<<< < te with G proteins. The N-terminal binding site of CSP, wte with G proteins. The N-terminal binding site of CSP, white with G proteins. The N-terminal binding site of CSPte with G proteins. The N-terminal binding site of CSP, wte with G proteins. The N-terminal binding site of CSP, wte with G proteins. The N-terminal binding site of CSP, white with G proteins. The N-terminal binding site of CSP, whicte with G proteins. The N-terminal binding site of CSP, which includes the J domain, binds G? subunits but not G?? subunits whereas the C termite with G proteins. The N-terminal binding site of CSP, which includes the J domain, binds G? subte with G proteins. The N-terminal binding site of CSP, which includes the J domain, bite with G proteins. The N-terminal binding site of CSP, which includes the J domain, binds G? subunits but not G?? subunits whereas tte with G proteins. The N-terminal binding site of CSP, which includes the J domain, binds G? subunits but not G?? subunits whereas the C terminal binding site of CSP associates with either free G?? subunits or G?? in complex with G?. The interaction of eitheding proteins (G proteins) and N-type calcium channels that results in a tonic G protein inhibition of the channels. In this report we directly demonstrate that two separate regions of CSP associate with G proteins. The N-terminal binding site of CSP, which includes the J domain, binds G? subunits but not G?? subunits whereas the C terminal binding site of CSP associates with either free G?? subunits or G?? in complex with G?. The interaction of either binding site of CSP (CSP1-82 or CSP83-198) with G proteins elicits robust tonic inhibition of N-type calcium channel activity. However, CSP1-82 inhibition and CSP83-198 inhibition of calcium channels occur through distinct mechanisms. Calcium channel inhibition by CSP83-198 (but not CSP1-82) is completely blocked by co-expression of the synaptic protein interaction site (synprint) of the N-type channel, indicating that CSP83-198 inhibition is dependent on a physical interaction with the calcium channel. These results suggest that distinct binding sites of CSP can play a role in modulating G protein function and G protein inhibition of calcium channels." /> ding proteins (G proteins) and N-type calcium channels that rding proteins (G proteins) and N-type calcium channels that ding proteins (G proteins) and N-type calcium channels thatding proteins (G proteins) and N-type calcium channels that results in a tonic G protein inhibition of the channels. In this repoding proteins (G proteins) and N-type calcium channels that results in a tonic G protein inhibition of the channels. In this report we directly demonstrate that two separate regions of CSP associate with G proteins. The N-terminal binding site of CSP, which includes the J domain, binds G? subunits but not G?? subunits whereas the C terminal binding site of CSP associates with either free G?? subunits or G?? in complex with G?. The interaction of either binding site of CSP (CSP1-82 or CSP83-198) with G proteins elicits robust tonic inhibition of N-type calcium channel activity. However, CSP1-82 inhibition and Cits whereas the C terminal binding site of CSP associates with either free G<sub>??</sub> subunits or G<sub>??</sub> in complex with G<sub>?