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NINDSNIMHNICHDNIDCDNEINIDCRNIANIAAANIDANHGRI NCCIHNIDDKNIEHSCCB

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Senior Investigator

Craig Blackstone, M.D., Ph.D.

Cell Biology Section

Porter Neuroscience Research Center
Building 35 Room 2C-913
35 Convent Drive MSC3704
Bethesda MD 20892-3704
Office: (301) 451-9680

Fax: (301) 480-4888
blackstc@ninds.nih.gov

Dr. Blackstone received B.S. and M.S. degrees in 1987 from the University of Chicago and M.D. and Ph.D. degrees in 1994 from Johns Hopkins University. His graduate studies, in the laboratory of Richard Huganir, were on the structure and regulation of glutamate receptors, for which he received the David Israel Macht Award. After a neurology residency at the Harvard-Longwood Neurology Program, Dr. Blackstone completed a fellowship in clinical movement disorders at the Massachusetts General Hospital. During this time he also conducted postdoctoral research with Morgan Sheng at Harvard Medical School, investigating the functions of proteins implicated in hereditary dystonias. Dr. Blackstone joined the NINDS as an investigator in 2001. His laboratory investigates the cellular and molecular mechanisms underlying hereditary movement disorders.



Our research group investigates cellular mechanisms underlying inherited neurological disorders, with an emphasis on neuromuscular and movement disorders. In particular, the pathogenesis of hereditary spastic paraplegias, which affect corticospinal motor axons in a length-dependent manner, is an area of very active interest. These disorders comprise well over 50 distinct genetic loci, with over 30 genes identified whose proteins segregate into a few common cellular themes. In addition to an active clinical program assessing new patients with these disorders, we investigate the functions of the disease gene products at the cellular level and in animal models. We have identified that the most common forms of inherited spastic paraplegia are due to mutations in genes encoding proteins with hydrophobic hairpin domains that help shape the distinct morphology of the tubular endoplasmic reticulum network. A number of these proteins as well as other spastic paraplegia proteins implicated in endocytic processes also act as inhibitors of bone morphogenetic protein signaling, providing an exciting translational line of investigation. Our current studies investigate both the disease pathogenic mechanisms as well as the more fundamental aspects of how organelles are shaped in cells, and why this is particularly important for neurons. The common pathogenic themes that are emerging will likely represent novel targets for therapeutic intervention.

