<<< < <<< tent="Cysteine string proteins (CSPs) are secretory vesictent="Cysteine string proteins (CSPs) are secretory vesicletent="Cysteine string proteins (CSPs) are secretory vetent="Cysteine string proteins (CSPs) are secretory vesictent="Cysteine string proteins (CSPs) are secretory vesictent="Cysteine string proteins (CSPs) are secretory vesicletent="Cysteine string proteins (CSPs) are secretory vesicle tent="Cysteine string proteins (CSPs) are secretory vesicle chaperones that are important for neurotransmitter release. We tent="Cysteine string proteins (CSPs) are secretory vesicle chaperones that aretent="Cysteine string proteins (CSPs) are secretory vesicle chatent="Cysteine string proteins (CSPs) are secretory vesi/sites/default/files/highwire/joces/116/14.cover.gif" /> /sites/default/files/highwire/joces/116/14.cover.gif" /> hibition of the channels. In this report we directly demonstrate that twohibition of the channels. In this report we directly demonstrate that two shibition of the channels. In this report we directly demonstrathibition of the channels. In this report we directly demonhibition of the channels. In this report we directhibition of the channels. In this report we directly demonstrate that two separate regions ohibition of the channels. In this report we directly demonstrate that two separate regions of CSP associate hibition of the channels. In this report we directly demonstrate that two separate regions of CSP ashibition of the channels. In this report we directly demonstrate that two separate regions of CSP associhibition of the channels. In this report we directhibition of the channels. In this report we direct < < < ory granule-associated protein regulating beta -cell exocytosis;citation_pages=5048-5058;citation_volume=17;citation_year=1998;citation_issue=17;citation_pmid=97246ory granule-associated protein regulating beta -cell exocytosis;citation_pages=5048-5058;citation_volume=17;citation_year=1998;citation_issue=17;citation_pmid=9724640;cory granule-associated protein regulating beta -cell exocytosis;citation_pages=5048-5058;citation_volume=17;citation_year=1998;citation_issue=17;citation_pmid=9724640;citation_doi=10.1093/emboj/17.17.5048" /> tion_issue=Pt 2;citation_pmid=11931641;citation_doi=10.1042/BJ20020123" /> ion_issue=3;citation_pmid=1326297;citation_doi=10.1016/0896-6273(92)90190-O" /> ;citation_year=2000;citation_issue=1;citation_pmid=11086994;citation_doi=10.1016/S0896-6273(00)00096-9" /> calcium channels.;citation_pages=1303-1313;citation_volume=13;citation_year=1994;citation_issue=6;citation_pmid=7993624;citation_doi=10.1016/0896-6273(94)90417-0" /> citation_title=Mutational analysis of cysteine-string protein function in insulin eume=277;citation_year=2002;citation_doi=10.1074/jbc.M111706200" /> ume=277;citation_year=2002;citation_doi=10.1074/jbc.M111706200" /> uuuuumume=277;citation_year=2002;citation_doi=10.1074/jbc.M111706200" /> llJlJr3PIJEvw3qLXc1cnYiLj2G4KgDPSXFOfm6Phf8hw__JdWGm15cDWjsK6KrFlQVXQix9YgNeYysf22XZHj-Y-c__i2IoKlTxCd8V23flRGAZBKbv_tVtd3FeaJyFtfvDlAw.css" media="all" /> ,,------ bblock-panels-mini-home-page-top-banner-add odd block-without-title" id="block-panels-minblock-pblblock-pablock-panblock-panels-block-panblock-pblock-pblock-pblock-panelblock-panblock-pblock-pablock-pblock-pablock-pblock-panelblock-panels-mini-home-page-top-banner-add odd block-without-title" id="block-panels-mini container-30"> container-30">