</sub>. The interaction of either binding site of CSP (CSP<sub>1-82</sub> or CSP83-198) with G proteins elicits robust tonic inhibition of N-type calcium channel activity. However, CSP<sub>1-82</sub> inhibition and CSP83-198 inhibition of calcium channels occur through distinct mechanisms. Calcium channel inhibition by CSP83-198 (but not CSP<sub>1-82</sub>) is completely blocked by co-expression of the synaptic protein interaction site (synprint) of the N-type channel, indicating that CSP83-198 inhibition is dependent on a physical interaction with the calcium channel. These results suggest that distinct binding sites of CSP can play a role in modulating G protein function and G protein inhibition of calcium channels.</p>" /> its whereas the C terminal binding site of CSP associates with either freits whereas the C terminal binding site of CSP associates with either free its whereas the C terminal binding site of CSP associates with its whereas the C terminal binding site of CSP associates its whereas the C terminal binding site of CSP assits whereas the C terminal binding site of CSP associates with either free G<sub>??<its whereas the C terminal binding site of CSP associates with either free G<sub>??</sub> subuniits whereas the C terminal binding site of CSP associates with either free G<sub>??</sub>its whereas the C terminal binding site of CSP associates with either free G<sub>??</sub&its whereas the C terminal binding site of CSP assits whereas the C terminal binding site of CSP assits whereas the C terminal binding site of CSP associatesits whereas the C terminal binding site of CSP asits whereas the C terminal binding site of CSPits whereas the C terminal binding site of Cits whereas the C terminal binding site of CSP associaits whereas the C terminal n" content="Research Article" /> n" content="Research Article" /> citation_volume=322;citation_year=1997;citation_pmid=9148760;citation_doi=10.1042/bj3220853" /> rexpression Reveals a Role for Csp in Late Steps of Membrane Fusion in Dense-Core Granule Exocytosis in Adrenal Chromaffin Cells;citation_pages=1281-1289;citation_volume=20;citation_year=2000;citation_issue=4;citation_pmid=10662817" /> 2-1858;citation_volume=295;citation_year=2002;citation_issue=5561;citation_pmid=11884745;citation_doi=10.1126/science.1068408" /> tle=ATP dependence of the SNARE/caveolin 1 interaction in the hippocampus.;citation_pages=1232-1238;citation_volume=291;citation_year=2002;citation_issue=5;citation_pmid=11883949;citation_doi=10.1006/bbrc.2002.6603" /> v=Eur J Cell Biol;citation_title=Two distinct domains in hsc70 are essential for the interaction with the synaptic vesicle cysteine string protein.;citation_pages=375-381;citation_volume=78;citation_year=1999;citation_issue=6;citation_pmid=10430018;citation_doi=10.1016/S0171-9335(99)80079-X" /> ion_volume=277;citation_year=2002;citation_doi=10.1074/jbc.M111706200" /> iiiion_vion_volume=277;citation_year=2002;citation_doi=10.1074/jbc.M111706200" /> iiieeeexext/css" rel="stylesheet" href="//cdn.jsdelivr.net/qtip2/2.2.1/jquery.qtip.min.css" media="all" /> )))SSSSS ienceience_130g_0.png"},"highwire_ahah":{"highwire-inst-branding-0":"\/highwire\/inst_branding\/markup\/inst_loience_130gience_130g_0.png"},"highwire_ahah":{"highwire-inst-branding-0":"\/highwire\/inst_branding\/markup\/inst_logo","highwire-inst-branding-1":"\/highwire\/inst_branding\/markup\/inst_name_logo"},"nice_menus_options":{ience_130g_0.png"},"highwir-invisible element-f-invisibl-invisible elem-invisible element-focusable">Skip to main content
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  • an>
  • N-type-calcium channels
  • els" rel="nofollow">N-els" rel="nofollow">N-type-calcium channels
  • Synaptic transmission
  • a id="xref-ref-35-1" class="xra id="a id="xref-a id="xref-ref-35-1" class="xref-bibr" href="#ref-35">Zinsmaier and Bronk, 2001) (Zinsmaier and Bronk, 2001) (Chamberlain and Burgoyne, 2000).

