The Experts below are selected from a list of 394518 Experts worldwide ranked by ideXlab platform

Emilia Chiancone - One of the best experts on this subject based on the ideXlab platform.

  • The sorcin–annexin VII calcium-Dependent Interaction requires the sorcin N-terminal domain
    FEBS Letters, 2000
    Co-Authors: Daniela Verzili, Carlotta Zamparelli, Benedetta Mattei, Angelika A. Noegel, Emilia Chiancone
    Abstract:

    Abstract Surface plasmon resonance experiments show that at neutral pH the stability of the complex between sorcin and annexin VII (synexin) increases dramatically between 3 and 6 μM calcium; at the latter cation concentration the KD value is 0.63 μM. In turn, the lack of complex formation between the sorcin Ca2+ binding domain (33–198) and synexin maps the annexin binding site to the N-terminal region of the sorcin polypeptide chain. Annexin VII likewise employs the N-terminal domain, more specifically the first 31 amino acids, to interact with sorcin [Brownawell, A.M. and Creutz, C.E. (1997) J. Biol. Chem. 272, 22182–22190]. The Interaction may involve similar structural motifs in the two proteins, namely GGYY and GYGG in sorcin and GYPP in synexin.

  • The sorcin-annexin VII calcium-Dependent Interaction requires the sorcin N-terminal domain.
    FEBS letters, 2000
    Co-Authors: Daniela Verzili, Carlotta Zamparelli, Benedetta Mattei, Angelika A. Noegel, Emilia Chiancone
    Abstract:

    Surface plasmon resonance experiments show that at neutral pH the stability of the complex between sorcin and annexin VII (synexin) increases dramatically between 3 and 6 microM calcium; at the latter cation concentration the K(D) value is 0.63 microM. In turn, the lack of complex formation between the sorcin Ca(2+) binding domain (33-198) and synexin maps the annexin binding site to the N-terminal region of the sorcin polypeptide chain. Annexin VII likewise employs the N-terminal domain, more specifically the first 31 amino acids, to interact with sorcin [Brownawell, A.M. and Creutz, C.E. (1997) J. Biol. Chem. 272, 22182-22190]. The Interaction may involve similar structural motifs in the two proteins, namely GGYY and GYGG in sorcin and GYPP in synexin.

D. Santos - One of the best experts on this subject based on the ideXlab platform.

  • Supersymmetric dark matter search via spin-Dependent Interaction with 3He
    Physics Letters B, 2005
    Co-Authors: E. Moulin, F. Mayet, D. Santos
    Abstract:

    The potentialities of MIMAC-He3, a MIcro-tpc MAtrix of Chambers of Helium 3, for supersymmetric dark matter search are discussed within the framework of effective MSSM models without gaugino mass unification at the GUT scale. A phenomenological study has been done to investigate the sensitivity of the MIMAC-He3 detector to neutralinos (m > 6 GeV/c2) via spin-Dependent Interaction with He3 as well as its complementarity to direct and indirect detection experiments. Comparison with other direct dark matter searches will be presented in a WIMP model-inDependent framework

  • Supersymmetric dark matter search via spin-Dependent Interaction with $^{3}He$
    Physics Letters B, 2005
    Co-Authors: E. Moulin, F. Mayet, D. Santos
    Abstract:

    The potentialities of MIMAC-He3, a MIcro-tpc MAtrix of Chambers of Helium 3, for supersymmetric dark matter search are discussed within the framework of effective MSSM models without gaugino mass unification at the GUT scale. A phenomenological study has been done to investigate the sensitivity of the MIMAC-He3 detector to neutralinos (m > 6 GeV/c2) via spin-Dependent Interaction with He3 as well as its complementarity to direct and indirect detection experiments. Comparison with other direct dark matter searches will be presented in a WIMP model-inDependent framework.

Daniela Verzili - One of the best experts on this subject based on the ideXlab platform.

  • The sorcin–annexin VII calcium-Dependent Interaction requires the sorcin N-terminal domain
    FEBS Letters, 2000
    Co-Authors: Daniela Verzili, Carlotta Zamparelli, Benedetta Mattei, Angelika A. Noegel, Emilia Chiancone
    Abstract:

    Abstract Surface plasmon resonance experiments show that at neutral pH the stability of the complex between sorcin and annexin VII (synexin) increases dramatically between 3 and 6 μM calcium; at the latter cation concentration the KD value is 0.63 μM. In turn, the lack of complex formation between the sorcin Ca2+ binding domain (33–198) and synexin maps the annexin binding site to the N-terminal region of the sorcin polypeptide chain. Annexin VII likewise employs the N-terminal domain, more specifically the first 31 amino acids, to interact with sorcin [Brownawell, A.M. and Creutz, C.E. (1997) J. Biol. Chem. 272, 22182–22190]. The Interaction may involve similar structural motifs in the two proteins, namely GGYY and GYGG in sorcin and GYPP in synexin.