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    Journal of Cell Scienceogistsogists.org/siogists.ogists.orogists.ogists.org/ogists.orogists.ogists.oogists.ogists.oogists.ogists.org/sites/default/files/CoB_CellScience_130g.png" alt="Journal of Cell Science" title="ogists.org/sites/default/files/CoB_CellScience_130g.png" alt="Journal of Cell Science" title="Journal of Cell Science" /> ogists.org/sites/default/files/CoB_CellScience_130g.png" alt="Journal of Cell Science" title="Journal ogists.org/sites/default/files/CoB_CellScience_130g.pngogists.org/sites/default/files/CoB_CellScience_130g.png" alt="Journal of Cell Science" title="Journogists.org/sites/default/files/CoB_CellScience_130g.png"ogists.org/sites/default/files/CoB_Ceogisogists.orogists.ogistsogists.org/sites/default/files/CoB_CellScience_130g.png" alt="Journal of Cell Science" title="Journal of Cell Scienogists.org/sites/default/files/CoB_CellScience_130g.png"ogists.org/sites/default/files/CoB_CellScience_130g.png"ogists.org/sites/default/ogists.org/sites/default/files/CoB_CellScience_130g.png" alt="Journal of Cell Science" titogists.org/sites/default/files/CoB_CellScience_130g.png" alt="Journal of Cell Science" togiogisogists.org/sitesogists.org/sites/default/files/CoB_CellScience_130g.png" alt="Journal of Cell Sciencogists.org/sites/default/files/ogisogistsogists.org/sites/default/files/CoB_CellScience_130g.png" alt="Journal oogists.org/ogisogistsogists.org/sites/default/files/CoB_CellScience_130g.png" alt="Journal http://jcs.biologists.orhttphttp:/http://jcs.biologists.org" data-hide-link-title="0" target="_blank" clahttp://jcs.biologists.org" data-httphttp:/http://jcs.biologists.org" data-hide-link-title="0" target="_blank" clhttp://jcs.biologists.org" data-httphttp:/http://jcs.biologists.org" data-hide-link-title="0" target="_blank" class="http://jcs.bhttphttp:/http:http:/http:http://jcs.http://jchttp://http://jhttp://http:/http://jcs.biologists.org" data-hide-link-title="0" target="_blank" class="" data-icon-position="">Journhttp://jcs.biologists.org" data-hide-link-title="0" targhttp://jcs.biologists.org" data-hide-link-title="0" target="_blank" class="" data-icon-position="">Journal of Cell Science
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    ?? subsite of Csite of CSP associates with either free G?? subunits or G?? in complex with G?. The site of Csite of CSP associates with either free G?? subunits or G?? in complex with G?. The interaction of either binding sitsite of Csite 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 site of Csite osite of CSP associates witsite of CSP assosite of CSP associates sitesite site of CSP assosite of CSsitesite site of CSP assosite of CSsitesite site of CSP assosite of CSP associates sitesite site of CSP assosite of CSP associatesitesite site of CSP assotle%3AJ%tle%tle%3tle%3tle%3AJ%2Bdomain%20text_abstract_title_tle%3AJ%2Bdomaintle%3AJ%2Bdotle%3AJ%2Bdomain%20text_abstract_title_flags%3Amatch-phrase%20sort%3Apublication-date" class="hw-term hw-article-keyword hw-article-keywordtle%3AJ%2Bdomatle%3AJ%2Bdomain%20text_abstract_title_flags%3Amatch-phrase%20sort%tle%3AJ%2Bdomain%20textle%3AJ%2Bdomain%20text_abstract_title_flags%3Amatch-phrase%20sort%3Apublication-date" class="hw-term hw-article-keyword hw-article-keyword-j-domain" rel="nofollow">J domain

