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Samuel E. Lux IV, MD


Pediatric Hematology/Oncology

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Physician

  • Chief Emeritus, Division of Hematology/Oncology, Boston Children's Hospital
  • Vice-Chair for Research, Department of Medicine, Boston Children's Hospital
  • Director, Internship Selection Committee, Boston Children's Hospital
  • Senior Physician
  • Robert A. Stranahan Professor of Pediatrics, Harvard Medical School

Centers/Programs

Clinical Interests

  • Anemias

Diseases Treated

  • Anemia, Childhood
  • Bone Marrow Failure, Childhood
  • Hemophilia, Childhood
  • Immune Thrombocytopenia (ITP), Childhood
  • Myelodysplastic Syndrome (MDS), Childhood
  • Sickle Cell Disease, Childhood
  • Thalassemia, Childhood

Contact Information

  • Appointments617-355-8246, ext. 1
  • Office Phone Number617-355-7904
  • Fax617-738-5922

Bio

Dr. Lux received his MD in 1967 from Kansas University School of Medicine. From 1967 to 1969, he did his internship and residency at Children's Hospital in Boston. He subsequently studied protein chemistry at the National Institutes of Health, before returning to Children's in 1972 for fellowship training in Hematology/Oncology. Since 1984, he has been Chief of the Hematology/Oncology Division at Children's Hospital Boston. His research focuses on red blood cell membrane disorders and anemias.

Board Certification:

  • Pediatrics, 1974

Fellowship:

  • Boston Children's Hospital

Residency:

  • Boston Children's Hospital

Medical School:

  • University of Kansas School of Medicine

Recent Awards:

  • Teaching Award, Harvard Medical School Second-Year Class 1999
  • Prize for Excellence in Preclinical Teaching, Harvard Medical School 1982
  • Teaching Prize, Harvard Medical School Graduating Class 1983
  • E. Mead Johnson Award for Research in Pediatrics, American Academy of Pediatrics 1983
  • Boylston Society Award for Excellence in Teaching, Harvard Medical School 1984
  • MERIT Award, National Institutes of Health 1988-95
  • Dameshek Prize for Research in Hematology, American Society of Hematology 1989
  • E. Donnall Thomas Award, American Society of Hematology 2001

Research

Structure and Function of Membrane Skeletons

Our laboratory focuses on the organization and functions of the spectrin-based membrane skeleton. Current work is directed at three related problems:Ankyrin functions. Ankyrins link integral membrane proteins to the spectrin-based membrane skeleton. Members of the laboratory first cloned red cell ankyrin or Ank1 and subsequently cloned and characterized Ank3, the major nonerythroid ankyrin. To understand how ankyrins work and what they do, we are knocking-out various ankyrins and replacing them with modified or chimeric ankyrins. We also are studying the interactions and functions of a 'death domain' that is found in all ankyrins.Hereditary defects in membrane skeleton proteins. During the past decade our laboratory and others have shown that hereditary spherocytosis is caused by defects in the connections that attach the membrane skeleton to the overlying lipid bilayer. To test the pathophysiology, we produced mice that lack the erythroid anion exchanger (AE1), the principal Ank1 ligand. Although much experimental evidence indicates that AE1 is required for membrane skeleton assembly, AE1-/- red blood cells have a normal membrane skeleton. Even so, they shed bilayer lipids at a prodigious rate, leading to extreme hemolysis and spherocytosis. This indicates that AE1 and probably other integral membrane proteins have a 'lipid-anchoring' function. Members of our laboratory are currently testing whether the anemia and lipid loss can be rescued by expression in situ of various modified AE1s.Organelle membrane skeletons. There is increasing evidence from our laboratory and others that some organelles (e.g., lysosomes, Golgi) also have membrane skeletons. This is a fertile area for investigation since, so far, almost nothing is known about the structure or function of these skeletons. In addition, we recently discovered two new spectrins (bIII and bIV) that are bound to the Golgi or a subset of cytoplasmic vesicles or both. We are currently characterizing the interactions of these spectrins and testing the hypothesis that they are involved in the vesicle trafficking.

