia". Cell 30 (3): 715–24. Oct 1982. doi:10.1016/0092-8674(82)90276-8. PMID 6291781.
- "Independent pathways for secretion of cholesterol and apolipoprotein E by macrophages". Science 219 (4586): 871–3. Feb 1983. doi:10.1126/science.6823554. PMID 6823554. Bibcode: 1983Sci...219..871B.
- "Recycling receptors: the round-trip itinerary of migrant membrane proteins". Cell 32 (3): 663–7. Mar 1983. doi:10.1016/0092-8674(83)90052-1. PMID 6299572.
- "The LDL receptor locus in familial hypercholesterolemia: multiple mutations disrupt transport and processing of a membrane receptor". Cell 32 (3): 941–51. Mar 1983. doi:10.1016/0092-8674(83)90079-X. PMID 6299582.
- "Depletion of intracellular potassium arrests coated pit formation and receptor-mediated endocytosis in fibroblasts". Cell 33 (1): 273–85. May 1983. doi:10.1016/0092-8674(83)90356-2. PMID 6147196.
- "Increase in membrane cholesterol: a possible trigger for degradation of HMG CoA reductase and crystalloid endoplasmic reticulum in UT-1 cells". Cell 36 (4): 835–45. Apr 1984. doi:10.1016/0092-8674(84)90033-3. PMID 6705048.
- Chin DJ; Gil G; Russell DW et al. (1984). "Nucleotide sequence of 3-hydroxy-3-methyl-glutaryl coenzyme A reductase, a glycoprotein of endoplasmic reticulum". Nature 308 (5960): 613–7. doi:10.1038/308613a0. PMID 6546784. Bibcode: 1984Natur.308..613C.
- "Domain map of the LDL receptor: sequence homology with the epidermal growth factor precursor". Cell 37 (2): 577–85. Jun 1984. doi:10.1016/0092-8674(84)90388-X. PMID 6327078.
- Reynolds GA; Basu SK; Osborne TF et al. (Aug 1984). "HMG CoA reductase: a negatively regulated gene with unusual promoter and 5' untranslated regions". Cell 38 (1): 275–85. doi:10.1016/0092-8674(84)90549-X. PMID 6088070.
- Yamamoto T; Davis CG; Brown MS et al. (Nov 1984). "The human LDL receptor: a cysteine-rich protein with multiple Alu sequences in its mRNA". Cell 39 (1): 27–38. doi:10.1016/0092-8674(84)90188-0. PMID 6091915.
- "Mutation in LDL receptor: Alu-Alu recombination deletes exons encoding transmembrane and cytoplasmic domains". Science 227 (4683): 140–6. Jan 1985. doi:10.1126/science.3155573. PMID 3155573. Bibcode: 1985Sci...227..140L.
- "The LDL receptor gene: a mosaic of exons shared with different proteins". Science 228 (4701): 815–22. May 1985. doi:10.1126/science.2988123. PMID 2988123. Bibcode: 1985Sci...228..815S.
- "Cassette of eight exons shared by genes for LDL receptor and EGF precursor". Science 228 (4701): 893–5. May 1985. doi:10.1126/science.3873704. PMID 3873704. Bibcode: 1985Sci...228..893S.
- "Membrane-bound domain of HMG CoA reductase is required for sterol-enhanced degradation of the enzyme". Cell 41 (1): 249–58. May 1985. doi:10.1016/0092-8674(85)90078-9. PMID 3995584.
- "Internalization-defective LDL receptors produced by genes with nonsense and frameshift mutations that truncate the cytoplasmic domain". Cell 41 (3): 735–43. Jul 1985. doi:10.1016/S0092-8674(85)80054-4. PMID 3924410.
- "5' end of HMG CoA reductase gene contains sequences responsible for cholesterol-mediated inhibition of transcription". Cell 42 (1): 203–12. Aug 1985. doi:10.1016/S0092-8674(85)80116-1. PMID 3860301.
- "Scavenger cell receptor shared". Nature 316 (6030): 680–1. 1985. doi:10.1038/316680a0. PMID 4033768.
- "A receptor-mediated pathway for cholesterol homeostasis". Science 232 (4746): 34–47. Apr 1986. doi:10.1126/science.3513311. PMID 3513311. Bibcode: 1986Sci...232...34B.
- "The J.D. mutation in familial hypercholesterolemia: amino acid substitution in cytoplasmic domain impedes internalization of LDL receptors". Cell 45 (1): 15–24. Apr 1986. doi:10.1016/0092-8674(86)90533-7. PMID 3955657.
- "Deletion in cysteine-rich region of LDL receptor impedes transport to cell surface in WHHL rabbit". Science 232 (4755): 1230–7. Jun 1986. doi:10.1126/science.3010466. PMID 3010466. Bibcode: 1986Sci...232.1230Y.