    a id="xref-ref-35-a id="xref-ref-35-1" class="xref-bibr" href="#refa id="xref-ref-35-a id="xref-ref-35-1" class="xref-bibr" href="#ref-35">Zinsmaier and Bronk, 2001) (Chamberlain and Burgoyne, 2000).

    We have recently shown that CSP is capable of binding to both the N-type calcium channel and to Ga id="xref-ref-35-a id="xref-ref-35-1" class="xref-bibr" href="#ref-35">Zinsmaier and Bronk, 2001) (Zinsmaier and Bronk, 2001a id="xa id="xref-ref-35-1" class="xref-bibr" href="#ref-35">Zinsmaier and Bronk, 2001) (Chamberlain and Burgoyne, 2000).

    We have recently shown that CSP is capable of binding to both the N-type calcium channel and to G?? in vitro and that the interaction betweena id="a id="xref-ref-35-1" class="xref-bibr" href="#ref-35">Zinsmaier and Bronk, 2001) (Chamberlain and Burgoyne, 2000).

    We have ren the present study we have therefore analyzed the association of CSP with G proteins and N-type calcium channels.n the pren the n the present study we have therefore an the present study we han the presenn the present study we have therefore analyzn the present study we happocampal homogenateppocampal homoppocampal homogenate

    Rat hippocampi were hand homogenized with a teflon-coated homogenizer in 0.32 M sucrose, 10 mM HEPES KOH (pH 7.0), 1 mM EGTA, 0.1 mM EDTA, 0.5 mM PMSF, protease inhibitor cocktail (Boehringer Mannheim), 1 ?M microcystin, 1? M okadaic acid and 1 mM sodium orthovanadate (2 ml per hippocampus). The homogenate was ppocampappocappocappocampal homogenate

    Rat hippocampi were hand homogenized with a teflppocampappocappocappocampal homogenate

    Rat hippocampi were hand homogenized with a teflon-coated homogenizer in 0.32 M sucppocamppocampal ppocamppocampal homogenate

    Rat hippocampi were hand homogenized with a teflon-coated homogenizer in 0.32 M sucrose, 10 mM HEPES KOH (pH 7.0), 1 mM EGTA, 0.1 mM EDTA, 0.5 mM PMSF, protease inhibitor cocktail (Boehringer Mannheim), 1 ?M microcystin, 1? M okadappocampappocappocappocampal homogenate

    Rat hippocampi were hand homogenized with a teflon-coated homogenizer in 0.32 M sucrose, 10 mM HEPES KOH (pH 7.0), 1 mM EGTA, 0.1 mM EDTA, 0.5 mM PMSF, protease inhibitor cocktail (Boehringer Mannheim), 1 ?M microcystin, 1? M okadaic acid and 1 mM sodium orthovanadate (2 ml per hippocampus). The homogenate wppocampal hppocampal homppocampal homogenate

    Rat hippocampi were hand homogenized with a tefloppocampal homogenappocamppocampal homogenate

    Rat hippocampi were hand homogenized with ppocampal homogenateppocampal homogenate

    Rat hippocampi weppocamppocampappocampppocampal homogenate

    Rat hippocampi were hand homogenized with a teflon-coated homogenizd previously (d previously (Jarvis et al., 2000). The sequences of all constructs were verified by sequencing both strands using the dideoxynucleotide chain termination method. After induction of expression with 100 ?M isopropyl-?-D-thiogalactopyranside for 5 hours, the bad prevd previoud prevd previously (Jarvis et al., 2000). The sequences of all constructs were verified by sequencing both strands using the dideoxynucleotide chain termination method. After induction of expression with d previd previously (Jarvis et al., 2000). The sequences of all constructs were verified by sequencingd prevd previousd prevd previously (Jarvis et al., 2000). The sequences of all constructs were verified by sequencing both strands using the dideoxynucleotide cd prevd previously (Jarvid previd previously (Jarvis et al., 2000). The sequences of all constructs were verified by sequencing both strands using the dideoxynucleotide chain termination method. After inductid previousld previously d previously (Jarvis et al., 2000). The sequences of all constructs were verified by sequencing both strands using the dideoxynucleotide chain termination method. After induction of expression with 100 ?M isopropyl-?-D-thiogalactopyranside for 5 hours, the bacteria were suspended in phosphate buffer saline (PBS: 137 mM NaCl, 2.7 md prevd previoud prevd previously (Jarvis et with primary antibody. The membranes were washed three to four times in the above milk/Tween/PBS solution and incubated for 30 minutes with goat anti-rabbit or goat anti-mouse IgG-coupled horseradish peroxidase. Antigen was detected using chemiluminescent horseradish peroxidase substrate (ECL, Amersham). Immunoreactive bands were visualized following exposure of the membranes to Amersham Hyperfilm-MP.eroxidase seroxidase suberoxidase substrate (ECL, Amersham). Immunoreroxidase substrate (ECL, Amersham). Imeroxidase subseroxidase substrate (ECL, Amersham). Immunoreactive bands were visualieroxidaeroxidase substrate (ECL, Amersham). Immunoreactive bands were visualized following exposure of the membranes to Amersham Hyperfilm-MP.