Lacy JN, Ulirsch JC, Grace RF, Towne MC, Hale J, Mohandas N, Lux SE, Agrawal PB, Sankaran VG. Exome sequencing results in successful diagnosis and treatment of a severe congenital anemia. Cold Spring Harb Mol Case Stud. 2016 Jul; 2(4):a000885.
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Lux SE. Anatomy of the red cell membrane skeleton: unanswered questions. Blood. 2016 Jan 14; 127(2):187-99.
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Stewart AK, Shmukler BE, Vandorpe DH, Rivera A, Heneghan JF, Li X, Hsu A, Karpatkin M, O'Neill AF, Bauer DE, Heeney MM, John K, Kuypers FA, Gallagher PG, Lux SE, Brugnara C, Westhoff CM, Alper SL. Loss-of-function and gain-of-function phenotypes of stomatocytosis mutant RhAG F65S. Am J Physiol Cell Physiol. 2011 Dec; 301(6):C1325-43.
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Williams DA, Porter ES, Lux SE, Grier HE, Mack JW, Orkin SH. Training program in cancer and blood diseases: Pediatric Hematology/Oncology Fellowship Program, Children's Hospital Boston/Dana-Farber Cancer Institute. Am J Hematol. 2010 Oct; 85(10):793-4.
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Korsgren C, Lux SE. The carboxyterminal EF domain of erythroid alpha-spectrin is necessary for optimal spectrin-actin binding. Blood. 2010 Oct 07; 116(14):2600-7.
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Stankewich MC, Gwynn B, Ardito T, Ji L, Kim J, Robledo RF, Lux SE, Peters LL, Morrow JS. Targeted deletion of betaIII spectrin impairs synaptogenesis and generates ataxic and seizure phenotypes. Proc Natl Acad Sci U S A. 2010 Mar 30; 107(13):6022-7.
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Robledo RF, Lambert AJ, Birkenmeier CS, Cirlan MV, Cirlan AF, Campagna DR, Lux SE, Peters LL. Analysis of novel sph (spherocytosis) alleles in mice reveals allele-specific loss of band 3 and adducin in alpha-spectrin-deficient red cells. Blood. 2010 Mar 04; 115(9):1804-14.
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Korsgren C, Peters LL, Lux SE. Protein 4.2 binds to the carboxyl-terminal EF-hands of erythroid alpha-spectrin in a calcium- and calmodulin-dependent manner. J Biol Chem. 2010 Feb 12; 285(7):4757-70.
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Stapleton FB, Lux SE. A uniform third-year application and offer date for pediatric fellow applicants: pro and con. J Pediatr. 2006 Nov; 149(5):587-588.
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An X, Debnath G, Guo X, Liu S, Lux SE, Baines A, Gratzer W, Mohandas N. Identification and functional characterization of protein 4.1R and actin-binding sites in erythrocyte beta spectrin: regulation of the interactions by phosphatidylinositol-4,5-bisphosphate. Biochemistry. 2005 Aug 09; 44(31):10681-8.
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Eber S, Lux SE. Hereditary spherocytosis--defects in proteins that connect the membrane skeleton to the lipid bilayer. Semin Hematol. 2004 Apr; 41(2):118-41.
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Lux S, Marshall JC, Ritzl A, Weiss PH, Pietrzyk U, Shah NJ, Zilles K, Fink GR. A functional magnetic resonance imaging study of local/global processing with stimulus presentation in the peripheral visual hemifields. Neuroscience. 2004; 124(1):113-20.
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Peters LL, Swearingen RA, Andersen SG, Gwynn B, Lambert AJ, Li R, Lux SE, Churchill GA. Identification of quantitative trait loci that modify the severity of hereditary spherocytosis in wan, a new mouse model of band-3 deficiency. Blood. 2004 Apr 15; 103(8):3233-40.
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Ozcan R, Jarolim P, Lux SE, Ungewickell E, Eber SW. Simultaneous (AC)n microsatellite polymorphism analysis and single-stranded conformation polymorphism screening is an efficient strategy for detecting ankyrin-1 mutations in dominant hereditary spherocytosis. Br J Haematol. 2003 Aug; 122(4):669-77.