Staff Image
  • Caroline Anderson, M.S.
    Graduate Student
    (301) 496-0284

  • Jaerak Chang, Ph.D.
    Postdoctoral Fellow
    (301) 451-9686

  • Do Kim, Ph.D.
    Postdoctoral Fellow

  • Seongju Lee, Ph.D.
    Postdoctoral Fellow
    (301) 451-9683

  • Brianna Malone, B.S.
    Postbaccalaureate IRTA

  • Benoit Renvoise, Ph.D.
    Postdoctoral Fellow
    (301) 451-9682

  • Ricardo Roda, M.D., Ph.D.
    Clinical Fellow

  • Julia Stadler, B.A.
    Research Assistant
    (301) 451-9685

  • Dr. Guohua Zhao, M.D.
    Visiting Fellow

  • Peng-Peng Zhu, M.D.
    Staff Scientist
    (301) 451-9687

  • 1) Landoure G, Zhu P-P, Lourenco CM, Johnson JO, Toro C, Bricceno KV, Rinaldi C, Meilleur KG, Sangare M, Diallo O, Pierson TM, Ishiura H, Tsuji S, Hein N, Fink JK, Stoll M, Nicholson G, Gonzalez M, Speziani F, Durr A, Stevanin G, Biesecker LG for the NIH Intramural Sequencing Center, Accardi J, Landis DMD, Gahl WA, Traynor BJ, Marques W Jr, Zuchner S, Blackstone C, Fischbeck KH, Burnett BG (2013)
  • Hereditary spastic paraplegia type 43 (SPG43) is caused by mutation in C19orf12
  • Hum Mutat, 34, 1357-1360
  • 2) Chang J, Lee S, Blackstone C (InPress) (2013)
  • Protrudin binds atlastins and endoplasmic reticulum-shaping proteins and regulates network formation
  • Proc Natl Acad Sci USA
  • 3) Donkervoort S, Dastgir J, Hu Y, Zein W, Marks H, Blackstone C, Bonnemann CG (InPress) (2013)
  • Phenotypic variability of a likely FA2H founder mutation in a family with complicated hereditary spastic paraplegia
  • Clin Genet
  • 4) Goyal U, Blackstone C (2013)
  • Untangling the web: mechanisms underlying ER network formation
  • Biochim Biophys Acta, 1833, 2492-2498
  • 5) Klemm RW, Norton JP, Cole RA, Li CS, Park SH, Crane MM, Li L, Jin D, Boye-Doe A, Liu TY, Shibata Y, Lu H, Rapoport TA, Farese RV Jr, Blackstone C, Guo Y, Mak HY (2013)
  • A conserved role for atlastin GTPases in regulating lipid droplet size
  • Cell Rep, 3, 1465-1475
  • 6) Anderson CA, Blackstone C (2013)
  • SUMO wrestling with Drp1 at mitochondria
  • EMBO J, 32, 1496-1498
  • 7) Gray JJ, Zommer AE, Bouchard RJ, Duval N, Blackstone C, Linseman DA (2013)
  • N-terminal cleavage of the mitochondrial fusion GTPase OPA1 occurs via a caspase-independent mechanism in cerebellar granule neurons exposed to oxidative or nitrosative stress
  • Brain Res, 1494, 28-43
  • 8) Chang J, Blackstone C (2013)
  • Rab10 joins the ER social network
  • Nat Cell Biol, 15, 135-136
  • 9) Pierson TM, Simeonov D, Sincan M, Adams DA, Markello T, Golas G, Fuentes-Fajardo K, Hansen NF, Cherukuri PF, Cruz P, Mullikin JC for the NISC Comparative Sequencing Program, Blackstone C, Tifft C, Boerkoel C, Gahl WA (2012)
  • Exome sequencing and SNP analysis detect novel compound heterozygosity in fatty acid hydroxylase-associated neurodegeneration
  • Eur J Hum Genet, 20, 476-479
  • 10) Renvoise B, Stadler J, Singh R, Bakowska JC, Blackstone C (2012)
  • Spg20-/- mice reveal multimodal functions for Troyer syndrome protein spartin in lipid droplet maintenance, cytokinesis, and BMP signaling
  • Hum Mol Genet, 21, 3604-3618
  • 11) Lee Seongju, Chang J, Renvoise B, Tipirneni A, Yang S, Blackstone C (2012)
  • MITD1 is recruited to midbodies by ESCRT-III and participates in cytokinesis
  • Mol Biol Cell, 23, 4347-4361
  • 12) Blackstone C, Murphy CT (2012)
  • Cell biology of disease and aging: a two-way street
  • Mol Biol Cell, 23, 975
  • 13) Blackstone C (2012)
  • Cellular pathways of hereditary spastic paraplegia
  • Annu Rev Neurosci, 35, 25-47
  • 14) Pierson TM, Adams D, Bonn F, Martinelli P, Cherukuri PF, Teer JK, Hansen NF, Cruz P, Mullikin JC for the NISC Comparative Sequencing Program, Blakesley RW, Golas G, Kwan J, Sandler A, Fajardo KF, Markello T, Tifft C, Blackstone C, Rugarli EI, Langer T, Gahl WA, Toro C (2011)