  • eroxidase substrateroxidase substrate (ECL, Amersham). Immunoreactive bands were eroxidaseeroxidase seroxidase eroxidase subseroxidase seroxidase substrate (ECL, Amersham). Immunoreactive bands were visualizeeroxideroxidase substrate (ECL, Amersham). Immunoreactive bands were visualized following exposure of the membranes to Amersham Hyperfilm-MP.

    Transient transfection of HEK cells

    N-type calcium channel subunits, G protein subunits, the? 1B II-III linker (corresponding to residues 718-963) and the C-terminus of ?ARK (corresponding to residues 495-689) were prepared aeroxidaeroxidase substrate (ECL, Amersham). Immunoreactive bands were visualized followeroxidaeroxidase substrate (ECL, eroxidaeroxidase eroxideroxidase sueroxidaseroxidase substrate (ECL, eroxidaeroxidase substraeroxideroxidase substrateroxideroxidaseroxidaeroxidase substrate (ECL, Amersham). Immunoreactive bands were visualized following exposure eroxidaseeroxidase suberoxidase seroxidase substrate (ECL, Amersham). Immunoreactive bands were visualized following exposure of theroxidase seroxidase suberoxidase substrate (ECL, Amersham). Immunoreroxidase substrate (ECL, eroxidase subseroxidase substrate (ECL, Amersham). Immunoreactive bands were visualized follrred to a 3 cm culture dish containing recording solution comprised of 20 mM BaClrred trred to a 3 cm curred trred to a 3 cm culture dish containing recording solution comprised of 20 mM BaCl2, 1 mM MgCl2, 10 mM HEPES, 40 mM Tetraethylammonium chloride (TEA-Cl), 10 mM glucose and 65 mM CsCl, (pH 7.2 with TEA-OH). Whole cell patch clamp recordings were performed using an Axopatch 200B amplifier (Axon Instruments, Foster City, CA) linked to a personal computer equipped with pCLAMP v 6.0. Patch pipettes (Sutter borosilicate glass, BF150-86-15) were pulled using a Sutter P-87 microelectrode puller, fire polished using a Narashige microforgrred trred to a 3 cm culture dish containing recording solution comprised of 20 mM BaCl2, 1 mM MgCl2, 10 mM HEPES, 40 mM Tetraethylammonium chloride (TEA-Cl), 10 mM glucose and 65 mM CsCl, (pH 7.2 with TEA-OH). Whole cell patch clamp recordings were performed using an Axopatch 200B amplifier (Axon Instruments, Foster City, CA) linked to a personal computer equipped with pCLAMP v 6.0. Patch pipettes (Sutter borosilicate glass, BF150-86-15) were pulled using a Sutter P-87 microelectrode puller, fire polished using a Narashige microforge, and showed typical resistances of 3 to 4 M?. The internal pipette solution contained 108 mM CsMS, rred to arred to a 3 cm culture dish containing recording solution comprised of 20 mM BaCl2, 1 mM MgCl2, 10 mM HEPES, 40 mM Tetraethylammonium chloride (TEA-Cl), 10 mM glucose and 65 mM CsCl, (pH 7.2 with TEA-OH). Whole cell patch clamp recordings were performed using an Axopatch 200B amplifier (Axon Instruments, Foster City, CA) linked to a personal computer equipped with pCLAMP v 6.0. Patch pipettes (Sutter borosilicate glass, BF150-86-15) were pulled using a Sutter P-87 microelectrode puller, fire polished using a Narashige microforge,rred rred to a 3 cmrred to a 3rred to a 3rred trred to a 3 cm culture dish containing rred to a 3rred to a 3 rred to a 3 cm culture dish containing recor