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Paw BH, Davidson AJ, Zhou Y, Li R, Pratt SJ, Lee C, Trede NS, Brownlie A, Donovan A, Liao EC, Ziai JM, Drejer AH, Guo W, Kim CH, Gwynn B, Peters LL, Chernova MN, Alper SL, Zapata A, Wickramasinghe SN, Lee MJ, Lux SE, Fritz A, Postlethwait JH, Zon LI. Cell-specific mitotic defect and dyserythropoiesis associated with erythroid band 3 deficiency. Nat Genet. 2003 May; 34(1):59-64.
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Tse WT, Tang J, Jin O, Korsgren C, John KM, Kung AL, Gwynn B, Peters LL, Lux SE. A new spectrin, beta IV, has a major truncated isoform that associates with promyelocytic leukemia protein nuclear bodies and the nuclear matrix. J Biol Chem. 2001 Jun 29; 276(26):23974-85.
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Gallagher PG, Romana M, Tse WT, Lux SE, Forget BG. The human ankyrin-1 gene is selectively transcribed in erythroid cell lines despite the presence of a housekeeping-like promoter. Blood. 2000 Aug 01; 96(3):1136-43.
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Donovan A, Brownlie A, Zhou Y, Shepard J, Pratt SJ, Moynihan J, Paw BH, Drejer A, Barut B, Zapata A, Law TC, Brugnara C, Lux SE, Pinkus GS, Pinkus JL, Kingsley PD, Palis J, Fleming MD, Andrews NC, Zon LI. Positional cloning of zebrafish ferroportin1 identifies a conserved vertebrate iron exporter. Nature. 2000 Feb 17; 403(6771):776-81.
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Jensen LJ, Stuart-Tilley AK, Peters LL, Lux SE, Alper SL, Breton S. Immunolocalization of AE2 anion exchanger in rat and mouse epididymis. Biol Reprod. 1999 Oct; 61(4):973-80.
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Rasband MN, Peles E, Trimmer JS, Levinson SR, Lux SE, Shrager P. Dependence of nodal sodium channel clustering on paranodal axoglial contact in the developing CNS. J Neurosci. 1999 Sep 01; 19(17):7516-28.
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Berezovska O, Frosch M, McLean P, Knowles R, Koo E, Kang D, Shen J, Lu FM, Lux SE, Tonegawa S, Hyman BT. The Alzheimer-related gene presenilin 1 facilitates notch 1 in primary mammalian neurons. Brain Res Mol Brain Res. 1999 Jun 08; 69(2):273-80.
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Peters LL, Jindel HK, Gwynn B, Korsgren C, John KM, Lux SE, Mohandas N, Cohen CM, Cho MR, Golan DE, Brugnara C. Mild spherocytosis and altered red cell ion transport in protein 4. 2-null mice. J Clin Invest. 1999 Jun; 103(11):1527-37.
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Tse WT, Lux SE. Red blood cell membrane disorders. Br J Haematol. 1999 Jan; 104(1):2-13.
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Berezovska O, McLean P, Knowles R, Frosh M, Lu FM, Lux SE, Hyman BT. Notch1 inhibits neurite outgrowth in postmitotic primary neurons. Neuroscience. 1999; 93(2):433-9.
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Cho MR, Eber SW, Liu SC, Lux SE, Golan DE. Regulation of band 3 rotational mobility by ankyrin in intact human red cells. Biochemistry. 1998 Dec 22; 37(51):17828-35.
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Stankewich MC, Tse WT, Peters LL, Ch'ng Y, John KM, Stabach PR, Devarajan P, Morrow JS, Lux SE. A widely expressed betaIII spectrin associated with Golgi and cytoplasmic vesicles. Proc Natl Acad Sci U S A. 1998 Nov 24; 95(24):14158-63.
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Doctor RB, Chen J, Peters LL, Lux SE, Mandel LJ. Distribution of epithelial ankyrin (Ank3) spliceoforms in renal proximal and distal tubules. Am J Physiol. 1998 Jan; 274(1 Pt 2):F129-38.
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Gallagher PG, Tse WT, Scarpa AL, Lux SE, Forget BG. Structure and organization of the human ankyrin-1 gene. Basis for complexity of pre-mRNA processing. J Biol Chem. 1997 Aug 01; 272(31):19220-8.