- "Duplication of seven exons in LDL receptor gene caused by Alu-Alu recombination in a subject with familial hypercholesterolemia". Cell 48 (5): 827–35. Mar 1987. doi:10.1016/0092-8674(87)90079-1. PMID 3815525.
- "42 bp element from LDL receptor gene confers end-product repression by sterols when inserted into viral TK promoter". Cell 48 (6): 1061–9. Mar 1987. doi:10.1016/0092-8674(87)90713-6. PMID 3030558.
- "Acid-dependent ligand dissociation and recycling of LDL receptor mediated by growth factor homology region". Nature 326 (6115): 760–5. 1987. doi:10.1038/326760a0. PMID 3494949. Bibcode: 1987Natur.326..760D.
- "Overexpression of low density lipoprotein (LDL) receptor eliminates LDL from plasma in transgenic mice". Science 239 (4845): 1277–81. Mar 1988. doi:10.1126/science.3344433. PMID 3344433. Bibcode: 1988Sci...239.1277H.
- "Inhibition of purified p21ras farnesyl:protein transferase by Cys-AAX tetrapeptides". Cell 62 (1): 81–8. Jul 1990. doi:10.1016/0092-8674(90)90242-7. PMID 2194674.
- "Diet-induced hypercholesterolemia in mice: prevention by overexpression of LDL receptors". Science 250 (4985): 1273–5. Nov 1990. doi:10.1126/science.2244210. PMID 2244210. Bibcode: 1990Sci...250.1273Y.
- "Protein farnesyltransferase and geranylgeranyltransferase share a common alpha subunit". Cell 65 (3): 429–34. May 1991. doi:10.1016/0092-8674(91)90460-G. PMID 2018975.
- "cDNA cloning and expression of the peptide-binding beta subunit of rat p21ras farnesyltransferase, the counterpart of yeast DPR1/RAM1". Cell 66 (2): 327–34. Jul 1991. doi:10.1016/0092-8674(91)90622-6. PMID 1855253.
- "Purification of component A of Rab geranylgeranyl transferase: possible identity with the choroideremia gene product". Cell 70 (6): 1049–57. Sep 1992. doi:10.1016/0092-8674(92)90253-9. PMID 1525821.
- "Koch's postulates for cholesterol". Cell 71 (2): 187–8. Oct 1992. doi:10.1016/0092-8674(92)90346-E. PMID 1423585.
- Andres DA; Seabra MC; Brown MS et al. (Jun 1993). "cDNA cloning of component A of Rab geranylgeranyl transferase and demonstration of its role as a Rab escort protein". Cell 73 (6): 1091–9. doi:10.1016/0092-8674(93)90639-8. PMID 8513495.
- Yokoyama C; Wang X; Briggs MR et al. (Oct 1993). "SREBP-1, a basic-helix-loop-helix-leucine zipper protein that controls transcription of the low density lipoprotein receptor gene". Cell 75 (1): 187–97. doi:10.1016/S0092-8674(05)80095-9. PMID 8402897.
- "Molecular characterization of a membrane transporter for lactate, pyruvate, and other monocarboxylates: implications for the Cori cycle". Cell 76 (5): 865–73. Mar 1994. doi:10.1016/0092-8674(94)90361-1. PMID 8124722.
- "SREBP-1, a membrane-bound transcription factor released by sterol-regulated proteolysis". Cell 77 (1): 53–62. Apr 1994. doi:10.1016/0092-8674(94)90234-8. PMID 8156598.
- "Sterol-regulated release of SREBP-2 from cell membranes requires two sequential cleavages, one within a transmembrane segment". Cell 85 (7): 1037–46. Jun 1996. doi:10.1016/S0092-8674(00)81304-5. PMID 8674110.
- "Sterol resistance in CHO cells traced to point mutation in SREBP cleavage-activating protein". Cell 87 (3): 415–26. Nov 1996. doi:10.1016/S0092-8674(00)81362-8. PMID 8898195.
- "The SREBP pathway: regulation of cholesterol metabolism by proteolysis of a membrane-bound transcription factor". Cell 89 (3): 331–40. May 1997. doi:10.1016/S0092-8674(00)80213-5. PMID 9150132.
- "Transport-dependent proteolysis of SREBP: relocation of site-1 protease from Golgi to ER obviates the need for SREBP transport to Golgi". Cell 99 (7): 703–12. Dec 1999. doi:10.1016/S0092-8674(00)81668-2. PMID 10619424.
- "Regulated intramembrane proteolysis: a control mechanism conserved from bacteria to humans". Cell 100 (4): 391–8. Feb 2000. doi:10.1016/S0092-8674(00)80675-3. PMID 10693756.
