O uso de Sistema de Informações Geográficas no Mapeamento dos Casos de Dengue no Município de Araraquara (SP)

Rios, Leonardo; Teixeira, Denílson; Teodoro, Valter Luiz Iost; Costa, Daniel Jadyr Leite; Ortiz, Lucía

doi:10.25061/2527-2675/rebram/2007.v11i2.190

Cited by 2 publications

(2 citation statements)

References 6 publications

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“…The thermodynamic parameters at equilibrium estimated from SPR analysis have been consistent with those determined directly using isothermal titration calorimetry (18 -20). The parameters for the transition state of the interactions were calculated by the Eyring theory using the temperature dependence of association rate constant (k a ) or dissociation rate constant (k d ) as described under "Experimental Procedures" (21). The temperature dependence of K D , k a , and k d from SPR analysis fit well with the theoretical equations ( Fig.…”

Section: Functional Roles Of the Rh Domain And C-terminal Region In Rmentioning

confidence: 74%

Activation of Leukemia-associated RhoGEF by Gα13 with Significant Conformational Rearrangements in the Interface

Suzuki

Tsumoto

Hajicek

et al. 2009

Journal of Biological Chemistry

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The transient protein-protein interactions induced by guanine nucleotide-dependent conformational changes of G proteins play central roles in G protein-coupled receptor-mediated signaling systems. Leukemia-associated RhoGEF (LARG), a guanine nucleotide exchange factor for Rho, contains an RGS homology (RH) domain and Dbl homology/ pleckstrin homology (DH/PH) domains and acts both as a GTPase-activating protein (GAP) and an effector for G␣ 13 . However, the molecular mechanism of LARG activation upon G␣ 13 binding is not yet well understood. In this study, we analyzed the G␣ 13 -LARG interaction using cellular and biochemical methods, including a surface plasmon resonance (SPR) analysis. The results obtained using various LARG fragments demonstrated that active G␣ 13 interacts with LARG through the RH domain, DH/PH domains, and C-terminal region. However, an alanine substitution at the RH domain contact position in G␣ 13 resulted in a large decrease in affinity. Thermodynamic analysis revealed that binding of G␣ 13 proceeds with a large negative heat capacity change (⌬Cp°), accompanied by a positive entropy change (⌬S°). These results likely indicate that the binding of G␣ 13 with the RH domain triggers conformational rearrangements between G␣ 13 and LARG burying an exposed hydrophobic surface to create a large complementary interface, which facilitates complex formation through both GAP and effector interfaces, and activates the RhoGEF. We propose that LARG activation is regulated by an induced-fit mechanism through the GAP interface of G␣ 13 .Heterotrimeric G proteins 3 serve as key molecular switches to transduce a large array of extracellular signals into cells by actively alternating their conformations between GDP-bound inactive and GTP-bound active forms. In the current model, the ligand-activated G protein-coupled receptors (GPCRs) catalyze the exchange of GDP for GTP on G␣ subunits (1). Upon activation, three switch regions in the G␣ subunit undergo significant conformational changes, followed by dissociation of the GTP-bound G␣ subunit from the G␤␥ subunits. Both G␣-GTP and free G␤␥ interact with diverse downstream effectors to transmit intracellular signals. The G␣ subunit hydrolyzes bound GTP to GDP by its intrinsic GTPase activity. This deactivation process is further accelerated by GTPase-activating proteins (GAPs) such as regulator of G protein signaling (RGS) proteins (2, 3). G␣-GDP dissociates from effectors and re-associates with G␤␥ to terminate the signal.Although this model explains the basic concept of G protein signaling, the molecular dynamics of interactions among GPCR, G protein, RGS protein, and effector during the signaling process is not well understood. It has been suggested that the GPCR signals are integrated into the intracellular signaling network at the level of G proteins (4). Accumulating evidence suggests that the G␣ subunit acts as the core of the signaling complex at the membrane, which is formed through the transient protein-protein interactions of multiple signaling compo...

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Section: Functional Roles Of the Rh Domain And C-terminal Region In Rmentioning

confidence: 74%

Activation of Leukemia-associated RhoGEF by Gα13 with Significant Conformational Rearrangements in the Interface

Suzuki

Tsumoto

Hajicek

et al. 2009

Journal of Biological Chemistry

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“…3A) and equilibrium (Fig. 3B) analysis, were used to obtain thermodynamic parameters by plotting ln (K D ) versus 1/T [45,48].…”

Section: Thermodynamic Analysismentioning

confidence: 99%

Immobilization of His-tagged kinase JAK2 onto the surface of a plasmon resonance gold disc modified with different copper (II) complexes

Kurzątkowska¹,

Mielecki²,

Grzelak³

et al. 2014

Talanta

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New surface plasmon resonance (SPR) sensing platform swhich consists of copper (II) complexes of a pentetic acid thiol ligand (DPTA-Cu(II)) and of a thiol derivative of dipyrromethene (DPM-Cu(II) created on the surface of gold SPR disc were applied to oriented immobilization of His-tagged Janus kinase 2 (GST-His 6 -JAK2). This method is based on the covalent bond formation between histidine from a His-tag chain of a protein and Cu(II) centres from the complexes. The kinetic and thermodynamic parameters of the oriented immobilization of GST-His 6 -JAK2 protein to DPTA-Cu(II) and DPM-Cu(II) complexes attached to the Au surface of a SPR disc were discussed.

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O uso de Sistema de Informações Geográficas no Mapeamento dos Casos de Dengue no Município de Araraquara (SP)

Cited by 2 publications

References 6 publications

Activation of Leukemia-associated RhoGEF by Gα13 with Significant Conformational Rearrangements in the Interface

Activation of Leukemia-associated RhoGEF by Gα13 with Significant Conformational Rearrangements in the Interface

Immobilization of His-tagged kinase JAK2 onto the surface of a plasmon resonance gold disc modified with different copper (II) complexes

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