    Introduction

    CSPs (cysteine string proteins) are secretory vesicle chaperone proteins that are evolutionarily tle%3AJ%2Bdomain%20tle%3Atle%3AJ%2Bdomain%20tle%3AJ%2Bdomain%20text_abstract_title_flags%3Amatch-phrase%20sort%3Apublication-date" class="hw-term hw-article-keyword hw-article-keyword-j-domain" rel="nofollow">J domain

    Introduction

    CSPs (cysteine string proteins) are secretory vesicle chaperone proteins that are evolutionarily conserved. Deletion of CSP in Drosophila is semi-lethal; only 4% of the flies develop into adulthood (Zinsmaier et al., 1994). Adult survtle%3AJtle%3AJ%2Bdomain%20text_abstle%3AJ%2Bdomain%20text_atle%3AJtle%3AJ%2Bdomain%20text_abstratle%3Atle%3AJ%2Bdtle%3AJ%2Bdomain%20text_abstract_title_flags%3Amatch-phrase%20sort%3Apublication-date" class="hw-term hw-artitle%3AJtle%3AJ%2Bdomain%20text_abstract_title_flags%3Amatch-phrase%20sort%3Apublic channel results in a robust tonic inhibition of channel activity by G protein ?? subunits ( channel results i channel results in a robust tonic inhibition of channel activity by G protein ?? subunits (Magga et al., 2000). The CSP/G protein inter channel results i channel results in a robust tonic inhibition of channel results i channel results in a robust tonic inhibition of channel activity by G protein ?? subunits (Magga et al., 2000). The CSP/G protein interaction was confirmed by co-immunoprecipitation, GST pull-down assays, crosslinking in intact brain slice channel results i channel results in a robust tonic inhibition of channel activity by G protein ?? subuni chann channel results in a robust tonic inhibition of channel activity by G protein channe channel results in a robust tonic inhibition of channel activity by G protein ?? subunits (Magga et al., 2000). The CSP/G protein interaction was confirmed by co-immunoprecipitation, GST pull-down assays, crosslinking in intact brain slices as well as evaluation of functional proteins in H chann channel results in a robust tonic inhibition of channel activity by G protein ?? subunits (Magga et al., 2000). The CSP/G protein interaction was confirmed by co-immunoprecipitation, GST pull-down assays, crosslinking in intact brain slices as well as evaluation channel chann channel results in a robust tonic inhi channel results in a rob channel res channel results in a robust tonic inhibitio channel results in a robust tonic inhibition channel resul channel results in a robust tonic inhibition of channel activity by 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 centrifuged for 10 minutes at 500 homogen homo homo homogenizer in 0.32 M sucrose, 10 mM HEPES KOH (pH 7.0), 1 mM EGTA, 0.1 mM EDTA, 0.5 mM PMSF, homogen homo homo 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 (Boehr homog homogeniz homog 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 centrifuged for 10 min homogen homo homo 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 centrifuged for 10 minutes at 500 g and the supernatant collected and subs homogenize homogenizer homogenizer in 0.32 M sucrose, 10 mM HEPES homogenizer in 0.32 M sucrose, 10 homogenizer i homogenizer in 0.32 M sucrose, 10 mM HEPES KOH (pH 7.0), 1 mM EGTA, 0.1 mM EDTA, 0.5 mM PMSF, homogenizer in 0. homog homogenizer in 0.32 M s homogenizer in 0.32 M sucrose, 10 mM HEPES KOH (pH 7.0), 1 mM EGTA, 0.1 mM EDTA, 0.5 mM homogenizer in 0.32 homogenizer in 0.32 M sucrose, 10 mM HEPES KOH (pH 7.0), 1 mM homog homogen homoge 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 (Boe homogenizer in 0.3 homogenizer inences 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 mM KCl, 10 mM Naences ences of ences ences of all coences ences ofences ences 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 ences oences of all constructs were verified by sequencing both strands using the dideoxynucleotide chain termination method. After induction of expression with ences ences of aences ences 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 fences ences of all constructs were verified by sequencing both strands using theences oences 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 suspendeences of alences of all ences of all constructs were verified by seqences of all constences of all cences 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 mM KCl, 10 mM Na2HPO4, 2 mM KH2PO4) supplemented with 0.05% ences ences of ences ences of all consences ences ofences ences of all constructs were verified by sequencing both strands using the dideoxynucleotide chain termination method. After induction of expression with 100 ?M isopropyl-?-D-thiogaion 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.ion and incion and incubion and incubated for 30 minutes with goat aion and incubated for 30 minutes with gion and incubaion and incubated for 30 minutes with goat anti-rabbit or goat anti-moion andion and incubated for 30 minutes with goat anti-rabbit or goat anti-mouse IgG-coupled horseradish peroxidase. Antigen was detected using chemiluminescent horseion and incubated ion and incubated for 30 minutes with goat anti-rabbit or goat ion and iion and incion and inion and incubaion and incion and incubated for 30 minutes with goat anti-rabbit or goat anti-mousion anion 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.