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Hoock TC, Peters LL, Lux SE. Isoforms of ankyrin-3 that lack the NH2-terminal repeats associate with mouse macrophage lysosomes. J Cell Biol. 1997 Mar 10; 136(5):1059-70.
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Peters LL, Shivdasani RA, Liu SC, Hanspal M, John KM, Gonzalez JM, Brugnara C, Gwynn B, Mohandas N, Alper SL, Orkin SH, Lux SE. Anion exchanger 1 (band 3) is required to prevent erythrocyte membrane surface loss but not to form the membrane skeleton. Cell. 1996 Sep 20; 86(6):917-27.
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Shalev O, Shinar E, Lux SE. Isolated beta-globin chains reproduce, in normal red cell membranes, the defective binding of spectrin to alpha-thalassaemic membranes. Br J Haematol. 1996 Aug; 94(2):273-8.
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Eber SW, Gonzalez JM, Lux ML, Scarpa AL, Tse WT, Dornwell M, Herbers J, Kugler W, Ozcan R, Pekrun A, Gallagher PG, Schröter W, Forget BG, Lux SE. Ankyrin-1 mutations are a major cause of dominant and recessive hereditary spherocytosis. Nat Genet. 1996 Jun; 13(2):214-8.
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Lu FM, Lux SE. Constitutively active human Notch1 binds to the transcription factor CBF1 and stimulates transcription through a promoter containing a CBF1-responsive element. Proc Natl Acad Sci U S A. 1996 May 28; 93(11):5663-7.
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Jenkins PB, Abou-Alfa GK, Dhermy D, Bursaux E, Féo C, Scarpa AL, Lux SE, Garbarz M, Forget BG, Gallagher PG. A nonsense mutation in the erythrocyte band 3 gene associated with decreased mRNA accumulation in a kindred with dominant hereditary spherocytosis. J Clin Invest. 1996 Jan 15; 97(2):373-80.
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Joiner CH, Franco RS, Jiang M, Franco MS, Barker JE, Lux SE. Increased cation permeability in mutant mouse red blood cells with defective membrane skeletons. Blood. 1995 Dec 01; 86(11):4307-14.
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Piepenhagen PA, Peters LL, Lux SE, Nelson WJ. Differential expression of Na(+)-K(+)-ATPase, ankyrin, fodrin, and E-cadherin along the kidney nephron. Am J Physiol. 1995 Dec; 269(6 Pt 1):C1417-32.
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Morris MB, Lux SE. Characterization of the binary interaction between human erythrocyte protein 4.1 and actin. Eur J Biochem. 1995 Aug 01; 231(3):644-50.
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Peters LL, John KM, Lu FM, Eicher EM, Higgins A, Yialamas M, Turtzo LC, Otsuka AJ, Lux SE. Ank3 (epithelial ankyrin), a widely distributed new member of the ankyrin gene family and the major ankyrin in kidney, is expressed in alternatively spliced forms, including forms that lack the repeat domain. J Cell Biol. 1995 Jul; 130(2):313-30.
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White RA, Geissler EN, Adkison LR, Dowler LL, Alper SL, Lux SE. Chromosomal location of the murine anion exchanger genes encoding AE2 and AE3. Mamm Genome. 1994 Dec; 5(12):827-9.
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Savvides P, Shalev O, John KM, Lux SE. Combined spectrin and ankyrin deficiency is common in autosomal dominant hereditary spherocytosis. Blood. 1993 Nov 15; 82(10):2953-60.
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Platt OS, Lux SE, Falcone JF. A highly conserved region of human erythrocyte ankyrin contains the capacity to bind spectrin. J Biol Chem. 1993 Nov 15; 268(32):24421-6.
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Becker PS, Tse WT, Lux SE, Forget BG. Beta spectrin kissimmee: a spectrin variant associated with autosomal dominant hereditary spherocytosis and defective binding to protein 4.1. J Clin Invest. 1993 Aug; 92(2):612-6.