  • Whole-exome sequencing identifies homozygous AFG3L2 mutations in a spastic ataxia-neuropathy syndrome linked to mitochondrial m-AAA proteases
  • PLoS Genet, 7, e1002325
  • 15) Blackstone C, O'Kane CJ, Reid E (2011)
  • Hereditary spastic paraplegias: membrane traffic and the motor pathway
  • Nat Rev Neurosci, 12, 31-42
  • 16) Chang C-R, Manlandro CM, Arnoult D, Stadler J, Posey AE, Hill RB, Blackstone C (2010)
  • A lethal de novo mutation in the middle domain of the dynamin-related GTPase Drp1 inhibits higher-order assembly and mitochondrial division
  • J Biol Chem, 285, 32494-32503
  • 17) Soderblom C, Stadler J, Jupille H, Blackstone C, Shupliakov O, Hanna MC (2010)
  • Targeted disruption of the Mast syndrome gene SPG21 in mice impairs hind limb function and alters axon branching in cultured corticlal neurons
  • Neurogenetics, 11, 369-378
  • 18) Chang C-R, Blackstone C (2010)
  • Dynamic regulation of mitochondrial fission through modification of the dynamin-related protein Drp1
  • Ann NY Acad Sci, 1201, 34-39
  • 19) Renvoise B, Blackstone C (2010)
  • Emerging themes of ER organization in the development and maintenance of axons
  • Curr Opin Neurobiol, 20, 531-537
  • 20) Meilleur KG, Traore M, Sangare M, Britton A, Landoure G, Coulibaly S, Niare B, Mochel F, La Pean A, Rafferty I, Watts C, Shriner D, Littleton-Kearney MT, Blackstone C, Singleton A, Fischbeck KH (2010)
  • Hereditary spastic paraplegia and amyotrophy associated with a novel locus on chromosome 19
  • Neurogenetics, 11, 313-318
  • 21) Park SH, Zhu P-P, Parker RL, Blackstone C (2010)
  • Spastic paraplegia proteins REEP1, spastin, and atlastin-1 coordinate microtubule interactions with the tubular ER network
  • J Clin Invest, 120, 1097-1110
  • 22) Park SH, Blackstone C (2010)
  • Further assembly required: construction and dynamics of the endoplasmic reticulum network
  • EMBO Rep, 11, 515-521
  • 23) Renvoise B, Parker RL, Yang D, Bakowska JC, Hurley JH, Blackstone C (2010)
  • SPG20 protein spartin is recruited to midbodies by ESCRT-III protein Ist1 and participates in cytokinesis
  • Mol Biol Cell, 21, 3293-3303
  • 24) Hu J, Shibata Y, Zhu P-P, Voss C, Rismanchi N, Prinz WA, Rapoport TA, Blackstone C (2009)
  • A class of dynamin-like GTPases involved in the generation of the tubular ER network
  • Cell, 138, 549-561
  • 25) Figueroa-Romero C, Iniguez-Lluhi JA, Stadler J, Chang C-R, Arnoult D, Keller PJ, Hong Y, Blackstone C, Feldman EL (2009)
  • SUMOylation of the mitochondrial fission protein Drp1 occurs at mutliple non-consensus sites and is linked to its activity cycle
  • FASEB J, 23, 3917-3927
  • 26) Blackstone C (2009)
  • Infantile parkinsonism-dystonia: a dopamine 'transportopathy'
  • J Clin Invest, 119, 1455-1458
  • 27) Hanna M, Blackstone C (2009)
  • Interaction of the SPG21 protein ACP33/maspardin with the aldehyde dehydrogenase ALDH16A1
  • Neurogenetics, 10, 217-228
  • 28) Loucks FA, Schroeder EK, Zommer AE, Hilger S, Kelsey NA, Bouchard RJ, Blackstone C, Brewster JL, Linseman DA (2009)
  • Caspases indirectly regulate cleavage of the mitochondrial fusion GTPase OPA1 in neurons undergoing apoptosis
  • Brain Res, 1250, 63-74
  • 29) Rismanchi R, Puertollano R, Blackstone C (2009)
  • STAM Adaptor Proteins Interact with COPII Complexes and Function in ER-to-Golgi Trafficking
  • Traffic, 10, 201-217
  • 30) Yang D, Rismanchi N, Renvoise B, Lippincott-Schwartz J, Blackstone C, Hurley JH (2008)
  • Structural basis for midbody targeting of spastin by the ESCRT-III protein CHMP1B
  • Nat Struct Mol Biol, 15, 1278-1286