    Transient transfection of HEK cells

    N-type calcium channel subunits, ion andion and incubated for 30 minutes with goat anti-rabbit or goat anti-mouse IgG-coion andion and incubated for 30 mion andion and inion anion and incuion and ion and incubated for 30 mion andion and incubatedion anion and incubated ion anion and ion andion and incubated for 30 minutes with goat anti-rabbit or goat anti-mouse IgG-coupled horseraion and iion and incubion and incion and incubated for 30 minutes with goat anti-rabbit or goat anti-mouse IgG-coupled horseradish ion and incion and

    Patch clamp recordings

    Immediately prior to recording, individual coverslips were <

    Patch clamp recordings

    Immediately prior to recording, individual coverslips were transferred 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 <

    Patch clamp recordings

    Immediately prior to recording, individual coverslips were transferred 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-8

    Patch clamp recordings

    Immediately prior to recording, individual coverslips were transferred 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 equnificant if nificnificant if P<0.05.

    nificant ifnificant if nificant if P<0.05.

    P<0.05.

    P<0.05.

    P<0.05.

    Results

    Binding properties of CSP and G proteins

    To establish if the interaction between CSP and G? is direct or indirect,nificantnificant if P<0.05.

    P<0.05.

    P<0.
    nificanificant if Pnificanificant if P<0.05.

    nificantnificant if P<0.05.

    nificanificant if P<0.05.

    Results

    monoc monoclonal and a monoc monoclonal monoc monoclonal and anti-Hsc70 monoclonal antibodies. G? does not interact with the J domain in the ab monoc monoclonal monoc monoclonal and anti-Hsc70 monoclonal antibodies. G? does not interact with the J domain in the absence or presence of any nucleotide tested. G? binds to the J domain in the presence of ATP. These results are representative of six independent experiments.

    To investigate the stability o monoclonal a monoclonal and anti-Hsc70 monocl mon monoclonal and anti-Hsc70 monoclonal a monoclonal and anti-Hsc70 mo monoclonal and anti-Hsc70 monoclona monoclonal and anti-Hsc70 mitrocellulose membrane was probe  Fig. 3.  itrocellul  Fig. 3.  itrocelluloitrocelitroitroceitroceitrocellulose membrane was probed with anitrocellulose membrane was probitrocellulose mitroitrocitrocellulonew-tab">new-tab">new-tab">Open in new tab

  • new-tanew-tab">new-tabnew-tab">Download figure
  • ?, anti-G? polyclonal (Calbiochem) was, CSP1-, CSP1-165 and CSP1-14, CSP1, CSP1, CSP1, CSP1-165 and CSP1-146. In addition to the identification of hip, CSP1, CSP1-165 and CSP1-146. In addition to the identification of hippocampal G?, anti-, CSP1, CSP1-165 and CSP1-146. In addition to the identification o, CSP1, CSP1, CSP1, CSP1-165 and CSP1-146. In addition to the identification of hippocampal G??, anti-G? polyclonal (Calbiochem) was observed to crossreact nonspecifically with abundant proteins, especially CSP83-198 and CSP137-198 (ysis. ). These data are consistent with our previous model suggesting that CSP may anchor and chaperone G protein ?? subunits to the N-type calcium channel (). These data ).). These ). These data are consistent ). These data are consistent with o). These data are consist). These data are consistent wit). These data are consisα1B +α 2 - δ +  Fig. 6.  α1B   Fig. 6.  α1B +αααα1B +α 2 - δ + β1α1B +α 2 - δ α1B +;α1B +α 2/14/2967/F6.lar/14//14/2/14/2967/F6.large.jpg" class="/14/2967/F6.large.j/14//14/2/14/2/14/29/14/2967/F6.large.jpg" cl/14/2967/F6.large.jpg" class="highwire-/14/2967/F6.lar/14/2967/F6.large.jpg"/14/2967/F6.large.jpg" /14/2967/F6.large.jpg" class="highwire-figure-link highwire-figure-link-newtab" target="_blank" data-icon-position="" data-hide-link-title="0/14/296/14/2967/F/14/29/14/2967/F6.la/14/296/14/2967/F6.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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  • Fig. 6.