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Birkenmeier CS, White RA, Peters LL, Hall EJ, Lux SE, Barker JE. Complex patterns of sequence variation and multiple 5' and 3' ends are found among transcripts of the erythroid ankyrin gene. J Biol Chem. 1993 May 05; 268(13):9533-40.
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Peters LL, Andrews NC, Eicher EM, Davidson MB, Orkin SH, Lux SE. Mouse microcytic anaemia caused by a defect in the gene encoding the globin enhancer-binding protein NF-E2. Nature. 1993 Apr 22; 362(6422):768-70.
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Peters LL, Lux SE. Ankyrins: structure and function in normal cells and hereditary spherocytes. Semin Hematol. 1993 Apr; 30(2):85-118.
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Wang CC, Badylak JA, Lux SE, Moriyama R, Dixon JE, Low PS. Expression, purification, and characterization of the functional dimeric cytoplasmic domain of human erythrocyte band 3 in Escherichia coli. Protein Sci. 1992 Sep; 1(9):1206-14.
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White RA, Peters LL, Adkison LR, Korsgren C, Cohen CM, Lux SE. The murine pallid mutation is a platelet storage pool disease associated with the protein 4.2 (pallidin) gene. Nat Genet. 1992 Sep; 2(1):80-3.
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Peters LL, White RA, Birkenmeier CS, Bloom ML, Lux SE, Barker JE. Changing patterns in cytoskeletal mRNA expression and protein synthesis during murine erythropoiesis in vivo. Proc Natl Acad Sci U S A. 1992 Jul 01; 89(13):5749-53.
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White RA, Birkenmeier CS, Peters LL, Barker JE, Lux SE. Murine erythrocyte ankyrin cDNA: highly conserved regions of the regulatory domain. Mamm Genome. 1992; 3(5):281-5.
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Gallagher PG, Tse WT, Scarpa AL, Lux SE, Forget BG. Large numbers of alternatively spliced isoforms of the regulatory region of human erythrocyte ankyrin. Trans Assoc Am Physicians. 1992; 105:268-77.
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Peters LL, Birkenmeier CS, Bronson RT, White RA, Lux SE, Otto E, Bennett V, Higgins A, Barker JE. Purkinje cell degeneration associated with erythroid ankyrin deficiency in nb/nb mice. J Cell Biol. 1991 Sep; 114(6):1233-41.
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Tse WT, Menninger JC, Yang-Feng TL, Francke U, Sahr KE, Lux SE, Ward DC, Forget BG. Isolation and chromosomal localization of a novel nonerythroid ankyrin gene. Genomics. 1991 Aug; 10(4):858-66.
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Becker PS, Schwartz MA, Morrow JS, Lux SE. Radiolabel-transfer cross-linking demonstrates that protein 4.1 binds to the N-terminal region of beta spectrin and to actin in binary interactions. Eur J Biochem. 1990 Nov 13; 193(3):827-36.
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Costa FF, Agre P, Watkins PC, Winkelmann JC, Tang TK, John KM, Lux SE, Forget BG. Linkage of dominant hereditary spherocytosis to the gene for the erythrocyte membrane-skeleton protein ankyrin. N Engl J Med. 1990 Oct 11; 323(15):1046-50.
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Lux SE, Tse WT, Menninger JC, John KM, Harris P, Shalev O, Chilcote RR, Marchesi SL, Watkins PC, Bennett V, et al. Hereditary spherocytosis associated with deletion of human erythrocyte ankyrin gene on chromosome 8. Nature. 1990 Jun 21; 345(6277):736-9.
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White RA, Birkenmeier CS, Lux SE, Barker JE. Ankyrin and the hemolytic anemia mutation, nb, map to mouse chromosome 8: presence of the nb allele is associated with a truncated erythrocyte ankyrin. Proc Natl Acad Sci U S A. 1990 Apr; 87(8):3117-21.