    Binding properties of CSP and G proteins3>Binding prop3>Binding properties of CSP and G proteins

    Bind3>Binding properties of CSP and G proteins

    To establish if the interaction between CSP and G? is direct or indire2, including the J domain) coupled to glutathione agarose beads were used in an in vitro binding assay. The beads were incubated with hippocampal homogenate or purified G2, inclu2, including the J domain) coupled to glutathione agarose beads were2, inc2, including the J domain) coupled to glutathione agar2, inc2, including the J domain) c2, inc2, including the 2, inc2, including the J domain) coupled to glutathione ag2, inclu2, including the J domain) coupled to glutathione agarose beads were used in an in vitro binding assay. The beads were incubat2, including the J2, inclu2, inc2, including the J domain) coupled to glutathione agarose beads were used in an in vitro binding assay. The beads w2, inc2, including the J domain) coupled to glutathion2, inc2, including the J domain) coupled to glutathione agarose beads were used in a2, inc2, including the J domain) c2, inc2, including the J domain)2, inclu2, including the J domain) coupled to glutathione agarose beads were used in an in vitro binding assay. The beads were incubated with hippocampal homo2, inc2, including the J domain)2, inclu2, including the J domain) coupled to glutathione agarose beads were used in an in vitro binding assay. The beads were incubated with hippoc2, inc2, including the J 2, including 2, including the J domain) couple2, i2, including the J domain) coupled to g2, including the J domain) co2, including the J domain) coupled t2, including the J domain) c buffer, fractionated by SDS-PAG  Fig. 1.  buffer, f  Fig. 1.  buffer, fr buffer buf buffe buffe buffer, fractionated by SDS-PAGE and sub buffer, fractionated by SDS-PA buffer, fracti buf buff buffer, fractionate buffer, fracti buf buff

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  • Fig. 2.

    Nucleotide dependency of G protein interaction with recombinant CSP and J domain. Immunoblot analysis showing binding of G?, G? and Hsc70 to J-domain-GST fusion protein immobilized on agarose. Fusion proteins were incubated in the absence (-) or presence of rat h556788556788" class="highwire-f556788556788" class="highwire-figure-link highwire-figure-link-556788556788" class="highwire-figure-link highwire-figure-link-ppt" data-icon-position="" data-hide-lin556788556788" class="highwire-figure-link highwire-figure-link-ppt" data-icon-position="" data-hide-link-title="0">Download556788" class="hi556788" class="highwire-figure-lin556788556788556788" class="556788" class="highwire-figure-link highwire-figure-link-ppt" data-icon-position="" data-hide-link-title="0">Download powerpoint

    Fig. 2.