    Regulation of N-type channel activity by individual CSP regions. (A) Current records obtained with N-type (?1B +? 2 - ? + ?1b) calcium channels expressed in tsa-201 cells before and after application of a 50 millisecond prepulse (pp) to +150 mV. Currents were elicited by stepping from a holding potential of -100 mV to a test potential of +20 mV. In the absence of CSP (left traces), the prepulses do not affect peak current amplitude. Following coexpression of either the cysteine string domain (middle traces) or /14/2/14/2967/F6.large.jp/14/2967/F6.large/14/2967/F6.large.jpg" class="high/14/29/14/29/14/2967/F6.lar/14/2967/F6.large.jpg" class="highwire-figure-link highwire-figure-li/14/2967//14/2967/F6.large.jpg" class="highwire-figure-link highwire-figure-link-newtab" target="_blank" datao be ineffective in mediating N-type channel inhibition. To our surprise, however, co-expression of the channel with the J domain resulted in robust prepulse relief, independently of the presence of ATP in the patch pipette (o be io be ineffective in mediao be inefo be ineffective in mediating N-type channel inhibition. To our surprise, however, co-expression of the channel with the J domain resulted in robust prepulse relief, independently of the presence of ATP in the patch pipette (Fig. 6). In addition to CSP1-82, co-expression of the o be ino be ineffective in medio be io be ineffective in mediating N-type channel inhibition. To our surprise, however, co-expression of the channel with the J domain resulted in robust prepulse relief, independently o be ineffecto be ineffective in mediating N-type channel inhibition. To our surprise, however, co-expression of to be ino be ineffective in mediating N-type channel inhibition. To our surprise, however, co-expression of the channel with the J domain resulted in robust prepulse relief, independently of the presence of ATP in the patch pipette (  Fig. 7.

    n> -488. -488n> -n> -488. -488n> -n> -488. -488n> -n> -488. -488n> -n> -48n> -488. -4n> -n> -488.
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  • Refn="" data-hide-link-title="0">Referenceskpoint-independent mechanism delays entry into mitosis after UV irradiationkpoint-kpoikpoint-kpoint-ikpointkpoinkpoint-independenkpoint-independent mechanism delays entry into mitosis after UV irradiation
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  • kpoint-independent mechanism delays entry into mitosis after UV irradiation
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    Other jopane-cob-journals" > target="_blank">Cell scientist to watch &nd tar target target="_blank">CMahak Sharma tar targe target="_bla target="_blank">Cell scientist to watch – Mahak Sharma

    Cell scientist to watch – Mahak Sharma

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    target="_blan target="_blank">Cell scientist to watch &ndas targe target tar target="_blank">Cell scientist to watch – Mahak Sharma tar target target="_blank">CSchematic showing actin assembly mechanisms: authophagosome, sorting endosome and lysosomeme, me, some, sortingme, sortinme, sorting endosome and lysosome" src="http://jcs.biologists.org/sites/default/files/Snippet/1017_AAG.JPG" style="border-width: 0px; border-style: solid; width: 90%;" />

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    In this me, sorting endome, sme, sorme,me, sortblank">DNA damage induces a kinetochore-based ATM/ATR-independent SAC arrest unique to the first meiotic division in mouse blanblank">DNblank">DNA damage induces a kinetochore-based ATM/ATR-independent SAC arrest unique to the first meiotic division in mouse oocytesDNA damage induces a kinetochore-based ATM/ATR-independeblank"blablank">Dblank">DNA damage induces a kinetochore-based ATM/ATR-independent SAC arrest unique tblanblank">DNblank">DNA damage induces a kinetochore-based ATM/ATR-independent SAC arrest unique to the first meiotic division in mouse oocytes
    Simon I. R. Lane, Stephablank">DNA damage induces a kinetochore-based ATM/ATR-independeblank"blank">blanblank">DNA damage induceblanblank">blank">DNA damage induces a kinetochore-based ATM/ATR-independent SAC arrest unique to the first meiotic division in mouse oocytes

    Simon I. Rblank">DNA dblank">DNA damage induces a kinetochore-based ATM/ATR-independent SAC arrest unique to the first meiotblanblankblank">blank">Dblank">DNblank">DNA dablank">blank">DNAblank">DNblank">DNAblank">blank">DNA damage induces a kinetblank">DNA dblank">DNblank">blank">DNA dblank">blank">Dblank">blank">DNA damage induceblank">DNA damage induces a kinetochore-based ATM/ATR-independent Sblank">DNA damage induces a kinetochore-based ATM/ATR-independent SAC arrest uniqublankclass="grid-7 prefix-1 region region-postscript-first" id="region-postscript-first"> class="grid-7 prefix-1 region region-postscript-first" id="reclass="grid-7 prefix-1 region region-postscript-first" id="region-postscript-first">

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