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    • Plusieurs versions

    C-Terminus of Apolipoprotein A-I Removes Phospholipids from a Triolein/Phospholipids/Water Interface, but the N-Terminus Does Not: A Possible Mechanism for Nascent HDL Assembly

    Mitsche, Matthew a, Small, Donald m
    Biophysical Journal, 20 July 2011, Vol.101(2), pp.353-361 [Revue évaluée par les pairs]

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    A unified introduction to linear algebra : models, methods, and theory

    Tucker, Alan
    Small, Donald
    New York : Macmillan ; London : Collier Macmillan
    [1988]
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    Titre: A unified introduction to linear algebra : models, methods, and theory / Alan Tucker ; assisted by Donald Small
    Auteur: Tucker, Alan
    Contributeur: Small, Donald
    Editeur: New York : Macmillan ; London : Collier Macmillan
    Date: [1988]
    Collation: XIII, 540 p. ; 26 cm
    Classification: IMATH C-3
    Identifiant: 0024215805 (ISBN)
    No RERO: 1013750
    Permalien:
    http://data.rero.ch/01-1013750/html?view=FR_V1

    • Plusieurs versions

    Apolipoprotein C-I Binds More Strongly to Phospholipid/Triolein/Water than Triolein/Water Interfaces: A Possible Model for Inhibiting Cholesterol Ester Transfer Protein Activity and Triacylglycerol-Rich Lipoprotein Uptake

    Meyers, Nathan L, Wang, Libo, Small, Donald M
    Biochemistry, 14 February 2012, Vol.51(6), pp.1238-1248 [Revue évaluée par les pairs]

    • Plusieurs versions

    Adsorption of Egg Phosphatidylcholine to an Air/Water and Triolein/Water Bubble Interface: Use of the 2-Dimensional Phase Rule To Estimate the Surface Composition of a Phospholipid/Triolein/Water Surface as a Function of Surface Pressure

    Mitsche, Matthew A, Wang, Libo, Small, Donald M
    The Journal of Physical Chemistry B, 11 March 2010, Vol.114(9), pp.3276-3284 [Revue évaluée par les pairs]

    • Plusieurs versions

    Role of ABC transporters in secretion of cholesterol from liver into bile

    Small, Donald M
    Proceedings of the National Academy of Sciences of the United States of America, 07 January 2003, Vol.100(1), pp.4-6 [Revue évaluée par les pairs]

    • Plusieurs versions

    MicroRNA-16 Is Down-Regulated in Mutated FLT3 Expressing Murine Myeloid FDC-P1 Cells and Interacts with Pim-1 (MicroRNA-16 in Mutated FLT3 Expressing Mouse Cell)

    Kim, Kyu-Tae, Carroll, Adam P, Mashkani, Baratali, Cairns, Murray J, Small, Donald, Scott, Rodney J
    2012, Vol.7(9), p.e44546 [Revue évaluée par les pairs]

    • Plusieurs versions

    Interfacial Properties of Apolipoprotein B292−593 (B6.4−13) and B611−782 (B13−17). Insights into the Structure of the Lipovitellin Homology Region in Apolipoprotein B

    Wang, Libo, Jiang, Zhenghui Gordon, Mcknight, C. James, Small, Donald M
    Biochemistry, 11 May 2010, Vol.49(18), pp.3898-3907 [Revue évaluée par les pairs]

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    FLT3 in lineage specification and plasticity