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Lux SE, John KM, Bennett V. Analysis of cDNA for human erythrocyte ankyrin indicates a repeated structure with homology to tissue-differentiation and cell-cycle control proteins. Nature. 1990 Mar 01; 344(6261):36-42.
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Tse WT, Menninger JC, Ward DC, Chilcote RR, John KM, Lux SE, Forget BG. Demonstration of the deletion of a copy of the ankyrin gene in a patient with hereditary spherocytosis by in situ hybridization. Trans Assoc Am Physicians. 1990; 103:242-8.
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Lux SE, John KM, Kopito RR, Lodish HF. Cloning and characterization of band 3, the human erythrocyte anion-exchange protein (AE1). Proc Natl Acad Sci U S A. 1989 Dec; 86(23):9089-93.
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Davies KA, Lux SE. Hereditary disorders of the red cell membrane skeleton. Trends Genet. 1989 Jul; 5(7):222-7.
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Davis L, Lux SE, Bennett V. Mapping the ankyrin-binding site of the human erythrocyte anion exchanger. J Biol Chem. 1989 Jun 05; 264(16):9665-72.
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Shinar E, Rachmilewitz EA, Lux SE. Differing erythrocyte membrane skeletal protein defects in alpha and beta thalassemia. J Clin Invest. 1989 Feb; 83(2):404-10.
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Moo-Penn WF, Jue DL, Johnson MH, Olsen KW, Shih D, Jones RT, Lux SE, Rodgers P, Arnone A. Hemoglobin Brockton [beta 138 (H16) Ala----Pro]: an unstable variant near the C-terminus of the beta-subunits with normal oxygen-binding properties. Biochemistry. 1988 Oct 04; 27(20):7614-9.
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Becker PS, Morrow JS, Lux SE. Abnormal oxidant sensitivity and beta-chain structure of spectrin in hereditary spherocytosis associated with defective spectrin-protein 4.1 binding. J Clin Invest. 1987 Aug; 80(2):557-65.
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Wolfe LC, Byrne AM, Lux SE. Molecular defect in the membrane skeleton of blood bank-stored red cells. Abnormal spectrin-protein 4.1-actin complex formation. J Clin Invest. 1986 Dec; 78(6):1681-6.
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Joiner CH, Platt OS, Lux SE. Cation depletion by the sodium pump in red cells with pathologic cation leaks. Sickle cells and xerocytes. J Clin Invest. 1986 Dec; 78(6):1487-96.
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Becker PS, Cohen CM, Lux SE. The effect of mild diamide oxidation on the structure and function of human erythrocyte spectrin. J Biol Chem. 1986 Apr 05; 261(10):4620-8.
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Beaven GH, Jean-Baptiste L, Ungewickell E, Baines AJ, Shahbakhti F, Pinder JC, Lux SE, Gratzer WB. An examination of the soluble oligomeric complexes extracted from the red cell membrane and their relation to the membrane cytoskeleton. Eur J Cell Biol. 1985 Mar; 36(2):299-306.
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Becker PS, Lux SE. Hereditary spherocytosis and related disorders. Clin Haematol. 1985 Feb; 14(1):15-43.
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Platt OS, Falcone JF, Lux SE. Molecular defect in the sickle erythrocyte skeleton. Abnormal spectrin binding to sickle inside-our vesicles. J Clin Invest. 1985 Jan; 75(1):266-71.
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Becker PS, Lux SE. The effect of oxidation on the structure and function of human erythrocyte spectrin. Prog Clin Biol Res. 1985; 195:185-93.
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Beardsley DS, Spiegel JE, Jacobs MM, Handin RI, Lux SE. Platelet membrane glycoprotein IIIa contains target antigens that bind anti-platelet antibodies in immune thrombocytopenias. J Clin Invest. 1984 Nov; 74(5):1701-7.
