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  1. Article ; Online: Amyloid-beta Alzheimer targets - protein processing, lipid rafts, and amyloid-beta pores.

    Arbor, Sage C / LaFontaine, Mike / Cumbay, Medhane

    The Yale journal of biology and medicine

    2016  Volume 89, Issue 1, Page(s) 5–21

    Abstract: Amyloid beta (Aβ), the hallmark of Alzheimer's Disease (AD), now appears to be deleterious in its low number aggregate form as opposed to the macroscopic Aβ fibers historically seen postmortem. While Alzheimer targets, such as the tau protein, amyloid ... ...

    Abstract Amyloid beta (Aβ), the hallmark of Alzheimer's Disease (AD), now appears to be deleterious in its low number aggregate form as opposed to the macroscopic Aβ fibers historically seen postmortem. While Alzheimer targets, such as the tau protein, amyloid precursor protein (APP) processing, and immune system activation continue to be investigated, the recent discovery that amyloid beta aggregates at lipid rafts and likely forms neurotoxic pores has led to a new paradigm regarding why past therapeutics may have failed and how to design the next round of compounds for clinical trials. An atomic resolution understanding of Aβ aggregates, which appear to exist in multiple conformations, is most desirable for future therapeutic development. The investigative difficulties, structures of these small Aβ aggregates, and current therapeutics are summarized in this review.
    MeSH term(s) Alzheimer Disease/metabolism ; Amyloid beta-Peptides/chemistry ; Amyloid beta-Peptides/metabolism ; Amyloid beta-Protein Precursor/chemistry ; Amyloid beta-Protein Precursor/metabolism ; Animals ; Humans ; Membrane Microdomains/metabolism
    Chemical Substances Amyloid beta-Peptides ; Amyloid beta-Protein Precursor
    Language English
    Publishing date 2016-03-24
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 200515-3
    ISSN 1551-4056 ; 0044-0086
    ISSN (online) 1551-4056
    ISSN 0044-0086
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Teaching Biochemistry to Students of Dentistry, Medicine, and Pharmacy: 7th International Conference of the Association of Biochemistry Educators (ABE) Tucson, AZ, USA, May 5-9, 2019.

    Cline, Susan D / Simmons, Jana M / Niederhoffer, Eric C / Cruthirds, Danielle L / Arbor, Sage C / Franklin, David S / Abali, Emine E / Bateman, Robert C / Fontes, Joseph D / Lindsley, Janet E / Rubenstein, Peter A / Symes, Karen / Viselli, Susan M

    Medical science educator

    2019  Volume 30, Issue 1, Page(s) 585–589

    Language English
    Publishing date 2019-11-15
    Publishing country United States
    Document type Journal Article
    ISSN 2156-8650
    ISSN (online) 2156-8650
    DOI 10.1007/s40670-019-00851-w
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article: c[D-pro-Pro-D-pro-N-methyl-Ala] adopts a rigid conformation that serves as a scaffold to mimic reverse-turns.

    Arbor, Sage / Kao, Jeff / Wu, Yun / Marshall, Garland R

    Biopolymers

    2008  Volume 90, Issue 3, Page(s) 384–393

    Abstract: ... the flexibility of CTPs was determined computationally. Four analogs of cyclic tetraproline c[Pro-pro-Pro-pro ... with alternating L- and D-prolines, namely c[pro-Pro-pro-NMe-Ala], c[pip-Pro-pip-Pro], c[pro-Pip-pro-Pro], and c ... conformations for all four peptides examined. c[pro-Pro-pro-NMe-Ala] was shown to have a single all trans-amide ...

    Abstract Naturally occurring cyclic tetrapeptides (CTPs) such as tentoxin (Halloin et al., Plant Physiol 1970, 45, 310-314; Saad, Phytopathology 1970, 60, 415-418), ampicidin (Darkin-Rattray, Proc Natl Acad Sci USA 1996, 93, 13143-13147), HC-toxin (Walton, Proc Natl Acad Sci USA 1987, 84, 8444-8447), and trapoxin (Yoshida and Sugita, Jpn J Cancer Res 1992, 83, 324-328; Itazaki et al., J Antibiot (Tokyo) 1990, 43, 1524-1532) have a wide range of biological activity and potential use ranging from herbicides (Walton, Proc Natl Acad Sci USA 1987, 84, 8444-8447; Judson, J Agric Food Chem 1987, 35, 451-456) to therapeutics (Loiseau, Biopolymers 2003, 69, 363-385) for malaria (Darkin-Rattray, Proc Natl Acad Sci USA 1996, 93, 13143-13147) and cancer (Yoshida and Sugita, Jpn J Cancer Res 1992, 83, 324-328). To elucidate scaffolds that have few low-energy conformations and could serve as semirigid reverse-turn mimetics, the flexibility of CTPs was determined computationally. Four analogs of cyclic tetraproline c[Pro-pro-Pro-pro] with alternating L- and D-prolines, namely c[pro-Pro-pro-NMe-Ala], c[pip-Pro-pip-Pro], c[pro-Pip-pro-Pro], and c[Ala-Pro-pip-Pro] were synthesized and characterized by NOESY NMR. Both molecular mechanics and Density Functional Theory quantum calculations found these head-to-tail CTPs to be constrained to one or two relatively stable conformations. NMR structures, while not always yielding the same lowest energy conformation as expected by in silico predictions, confirmed only one or two highly populated solution conformations for all four peptides examined. c[pro-Pro-pro-NMe-Ala] was shown to have a single all trans-amide bond conformation from both in silico predictions and NMR characterization, and to be a reverse-turn mimetic by overlapping four Calpha-Cbeta bonds with those for approximately 6.5% (Tran, J Comput Aided Mol Des 2005, 19, 551-566) of reverse-turns in the Protein Data Bank PDB with a RMSD of 0.57 A.
    MeSH term(s) Amides/chemistry ; Amino Acids/chemistry ; Computational Biology ; Computer Simulation ; Models, Chemical ; Molecular Mimicry ; Monte Carlo Method ; Nuclear Magnetic Resonance, Biomolecular ; Peptides, Cyclic/chemical synthesis ; Peptides, Cyclic/chemistry ; Proline/chemistry ; Protein Conformation ; Protein Structure, Secondary ; Quantum Theory
    Chemical Substances Amides ; Amino Acids ; Peptides, Cyclic ; Proline (9DLQ4CIU6V)
    Language English
    Publishing date 2008
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 1123-x
    ISSN 1097-0282 ; 0006-3525
    ISSN (online) 1097-0282
    ISSN 0006-3525
    DOI 10.1002/bip.20869
    Database MEDical Literature Analysis and Retrieval System OnLINE

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