  • 31) Rismanchi N, Soderblom C, Stadler J, Zhu P-P, Blackstone C (2008)
  • Atlastin GTPases are required for Golgi apparatus and ER morphogenesis
  • Hum Molec Genet, 17, 1591-1604
  • 32) Guillery O, Malka F, Landes T, Guillou E, Blackstone C, Lombes A, Belenguer P, Arnoult D, Rojo M (2008)
  • Metalloprotease-mediated OPA1 processing is modulated by the mitochondrial membrane potential
  • Biol Cell, 100, 315-325
  • 33) Bakowska JC, Wang H, Xin B, Sumner CJ, Blackstone C (2008)
  • Loss of spartin protein in Troyer syndrome: a loss-of-function disease mechanism?
  • Arch Neurol, 65, 520-524
  • 34) Cereghetti GM, Stangherlin A, Martins de Brito O, Chang CR, Blackstone C, Bernardi P, Scorrano L (2008)
  • Dephosphorylation by calcineurin regulates translocation of Drp1 to mitochondria
  • Proc Natl Acad Sci USA, 105, 15803-15808
  • 35) Bakowska J, Jupille H, Fatheddin P, Puertollano R, Blackstone C (2007)
  • Troyer syndrome protein spartin is mono-ubiquitinated and functions in EGF receptor trafficking
  • Mol Biol Cell, 18, 1683-1692
  • 36) Papapetropoulos S, Friedman J, Blackstone C, Kleiner G, Bowen BC, Singer C (2007)
  • A progressive, fatal dystonia-parkinsonism syndrome in a patient with primary immunodeficiency receiving chronic IVIG therapy
  • Mov Disord, 22, 1664-1666
  • 37) Meijer IA, Dion P, Laurent S, Dupre N, Brais B, Levert A, Puymirat J, Rioux MF, Sylvain M, Zhu P-P, Soderblom C, Stadler J, Blackstone C, Rouleau GA (2007)
  • Characterization of a novel SPG3A deletion in a French-Canadian family
  • Ann Neurol, 61, 599-603
  • 38) Rismanchi N, Blackstone C (2007)
  • Mitochondrial function and dysfunction in the nervous system
  • Molecular Neurology (S. Waxman, ed.), 29-41
  • 39) Chang C-R, Blackstone C (2007)
  • Cyclic-AMP-dependent phosphorylation of Drp1 regulates its GTPase activity and mitochondrial morphology
  • J Biol Chem, 282, 21583-21587
  • 40) Chang C-R, Blackstone C (2007)
  • Drp1 phosphorylation and mitochondrial regulation
  • EMBO Rep, 8, 1088-1089
  • 41) Zhu P-P, Soderblom C, Tao-Cheng J-H, Stadler J, Blackstone C (2006)
  • SPG3A protein atlastin-1 is enriched in growth cones and promotes axon elongation during neuronal development
  • Hum Mol Genet, 15, 1343-1353
  • 42) Blindauer K and the Parkinson Study Group (C Blackstone) (2006)
  • A randomized control trial of etilevodopa in Parkinson's disease patients with motor fluctuations
  • Arch Neurol, 63, 210-216
  • 43) Soderblom C, Blackstone C (2006)
  • Traffic accidents: molecular genetic insights into the pathogenesis of the hereditary spastic paraplegias
  • Pharmacol Ther, 109, 42-56
  • 44) Arnoult D, Rismanchi N, Grodet A, Roberts RG, Seeburg DP, Estaquier J, Sheng M, Blackstone C (2005)
  • Bax/Bak-dependent release of DDP/TIMM8a promotes Drp1-mediated mitochondrial fission and mitoptosis during programmed cell death
  • Curr Biol, 15, 2112-2118
  • 45) Arnoult D, Grodet A, Lee Y-J, Estaquier J, Blackstone C (2005)
  • Release of OPA1 during apoptosis participates in the rapid and complete release of cytochrome c and subsequent mitochondrial fragmentation
  • J Biol Chem, 280, 35742-35750
  • 46) Bakowska JC, Jenkins R, Pendleton J, Blackstone C (2005)
  • The Troyer syndrome (SPG20) protein spartin interacts with Eps15
  • Biochem Biophys Res Commun, 334, 1042-1048
  • 47) Zhu P-P, Patterson A, Stadler J, Seeburg DP, Sheng M, Blackstone C (2004)
  • Intra- and intermolecular domain interactions of the C-terminal GTPase effector domain of the multimeric dynamin-like GTPase Drp1
  • J Biol Chem, 279, 35967-35974
  • 48) Zhu P-P, Patterson A, Lavoie B, Stadler J, Shoeb M, Patel R, Blackstone C (2003)
  • Cellular Localization, Oligomerization, and Membrane Association of the Hereditary Spastic Paraplegia 3A (SPG3A) Protein Atlastin