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Shohet SB, Lux SE. The erythrocyte membrane skeleton: pathophysiology. Hosp Pract (Off Ed). 1984 Nov; 19(11):89-95, 99, 103 passim.
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Lux S, Shohet SB. The erythrocyte membrane skeleton: biochemistry. Hosp Pract (Off Ed). 1984 Oct; 19(10):77-83.
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Ohanian V, Wolfe LC, John KM, Pinder JC, Lux SE, Gratzer WB. Analysis of the ternary interaction of the red cell membrane skeletal proteins spectrin, actin, and 4.1. Biochemistry. 1984 Sep 11; 23(19):4416-20.
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Spiegel JE, Beardsley DS, Southwick FS, Lux SE. An analogue of the erythroid membrane skeletal protein 4.1 in nonerythroid cells. J Cell Biol. 1984 Sep; 99(3):886-93.
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Pinder JC, Dhermy D, Baines AJ, Lux SE, Gratzer WB. A phenomenological difference between membrane skeletal protein complexes isolated from normal and hereditary spherocytosis erythrocytes. Br J Haematol. 1983 Nov; 55(3):455-63.
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Palek J, Lux SE. Red cell membrane skeletal defects in hereditary and acquired hemolytic anemias. Semin Hematol. 1983 Jul; 20(3):189-224.
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Becker PS, Spiegel JE, Wolfe LC, Lux SE. High yield purification of protein 4.1 from human erythrocyte membranes. Anal Biochem. 1983 Jul 01; 132(1):195-201.
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Unger AE, Harris MJ, Bernstein SE, Falcone JC, Lux SE. Hemolytic anemia in the mouse. Report of a new mutation and clarification of its genetics. J Hered. 1983 Mar-Apr; 74(2):88-92.
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Wolfe LC, John KM, Falcone JC, Byrne AM, Lux SE. A genetic defect in the binding of protein 4.1 to spectrin in a kindred with hereditary spherocytosis. N Engl J Med. 1982 Nov 25; 307(22):1367-74.
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Mohandas N, Clark MR, Health BP, Rossi M, Wolfe LC, Lux SE, Shohet SB. A technique to detect reduced mechanical stability of red cell membranes: relevance to elliptocytic disorders. Blood. 1982 Apr; 59(4):768-74.
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Platt OS, Lux SE, Nathan DG. Exercise-induced hemolysis in xerocytosis. Erythrocyte dehydration and shear sensitivity. J Clin Invest. 1981 Sep; 68(3):631-8.
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Tomaselli MB, John KM, Lux SE. Elliptical erythrocyte membrane skeletons and heat-sensitive spectrin in hereditary elliptocytosis. Proc Natl Acad Sci U S A. 1981 Mar; 78(3):1911-5.
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Lux SE, Wolfe LC, Pease B, Tomaselli MB, John KM, Bernstein SE. Hemolytic anemias due to abnormalities in red cell spectrin: a brief review. Prog Clin Biol Res. 1981; 45:159-68.
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Harris HW, Lux SE. Structural characterization of the phosphorylation sites of human erythrocyte spectrin. J Biol Chem. 1980 Dec 10; 255(23):11512-20.
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Harris HW, Levin N, Lux SE. Comparison of the phosphorylation of human erythrocyte spectrin in the intact red cell and in various cell-free systems. J Biol Chem. 1980 Dec 10; 255(23):11521-5.
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Lux SE, Wolfe LC. Inherited disorders of the red cell membrane skeleton. Pediatr Clin North Am. 1980 May; 27(2):463-86.
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Lux SE. Dissecting the red cell membrane skeleton. Nature. 1979 Oct 11; 281(5731):426-9.
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Lux SE, Pease B, Tomaselli MB, John KM, Bernstein SE. Hemolytic anemias associated with deficient or dysfunctional spectrin. Prog Clin Biol Res. 1979; 30:463-9.