- "Regulated step in cholesterol feedback localized to budding of SCAP from ER membranes". Cell 102 (3): 315–23. Aug 2000. doi:10.1016/S0092-8674(00)00037-4. PMID 10975522.
- Yang T; Espenshade PJ; Wright ME et al. (Aug 2002). "Crucial step in cholesterol homeostasis: sterols promote binding of SCAP to INSIG-1, a membrane protein that facilitates retention of SREBPs in ER". Cell 110 (4): 489–500. doi:10.1016/S0092-8674(02)00872-3. PMID 12202038.
See also
- List of Jewish Nobel laureates
References
- ↑ 1.0 1.1 "Professor Michael Brown ForMemRS". London: Royal Society. https://royalsociety.org/people/michael-brown-11147/.
- ↑ "Biography: Michael S. Brown". The Notable Names Database. Soylent Communications. 2008. http://www.nndb.com/people/174/000123802.
- ↑ "Michael Brown - Nobel Prize Inspiration Initiative". Nobelprizeii.org. http://www.nobelprizeii.org/nobel-laureate/michael-brown/.
- ↑ 4.0 4.1 "Michael S. Brown - Biographical". Nobelprize.org. 1941-04-13. https://www.nobelprize.org/nobel_prizes/medicine/laureates/1985/brown-bio.html.
- ↑ "Michael S. Brown - Nobel Lecture: A Receptor-Mediated Pathway for Cholesterol Homeostasis". Nobelprize.org. 1985-12-08. https://www.nobelprize.org/nobel_prizes/medicine/laureates/1985/brown-lecture.html.
- ↑ "BROWN (Brown), Michael, photo, biography". Persona.rin.ru. 1941-04-13. http://persona.rin.ru/eng/view/f/0/17629/brown-brown,-michael.
- ↑ "Jewish Nobel Prize Winners in Medicine". https://www.jinfo.org/Nobels_Medicine.html.
- ↑ "Earl and Thressa Stadtman Distinguished Scientist Award". Asbmb.org. http://www.asbmb.org/Page.aspx?id=6128.
- ↑ "University of Texas Southwestern Medical Center Leaders to Receive Research!America Advocacy Award". Research!America. 2007-03-21. http://www.researchamerica.org/release_07mar21_builders.
- ↑ [1]
- ↑ "Herbert Tabor Research Award". Asbmb.org. http://www.asbmb.org/Page.aspx?id=536.
- ↑ "Albany Medical College: 2003". Amc.edu. 2015-08-14. http://www.amc.edu/Academic/AlbanyPrize/Recipients/recipients_previous/2003.cfm.
- ↑ "Presentation of the Kober Medal to Joseph L. Goldstein and Michael S. Brown" (PDF). Jci.org. http://www.jci.org/articles/view/120039/files/pdf.
- ↑ [2]
- ↑ "APS Member History". https://search.amphilsoc.org/memhist/search?creator=Michael+S.+Brown&title=&subject=&subdiv=&mem=&year=&year-max=&dead=&keyword=&smode=advanced.
- ↑ "Golden Plate Awardees of the American Academy of Achievement". American Academy of Achievement. https://achievement.org/our-history/golden-plate-awards/#science-exploration.
- ↑ "The Nobel Prize in Physiology or Medicine 1985". The Nobel Foundation. https://www.nobelprize.org/prizes/medicine/1985/summary/.
- ↑ "1985 Basic Medical Research Award". The Lasker Foundation. 2007-09-16. http://www.laskerfoundation.org/awards/1985basic.htm.
- ↑ "Past ASHG Award Recipients". ASHG. http://www.ashg.org/pages/awards_pastrecipients.shtml#allan.
- ↑ "Horwitz Prize Awardees". Columbia University. 20 June 2018. https://www.cuimc.columbia.edu/research/louisa-gross-horwitz-prize/horwitz-prize-awardees.
- ↑ "Joseph L. Goldstein". Gairdner. http://www.gairdner.org/content/joseph-l-goldstein.
- ↑ "Michael Stuart Brown". https://www.amacad.org/person/michael-stuart-brown.
- ↑ "Michael Brown". http://www.nasonline.org/member-directory/members/57317.html.
- ↑ "Richard Lounsbery Award". Nasonline.org. http://www.nasonline.org/programs/awards/richard-lounsbery-award.html.
- ↑ [3]
- ↑ "Pfizer Award in Enzyme Chemistry". Divbiolchem.org. http://www.divbiolchem.org/content/pfizerawardees1.
- ↑ "Heinrich Wieland Prize Laureates 1970 - 1979". Boehringer Ingelheim Stiftung. https://www.heinrich-wieland-prize.de/heinrich-wieland-laureates/id-1979-1970.html.
External links
- Miss nobel-id as parameter
Original source: https://en.wikipedia.org/wiki/Michael Stuart Brown.
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