  • J Biol Chem, 278, 49063-49071
  • 49) Blackstone C, Roberts RG, Seeburg DP, Sheng M (2003)
  • Interaction of the deafness-dystonia protein DDP/TIMM8a with the signal transducing adaptor molecule STAM1
  • Biochem Biophys Res Comm, 305, 345-352
  • 50) Miller DW, Ahmad R, Hague S, Baptista MJ, Canet-Aviles R, McLendon C, Carter DM, Zhu P-P, Stadler J, Chandran J, Klinefelter GR, Blackstone C, Cookson MR (2003)
  • L166P mutant DJ-1, causative for recessive Parkinson's disease, is degraded through the ubiquitin-proteosome system
  • J Biol Chem, 278, 36588-36595
  • 51) Blackstone C, Sheng M (2002)
  • Postsynaptic calcium signaling microdomains in neurons
  • Front Biosci, 7, d872-d885
  • 52) Blackstone C, Sheng M (1999)
  • Protein targeting and calcium signaling microdomains in neuronal cells
  • Cell Calcium, 26, 181-192
  • 53) Martin LJ, Furuta A, Blackstone CD (1998)
  • AMPA receptor protein in developing rat brain: glutamate receptor-1 expression and localization change at regional, cellular, and subcellular levels with maturation
  • Neuroscience, 83, 917-928
  • 54) Wright DD, Blackstone CD, Huganir RL, Ryugo DK (1996)
  • Immunocytochemical localization of the mGluR1 metabotropic glutamate receptor in the dorsal cochlear nucleus
  • J Comp Neurol, 364, 729-745
  • 55) Blackstone CD, Huganir RL (1995)
  • Molecular structure of glutamate receptor channels
  • In: TW Stone, ed. CNS Neurotransmitters and Neuromodulators,, Vol. 1, 53-67
  • 56) Peng Y-W, Blackstone CD, Huganir RL, Yau K-W (1995)
  • Distribution of glutamate receptor subtypes in the vertebrate retina
  • Neuroscience, 66, 483-497
  • 57) Ginsberg SD, Price DL, Blackstone CD, Huganir RL, Martin LJ (1995)
  • The AMPA glutamate receptor GluR3 is enriched in oxytocinergic magnocellular neurons and is localized at synapses
  • Neuroscience, 65, 563-575
  • 58) Prince HK, Conn PJ, Blackstone CD, Huganir RL, Levey AI (1995)
  • Down-regulation of AMPA receptor subunit GluR2 in amygdaloid kindling
  • J Neurochem, 64, 462-465
  • 59) Ginsberg SD, Price DL, Blackstone CD, Huganir RL, Martin LJ (1995)
  • Non-NMDA glutamate receptors are present throughout the primate hypothalamus
  • J Comp Neurol, 353, 539-552
  • 60) Blackstone C, Murphy TH, Moss SJ, Baraban JM, Huganir RL (1994)
  • Cyclic AMP and synaptic activity-dependent phosphorylation of AMPA-preferring glutamate receptors
  • J Neurosci, 14, 7585-7593
  • 61) Krishek BJ, Xie X, Blackstone C, Huganir RL, Moss SJ, Smart TG (1994)
  • Regulation of GABA receptor function by protein kinase C phosphorylation
  • Neuron, 12, 1081-1095
  • 62) van den Pol A, Kogelman L, Ghosh P, Liljelund P, Blackstone C (1994)
  • Developmental regulation of the hypothalamic metabotropic glutamate receptor mGluR1
  • J Neurosci, 14, 3816-3834
  • 63) Hyman BT, Penney JB Jr, Blackstone CD, Young AB (1994)
  • Localization of non-N-methyl-D-aspartate glutamate receptors in normal and Alzheimer hippocampal formation
  • Ann Neurol, 35, 31-37
  • 64) Roche KW, Raymond LA, Blackstone C, Huganir RL (1994)
  • Transmembrane topology of the glutamate receptor subunit GluR6
  • J Biol Chem, 269, 11679-11682
  • 65) Paschen W, Blackstone CD, Huganir RL, Ross CA (1994)
  • Human GluR6 kainate receptor (GRIK2): molecular cloning, expression, polymorphism, and chromosomal assignment
  • Genomics, 20, 435-440
  • 66) Craig AM, Blackstone CD, Huganir RL, Banker G (1994)
  • Selective clustering of glutamate and gamma-aminobutyric acid receptors opposite terminals releasing the corresponding neurotransmitters
  • Proc Natl Acad Sci USA, 91, 12373-12377
  • 67) Raymond LA, Tingley WG, Blackstone CD, Roche KW, Huganir RL (1994)