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Lux SE. Spectrin-actin membrane skeleton of normal and abnormal red blood cells. Semin Hematol. 1979 Jan; 16(1):21-51.
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Glader BE, Lux SE, Muller-Soyano A, Platt OS, Propper RD, Nathan DG. Energy reserve and cation composition of irreversibly sickled cells in vivo. Br J Haematol. 1978 Dec; 40(4):527-32.
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Wolfe LC, Lux SE. Membrane protein phosphorylation of intact normal and hereditary spherocytic erythrocytes. J Biol Chem. 1978 May 10; 253(9):3336-42.
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Lux SE, John KM, Ukena TE. Diminished spectrin extraction from ATP-depleted human erythrocytes. Evidence relating spectrin to changes in erythrocyte shape and deformability. J Clin Invest. 1978 Mar; 61(3):815-27.
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Lux SE, John KM. Isolation and partial characterization of a high molecular weight red cell membrane protein complex normally removed by the spleen. Blood. 1977 Oct; 50(4):625-41.
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Lux SE, John KM. Evidence that spectrin is a determinant of shape and deformability in the human erythrocyte. Prog Clin Biol Res. 1977; 17:481-91.
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Lux SE, John KM, Karnovsky MJ. Irreversible deformation of the spectrin-actin lattice in irreversibly sickled cells. J Clin Invest. 1976 Oct; 58(4):955-63.
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Jackson RL, Gotto AM, Lux SE, John KM, Fleischer S. Human plasma high density lipoprotein. Interaction of the cyanogen bromide fragments from apolipoprotein glutamine II (A-II) with phosphatidylcholine. J Biol Chem. 1973 Dec 25; 248(24):8449-56.
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Lux SE, John KM, Brewer HB. Isolation and characterization of apoLp-Gln-II (apoA-II), a plasma high density apolipoprotein containing two identical polypeptide chains. J Biol Chem. 1972 Dec 10; 247(23):7510-8.
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Lux SE, John KM, Ronan R, Brewer HB. Isolation and characterization of the tryptic and cyanogen bromide peptides of apoLp-Gln-II (apoA-II), plasma high density apolipoprotein. J Biol Chem. 1972 Dec 10; 247(23):7519-27.
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Lux SE, John KM, Fleischer S, Jackson RL, Gotto AM. Identification of the lipid-binding cyanogen bromide fragment from the cystine-containing high density apolipoprotein, APOLP-GLN-II. Biochem Biophys Res Commun. 1972 Oct 06; 49(1):23-9.
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Lux SE, Levy RI, Gotto AM, Fredrickson DS. Studies on the protein defect in Tangier disease. Isolation and characterization of an abnormal high density lipoprotein. J Clin Invest. 1972 Oct; 51(10):2505-19.
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Lux SE, John KM. Further characterization of the polymorphic forms of a human high density apolipoprotein, apoLP-Gln-I (apoA-I). Biochim Biophys Acta. 1972 Sep 29; 278(2):266-70.
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Brewer HB, Lux SE, Ronan R, John KM. Amino acid sequence of human apoLp-Gln-II (apoA-II), an apolipoprotein isolated from the high-density lipoprotein complex. Proc Natl Acad Sci U S A. 1972 May; 69(5):1304-8.
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Jacob HS, Lux SE. Degradation of membrane phospholipids and thiols in peroxide hemolysis: studies in vitamin E deficiency. Blood. 1968 Oct; 32(4):549-68.
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Research Departments:

Location

Boston Children's Hospital
300 Longwood Ave.
Boston MA, 02115
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