  • The sorcin-annexin VII calcium-Dependent Interaction requires the sorcin N-terminal domain.
    FEBS letters, 2000
    Co-Authors: Daniela Verzili, Carlotta Zamparelli, Benedetta Mattei, Angelika A. Noegel, Emilia Chiancone
    Abstract:

    Surface plasmon resonance experiments show that at neutral pH the stability of the complex between sorcin and annexin VII (synexin) increases dramatically between 3 and 6 microM calcium; at the latter cation concentration the K(D) value is 0.63 microM. In turn, the lack of complex formation between the sorcin Ca(2+) binding domain (33-198) and synexin maps the annexin binding site to the N-terminal region of the sorcin polypeptide chain. Annexin VII likewise employs the N-terminal domain, more specifically the first 31 amino acids, to interact with sorcin [Brownawell, A.M. and Creutz, C.E. (1997) J. Biol. Chem. 272, 22182-22190]. The Interaction may involve similar structural motifs in the two proteins, namely GGYY and GYGG in sorcin and GYPP in synexin.

E. Moulin - One of the best experts on this subject based on the ideXlab platform.

  • Supersymmetric dark matter search via spin-Dependent Interaction with 3He
    Physics Letters B, 2005
    Co-Authors: E. Moulin, F. Mayet, D. Santos
    Abstract:

    The potentialities of MIMAC-He3, a MIcro-tpc MAtrix of Chambers of Helium 3, for supersymmetric dark matter search are discussed within the framework of effective MSSM models without gaugino mass unification at the GUT scale. A phenomenological study has been done to investigate the sensitivity of the MIMAC-He3 detector to neutralinos (m > 6 GeV/c2) via spin-Dependent Interaction with He3 as well as its complementarity to direct and indirect detection experiments. Comparison with other direct dark matter searches will be presented in a WIMP model-inDependent framework

  • Supersymmetric dark matter search via spin-Dependent Interaction with $^{3}He$
    Physics Letters B, 2005
    Co-Authors: E. Moulin, F. Mayet, D. Santos
    Abstract:

    The potentialities of MIMAC-He3, a MIcro-tpc MAtrix of Chambers of Helium 3, for supersymmetric dark matter search are discussed within the framework of effective MSSM models without gaugino mass unification at the GUT scale. A phenomenological study has been done to investigate the sensitivity of the MIMAC-He3 detector to neutralinos (m > 6 GeV/c2) via spin-Dependent Interaction with He3 as well as its complementarity to direct and indirect detection experiments. Comparison with other direct dark matter searches will be presented in a WIMP model-inDependent framework.

Angelika A. Noegel - One of the best experts on this subject based on the ideXlab platform.

  • The sorcin–annexin VII calcium-Dependent Interaction requires the sorcin N-terminal domain
    FEBS Letters, 2000
    Co-Authors: Daniela Verzili, Carlotta Zamparelli, Benedetta Mattei, Angelika A. Noegel, Emilia Chiancone
    Abstract:

    Abstract Surface plasmon resonance experiments show that at neutral pH the stability of the complex between sorcin and annexin VII (synexin) increases dramatically between 3 and 6 μM calcium; at the latter cation concentration the KD value is 0.63 μM. In turn, the lack of complex formation between the sorcin Ca2+ binding domain (33–198) and synexin maps the annexin binding site to the N-terminal region of the sorcin polypeptide chain. Annexin VII likewise employs the N-terminal domain, more specifically the first 31 amino acids, to interact with sorcin [Brownawell, A.M. and Creutz, C.E. (1997) J. Biol. Chem. 272, 22182–22190]. The Interaction may involve similar structural motifs in the two proteins, namely GGYY and GYGG in sorcin and GYPP in synexin.

  • The sorcin-annexin VII calcium-Dependent Interaction requires the sorcin N-terminal domain.
    FEBS letters, 2000
    Co-Authors: Daniela Verzili, Carlotta Zamparelli, Benedetta Mattei, Angelika A. Noegel, Emilia Chiancone
    Abstract:

    Surface plasmon resonance experiments show that at neutral pH the stability of the complex between sorcin and annexin VII (synexin) increases dramatically between 3 and 6 microM calcium; at the latter cation concentration the K(D) value is 0.63 microM. In turn, the lack of complex formation between the sorcin Ca(2+) binding domain (33-198) and synexin maps the annexin binding site to the N-terminal region of the sorcin polypeptide chain. Annexin VII likewise employs the N-terminal domain, more specifically the first 31 amino acids, to interact with sorcin [Brownawell, A.M. and Creutz, C.E. (1997) J. Biol. Chem. 272, 22182-22190]. The Interaction may involve similar structural motifs in the two proteins, namely GGYY and GYGG in sorcin and GYPP in synexin.