    Greenblatt, Sarah, Small, Donald
    Oncotarget, May 2012, Vol.3(5), pp.576-80 [Revue évaluée par les pairs]
    MEDLINE/PubMed (U.S. National Library of Medicine)
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    Titre: FLT3 in lineage specification and plasticity
    Auteur: Greenblatt, Sarah; Small, Donald
    Sujet: Drug Therapy ; Leukemia -- Pathology ; Lymphocytes -- Pathology ; Myeloid Cells -- Pathology ; Fms-Like Tyrosine Kinase 3 -- Metabolism
    Description: FLT3 is a receptor tyrosine kinase that is expressed in CD34+ hematopoietic stem/ progenitor cells (HSPCs) and is important for both normal myeloid and lymphoid differentiation. FLT3 expression in Pax5 negative lymphoid precursors coincides with a window of multilineage differentiation potential in mice and humans. Recent work has shown that FLT3 activating mutations can collaborate with a Nup98-HoxD13 mutation to induce an aggressive acute leukemia. The leukemic initiating population in this model displayed properties of both lymphoid and myeloid precursors, making it a useful tool to study the role of FLT3 in lineage plasticity. Through a variety of assays, the leukemic initiating population was shown to be restricted to myeloid differentiation, suggesting that the B-lineage properties in these cells are due to the priming of lymphoid transcription programs in multipotent progenitors rather than a true capacity for B-cell maturation. The development of an undifferentiated myeloid leukemia...
    Fait partie de: Oncotarget, May 2012, Vol.3(5), pp.576-80
    Identifiant: 1949-2553 (E-ISSN); 22643831 Version (PMID)

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    Correlated miR-mRNA expression signatures of mouse hematopoietic stem and progenitor cell subsets predict "Stemness" and "Myeloid" interaction networks

    Heiser, Diane, Tan, Yee Sun, Kaplan, Ian, Godsey, Brian, Morisot, Sebastien, Cheng, Wen-Chih, Small, Donald, Civin, Curt I
    PloS one, 2014, Vol.9(4), pp.e94852 [Revue évaluée par les pairs]

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    Apolipoprotein B Is Conformationally Flexible but Anchored at a Triolein/Water Interface: A Possible Model for Lipoprotein Surfaces

    Wang, Libo, Walsh, Mary T., Small, Donald M.
    Proceedings of the National Academy of Sciences of the United States of America, 2 May 2006, Vol.103(18), pp.6871-6876 [Revue évaluée par les pairs]
    Archival Journals (JSTOR)
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    Titre: Apolipoprotein B Is Conformationally Flexible but Anchored at a Triolein/Water Interface: A Possible Model for Lipoprotein Surfaces
    Auteur: Wang, Libo; Walsh, Mary T.; Small, Donald M.
    Description: Apolipoprotein B (apoB) is one of a unique group of proteins that form and bind to fat droplets, stabilize the emulsified fat, and direct their metabolism. ApoB, secreted on lipoproteins (emulsions), remains bound during lipid metabolism yet exhibits conformational flexibility. It has amphipathic β-strand (AβS)-rich domains and amphipathic α-helix (AαH)-rich domains. We showed that two consensus AβS peptides of apoB bound strongly to hydrophobic interfaces [triolein/water (TO/W) and dodecane/ water], were elastic, and were not pushed off the interface when the surface was compressed. In contrast, an AαH peptide modeling helical parts of apoB was forced off the TO/W interface by compression and readsorbed when the interface was expanded. In this report, the surface behavior of apoB-100 was studied at the TO/W interface. Solubilized apoB lowered the interfacial tension of TO/W in a concentration-dependent fashion. At equilibrium tension, if the surface was compressed, part of apoB was pushed off but quickly readsorbed when the surface was expanded. Even when the surface area was compressed by ≈ 55%, part of the apoB molecule remained bound. The maximum surface pressure that apoB could withstand without being partially ejected was 13 mN/m. ApoB showed high elasticity at the TO/W interface. Based on studies of the consensus AβS and A±H peptides, we suggest that AβSs anchor apoB and are its nonexchangeable motif, whereas its conformational flexibility arises from both the elastic nature of the AP3S and the ability of A±H domains of the molecule to desorb and readsorb rapidly in response to surface pressure changes.
    Fait partie de: Proceedings of the National Academy of Sciences of the United States of America, 2 May 2006, Vol.103(18), pp.6871-6876
    Identifiant: 00278424 (ISSN); www.pnas.org/cgi/doi/10.1073/pnas.0602213103 (DOI)