  • Glutamate receptor modulation by protein phosphorylation
  • J Physiol (Paris), 88, 181-192
  • 68) Milani D, Candeo P, Favaron M, Blackstone CD, Manev H (1993)
  • A subpopulation of cerebellar granule cells in culture expresses a functional mGluR1 metabotropic glutamate receptor: effect of depolarizing growing conditions
  • Receptors and Channels, 1, 243-250
  • 69) Craig AM, Blackstone CD, Huganir RL, Banker G (1993)
  • The distribution of glutamate receptors in cultured rat hippocampal neurons: postsynaptic clustering of AMPA-selective subunits
  • Neuron, 10, 1055-1068
  • 70) Martin LJ, Blackstone CD, Levey AI, Huganir RL, Price DL (1993)
  • Cellular localizations of AMPA glutamate receptors within the basal forebrain magnocellular complex of rat and monkey
  • J Neurosci, 13, 2249-2263
  • 71) Martin LJ, Blackstone CD, Huganir RL, Price DL (1993)
  • The striatal mosaic in primates: striosomes and matrix are differentially enriched in ionotropic glutamate receptor subunits.
  • J Neurosci, 13, 782-792
  • 72) Martin LJ, Blackstone CD, Levey AI, Huganir RL, Price DL (1993)
  • AMPA glutamate receptor subunits are differentially distributed in rat brain
  • Neuroscience, 53, 327-358
  • 73) Raymond LA, Blackstone CD, Huganir RL (1993)
  • Phosphorylation of amino acid neurotransmitter receptors in synaptic plasticity
  • Trends Neurosci, 16, 147-153
  • 74) Raymond LA, Blackstone CD, Huganir RL (1993)
  • Phosphorylation and modulation of recombinant GluR6 glutamate receptors by cAMP-dependent protein kinase
  • Nature, 361, 637-641
  • 75) Moss SJ, Blackstone CD, Huganir RL (1993)
  • Phosphorylation of recombinant non-NMDA glutamate receptors on serine and tyrosine residues
  • Neurochem Res, 18, 105-110
  • 76) Moss SJ, Smart TG, Blackstone CD, Huganir RL (1992)
  • Functional modulation of GABA receptors by cAMP-dependent protein phosphorylation
  • Science, 257, 661-665
  • 77) Blackstone CD, Huganir RL (1992)
  • Glutamate receptor phosphorylation
  • Neuroscience Facts, 3, 2-3
  • 78) Martin LJ, Blackstone CD, Huganir RL, Price DL (1992)
  • Cellular localization of a phosphoinositide-linked metabotropic glutamate receptor in rat brain
  • Neuron, 9, 259-270
  • 79) Blackstone CD, Levey AI, Martin LJ, Price DL, Huganir RL (1992)
  • Immunological detection of glutamate receptor sybtypes in human central nervous system
  • Ann Neurol, 31, 680-683
  • 80) Blackstone CD, Moss SJ, Martin LJ, Levey AI, Price DL, Huganir RL (1992)
  • Biochemical characterization and localization of a non-N-methyl-D-aspartate glutamate receptor in rat brain
  • J Neurochem, 58, 1118-1126
  • 81) Blackstone CD, Raymond L, Moss SJ, Huganir RL (1992)
  • Regulation of non-NMDA gluatmate receptors by protein phosphorylation
  • In: Simon RP, ed. Fidia Research Foundation Symposium Series: Excitatory Amino Acids,, Vol. 9, 15-20
  • 82) Swope SL, Moss SJ, Blackstone CD, Huganir RL (1992)
  • Phosphorylation of ligand-gated ion channels: a possible mode of synaptic plasticity
  • FASEB J, 6, 2514-2523
  • 83) Blackstone CD, Supattapone S, Snyder SH (1989)
  • Phosphoinositide-linked glutamate receptors mediate cerebellar parallel fiber-Purkinje cell synaptic transmission
  • Proc Natl Acad Sci USA, 86, 4316-4320
  • 84) Seino S, Blackstone CD, Chan SJ, Whittaker J, Bell GI, Steiner DF (1988)
  • Appalachian spring: variations on ancient gastro-entero-pancreatic themes in New World mammals
  • Horm Metabol Res, 20, 430-435
  • 85) Blackstone CD, Seino S, Takeuchi T, Yamada T, Steiner DF (1988)
  • Novel organization and processing of the guinea pig pancreatic polypeptide precursor
  • J Biol Chem, 263, 2911-2916
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