Search Results - "SORENSON, Martha M."

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    Myosin is reversibly inhibited by S-nitrosylation by Nogueira, Leonardo, Figueiredo-Freitas, Cicero, Casimiro-Lopes, Gustavo, Magdesian, Margaret H, Assreuy, Jamil, Sorenson, Martha M

    Published in Biochemical journal (01-12-2009)
    “…Nitric oxide (NO*) is synthesized in skeletal muscle and its production increases during contractile activity. Although myosin is the most abundant protein in…”
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    Betaine protects urea-induced denaturation of myosin subfragment-1 by Ortiz-Costa, Susana, Sorenson, Martha M, Sola-Penna, Mauro

    Published in The FEBS journal (01-07-2008)
    “…We have demonstrated previously that urea inhibits the activity and alters the tertiary structure of skeletal muscle myosin in a biphasic manner. This was…”
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    Brazilian Science and Research Integrity: Where are We? What Next? by Vasconcelos, Sonia M R, Sorenson, Martha M, Watanabe, Edson H, Foguel, Debora, Palácios, Marisa

    Published in Anais da Academia Brasileira de Ciências (01-06-2015)
    “…Building a world-class scientific community requires first-class ingredients at many different levels: funding, training, management, international…”
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    Modulation of troponin C affinity for the thin filament by different cross-bridge states in skinned skeletal muscle fibers by Pinto, José Renato, Veltri, Tiago, Sorenson, Martha M.

    Published in Pflügers Archiv (01-09-2008)
    “…In vertebrate skeletal muscle, the C-domain of troponin C (TnC) serves as an anchor; the N-domain regulates the position of troponin–tropomyosin on the thin…”
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    2,4-Dinitrophenol reduces the reactivity of Lys553 in the lower 50-kDa region of myosin subfragment 1 by Bomfim, Theresa R., Machado, Luciana E.S.F., Lima, Luis Mauricio T.R., Sorenson, Martha M., Salerno, Verônica P.

    “…► The compound 2,4-dinitrophenol (DNP) binds near a helix-loop-helix that includes a reactive lysine (Lys553) in myosin’s lower 50-kDa subdomain, activating…”
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    Discussing plagiarism in Latin American science: Brazilian researchers begin to address an ethical issue by Vasconcelos, Sonia, Leta, Jacqueline, Costa, Lídia, Pinto, André, Sorenson, Martha M

    Published in EMBO reports (01-07-2009)
    “…Most developed countries have extensive guidelines about research integrity, which reflects a global attempt to harmonize policies for handling research…”
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    Exogenous β-amyloid peptide interferes with GLUT4 localization in neurons by Oliveira, Leandro T, Leon, Gabbriela V.O, Provance, D. William, de Mello, Fernando G, Sorenson, Martha M, Salerno, Verônica P

    Published in Brain research (30-07-2015)
    “…Abstract Aging represents a major risk factor for numerous illnesses that are of increasing importance to society, including two of the most prevalent:…”
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    Redox state of Troponin C Cysteine in the D/E helix alters the C-domain affinity for the thin filament of vertebrate striated muscle by Pinto, José Renato, de Sousa, Valeria Pereira, Sorenson, Martha M

    Published in Biochimica et biophysica acta (01-04-2011)
    “…BACKGROUND: Despite a broad spectrum of structural studies, it is not yet clear whether the D/E helix of troponin C (TnC) contributes to the interaction of TnC…”
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    Redox balance and mitochondrial glycerol phosphate dehydrogenase activity in trained rats by Casimiro-Lopes, Gustavo, Ramos, Dionizio, Sorenson, Martha M., Salerno, Verônica P.

    Published in European journal of applied physiology (01-11-2012)
    “…Free radical production is increased in many disease states and during exercise, but in the latter the concurrent stimulation of the antioxidant defense system…”
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    Chemical treatment of mica for atomic force microscopy can affect biological sample conformation by Costa, Lilian T., Pinto, José R., Moraes, Marta B., de Souza, Guttierre G.B., Sorenson, Martha M., Bisch, Paulo M., Weissmüller, Gilberto

    Published in Biophysical chemistry (01-04-2004)
    “…An important aspect in the preparation of substrate materials to use in atomic force microscopy lies in the question of interactions introduced by treatments…”
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