    Nucleotide dependency of G protein inte556788556788" class="hi556788556788" clas556788556788" class="highwire-figure-link highwire-figure-link-ppt" data-icon-position="" data-hide-link-title="0">556788556788" clas556788556788" class="highwire-figure-link higexamined (in the absence of ATP). Note that at a pH of 3.0 or 10 the recombinant fusion proteins only partially remained immobilized to the agarose beads. The G-protein-CSP complex was detected over the full pH range examined. These observations emphasize that the nucleotide-independent direct interaction between CSP and G proteins is a very stable complex.examined (in examined (in the absence of ATP).examexamined (in the absence of ATP). Note examined (in the absence of Aexamined (in the absence of ATP). Noexamined (in the absence of -Gα polyclonal (Calbiochem  Fig. 3.  -Gα   Fig. 3.  -Gα p-G;-G&#-G-G-Gα polyclonal (Calbiochem). These -Gα polyclonal (Calbioche-Gα polyc-G&#-G&#x-Gα polyclonal-Gα polyc-G&#-G&#x-Gα polyclonal (Calbioch-Gα polyclona-G&#-G&#x-G&#x-G-Gα polyclonal (Cal-Gα polyclonal (Calbiochem). Thes-Gα polyc-Gα polyclonal (-Gα polyclonal (C-Gα polyclonal (Calbiochem). These results are representative of five experiments. Gβ binding to CSP is very s-G-Gα po-G-Gα polyclonal (Calbiochem). These results are representative of five experiments. Gβ binding to CSP is very stable over a broad pH range. In contrast, Gβ does not bind to the J domain under any of the conditions examined.</div>" data-i SDS-PAGE and subjected to western blot analysis. The nitrocellulose membrane was probed with anti-G SDS-P SDS-PAGE and subjected to w SDS-P SDS-PAGE and subjected to western blot analysis. The nitrocellulose membrane was probe SDS-P SDS-PAGE and subjected to western blot analysis. The nitrocellulose membr SDS-P SDS-PAGE and subjected to western blot analysis. The nitrocellulose membr SDS-PAGE and sub SDS-PAGE and subjected to western SDS-P SDS-P SDS-PAGE and SDS-PAGE and SDS-PAGE and subjected to western blot analy SDS-PAGE and subjected to G proteins and N-type calcium channels G proteins an G proteins and N-type calcium channels

    To begin to understand the structural requirements for CSP association with G proteins, a series of CSP deleti G pro G proteins and N-type calcium channels

    To begin to understand the structural requirements for CSP association with G prot G proteins and N-type calcium channels

    To begin to understand the structural requirements for CSP association with G proteins, a series of CSP deletion mutants were constructed, expressed and purified (Fig. 4). The regions of CSP required for interaction with G proteins were determined t G proteins and N- G proteins and N-type calcium channels

    To begin to understand the structural requirements for CSP association with G proteins, a series of CSP deletion mutants were constructed, expressed and purified (Fig. 4). The regions of CSP required for interaction with G proteins were determined through binding experiments with the CSP deletion mutants.

    To begin to understand the s G pro G proteins and N-type ca G pro G proteins and N-type calcium channels

    To begin to underst G pro G proteins and N-type calcium channels

    To begin to understand the structural requirements for CSP association with G proteins, a series of CSP deletion mutants were constructed, expressed and G proteins a G proteins and N-type calcium ch G p G proteins and N-type calcium channels G proteins and N-te-figure">e-figure">

    Fig. 7. org/coorg/content/joces/116/14/2967/F7.large.jpg" class="highwire-figure-link highwire-figure-link-newtab" target="_blank" data-icon-position="" data-hide-link-title="0">Open in new tab
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  • Magga et al., 2000). It is conceivable that the remaining modulation was mediated by the interaction of the J domain with G?.

    The identistically significisticaistically significisticaistically significant portion isticaistically significistically significant portion of the G protein effect intact (Magga et al., 2000).istically significanistically significant portion of the G protein effect intact (istically significanistically significant portion of the G protein effect intact (Magga et al., 2000). It is conceivable that the remaining modulation was mediated by the interaction of the J domain with G?.

    The identification of specific Hscistically sistically significant portion of the G protein effect intact (tion of calcium trtion of calcium transmembrane fluxtion of calcium trtion of calcium transmembrantion of calcium ttion otion of calcium trantion otion of calciumtion otion of calcium trtion of calcium transmembrane fluxes (Brotion of calcium tion otion of calcium trtion otion of calciumtion of calcium transmed synaptobrevin) (ed synaptobrevin) (ed synaptobrevin) (ed synaptobrevin) (ed synaptobrevin) ed synaptobrevin) (Leveque et al., 1998), synaptotagmin I (Evans and Morgan, 2002), ?GDI (Leveque et al., 1998), synaptotagmin I (Evans ed synapted syned synaptobrevin) (nnd Snd Stroke Foundation of nd Stroke Foundation of Canada.

  • nd Stroke Foundation nd Stnd Stnd Stroke Foundation of Canada.
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  • li>lli>strong>Brown,strong>strostrongstrong>Brown, H., Larsson, O., Branstrom, R.strong>strong>strostrongstrong>Brown,stronstrostrong>Brown, H., Larsson, O., Branstromstrong>sstrong>Brown,strong>Brown, H., Larsson, O., Branstrom, R., Yang, S., Leibiger, B., Leibiger, I., Fristrong>Brown, H., Larsson,strongstrong>Brown, H., Larsson, O., Branstrom, R., strong>Browstrong>Brown, H., La-date">1997-date">1997). Activation of the ATPase activity of heat-shock proteins Hsc70/Hsp70 by cysteine-strin-date">1997). Activation of t-date">1-date">1997). Acti-date">1-date">1997). Activa-date">1997-date"-date">1997). Ac-date">1997-dat-date"-date">1997). Activation of the ATPas-date">-date">1997). Activation of the ATPase activit-date">-date">1997). Activation of th-date">1997). Activation of-date">1997-date">-dat-date"-date">19971997). Activation of the A-date">--date">19971997). Activation of the ATPase activity of heat-shock proteins Hsc70/Hsp70 -date">1997). Activ-date"-date">1997). Activation of the ATPase -date">1997-date">1997). Activation-date">1997). Activation of the ATPase activity of heat-shock proteins -date">1997). Activation of the AT-date">1-date">1997). Ac-date">1-date">1997). Activat-date">1997-date"-date">1997). Acprinkles-openprinkleprinprinkles-openuprinkleprinprinklprinkles-openprinkprinprinkles-openurl cit-ref-sprinkles-open-prinklepprinkles-openprinkles-openurl cit-ref-sprinkles-open-url">OpenUrlOpenUrlprinkles-openurl cit-ref-sprinkles-opeprinklesprinkles-openurl cit-refprinklesprinkles-openurl cit-ref-sprprinkles-openuprinkleprinklprinkles-openurl cit-reprinkles-openprinkleprinprinkles-openuprinkleprinprinkles-opeprinkleprin1&link_type=ISI"1&l1&am1&1&link_ty1&1&am1&link_type=ISI" class="cit-ref-spri1&l11&link_ty1&link_type=ISI" class="cit-ref-sprinkles cit-ref-sprinkles-newisilink cit-ref-sprinkles-webof1&link_type=ISI" class1&1&link_type=ISI" class="cit-ref-sprinkles cit-ref-sprinkles-newisilink cit-ref-spr1&link_1&link_type=ISI" class="cit1&link_type=ISI" class="cit-ref-sprinkles cit-ref-sprinkles-newisilink cit-re1&link_type=ISI" class="cit-ref-1&li1&link_type=ISI" clas1&li1&link_type=ISI" class=1&link_ty1&l1&1&link_type=ISI" cl1&link_ty1&l1&am1&link_typ1&l1&am1&link_t1&l1&am1&link_type=ISI"1&l1&am1&1&link_ty1&1&am1&link_type=ISI" class="cit-ref-spri1&l11&link_ty1&link_type=ISI" class="cit-r" id="cit-116.14.2967.9" data-doi="10.1161/01.RES.83.1.103">r" id="cit-116.14.2967.9" r" id=r" id="cit-116.14.2967.9" data-doi="10.1161/01.RES.83.1.103">
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  • Abstractcit-refcit-reflinks-abstract">AbstractAbstractAbstractAbstract class="rev-x class="rev-xref-ref" href="#xref-ref-14-1" title="View reference in text" id="ref-14">? class="rev-xref-ref" href class class="rev-xref-ref" href="#xref-re class="rev class="rev-xref-ref" href="#xr class="rev-xref-ref" href="#xref-ref-14-1" class="rev-xref-ref class="rev-xref-ref" href="#xref-ref-14-1" title="View reference in text" id="ref-14">? b of Scbb of Science
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