GLORIA

GEOMAR Library Ocean Research Information Access

X

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
Filter
Material
Publisher
Person/Organisation
Language
Years
FID
Subjects(RVK)
  • 1
    Online Resource
    Online Resource
    Probing Structure-Function Relationships in Missense Variants in the Carboxy-Terminal Region of BRCA1
    Public Library of Science (PLoS) ; 2014
    In:  PLoS ONE Vol. 9, No. 5 ( 2014-5-20), p. e97766-
    Details
    In: PLoS ONE, Public Library of Science (PLoS), Vol. 9, No. 5 ( 2014-5-20), p. e97766-
    Type of Medium: Online Resource
    ISSN: 1932-6203
    URL: Article
    URL: Article
    URL: Article
    URL: Article
    URL: Article
    URL: Article
    URL: Article
    URL: Article
    URL: Article
    DOI: 10.1371/journal.pone.0097766
    DOI: 10.1371/journal.pone.0097766.g001
    DOI: 10.1371/journal.pone.0097766.g002
    DOI: 10.1371/journal.pone.0097766.g003
    DOI: 10.1371/journal.pone.0097766.g004
    DOI: 10.1371/journal.pone.0097766.g005
    DOI: 10.1371/journal.pone.0097766.t001
    DOI: 10.1371/journal.pone.0097766.s001
    DOI: 10.1371/journal.pone.0097766.s002
    Language: English
    Publisher: Public Library of Science (PLoS)
    Publication Date: 2014
    detail.hit.zdb_id: 2267670-3
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Online Resource
  • 2
    Online Resource
    Online Resource
    Tracking the turnover of SARS-CoV-2 VOCs Gamma to Delta in a Brazilian state (Minas Gerais) with a high-vaccination status
    Oxford University Press (OUP) ; 2022
    In:  Virus Evolution Vol. 8, No. 2 ( 2022-08-06)
    Details
    In: Virus Evolution, Oxford University Press (OUP), Vol. 8, No. 2 ( 2022-08-06)
    Abstract: The emergence and global dissemination of Severe Acute Respiratory Syndrome virus 2 (SARS-CoV-2) variants of concern (VOCs) have been described as the main factor driving the Coronavirus Disease 2019 pandemic. In Brazil, the Gamma variant dominated the epidemiological scenario during the first period of 2021. Many Brazilian regions detected the Delta variant after its first description and documented its spread. To monitor the introduction and spread of VOC Delta, we performed Polymerase Chain Reaction (PCR) genotyping and genome sequencing in ten regional sentinel units from June to October 2021 in the State of Minas Gerais (MG). We documented the introduction and spread of Delta, comprising 70 per cent of the cases 8 weeks later. Comparing the viral loads of the Gamma and Delta dominance periods, we provide additional evidence that the latter is more transmissible. The spread and dominance of Delta did not culminate in the increase in cases and deaths, suggesting that the vaccination may have restrained the epidemic growth. Analysis of 224 novel Delta genomes revealed that Rio de Janeiro state was the primary source for disseminating this variant in the state of MG. We present the establishment of Delta, providing evidence of its enhanced transmissibility and showing that this variant shift did not aggravate the epidemiological scenario in a high immunity setting.
    Type of Medium: Online Resource
    ISSN: 2057-1577
    URL: Article
    DOI: 10.1093/ve/veac064
    Language: English
    Publisher: Oxford University Press (OUP)
    Publication Date: 2022
    detail.hit.zdb_id: 2818949-8
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Online Resource
  • 3
    Online Resource
    Online Resource
    Modulation of expression and activity of cytochrome P450s and alteration of praziquantel kinetics during murine schistosomiasis
    FapUNIFESP (SciELO) ; 2011
    In:  Memórias do Instituto Oswaldo Cruz Vol. 106, No. 2 ( 2011-03), p. 212-219
    Details
    In: Memórias do Instituto Oswaldo Cruz, FapUNIFESP (SciELO), Vol. 106, No. 2 ( 2011-03), p. 212-219
    Type of Medium: Online Resource
    ISSN: 0074-0276
    URL: Article
    DOI: 10.1590/S0074-02762011000200016
    Language: Unknown
    Publisher: FapUNIFESP (SciELO)
    Publication Date: 2011
    detail.hit.zdb_id: 2017165-1
    SSG: 12
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Online Resource
  • 4
    Online Resource
    Online Resource
    Genomics and epidemiology of the P.1 SARS-CoV-2 lineage in Manaus, Brazil
    American Association for the Advancement of Science (AAAS) ; 2021
    In:  Science Vol. 372, No. 6544 ( 2021-05-21), p. 815-821
    Details
    In: Science, American Association for the Advancement of Science (AAAS), Vol. 372, No. 6544 ( 2021-05-21), p. 815-821
    Abstract: Cases of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection in Manaus, Brazil, resurged in late 2020 despite previously high levels of infection. Genome sequencing of viruses sampled in Manaus between November 2020 and January 2021 revealed the emergence and circulation of a novel SARS-CoV-2 variant of concern. Lineage P.1 acquired 17 mutations, including a trio in the spike protein (K417T, E484K, and N501Y) associated with increased binding to the human ACE2 (angiotensin-converting enzyme 2) receptor. Molecular clock analysis shows that P.1 emergence occurred around mid-November 2020 and was preceded by a period of faster molecular evolution. Using a two-category dynamical model that integrates genomic and mortality data, we estimate that P.1 may be 1.7- to 2.4-fold more transmissible and that previous (non-P.1) infection provides 54 to 79% of the protection against infection with P.1 that it provides against non-P.1 lineages. Enhanced global genomic surveillance of variants of concern, which may exhibit increased transmissibility and/or immune evasion, is critical to accelerate pandemic responsiveness.
    Type of Medium: Online Resource
    ISSN: 0036-8075 , 1095-9203
    URL: Article
    DOI: 10.1126/science.abh2644
    RVK:
    TA 1000
    RVK:
    WA 15000
    Language: English
    Publisher: American Association for the Advancement of Science (AAAS)
    Publication Date: 2021
    detail.hit.zdb_id: 128410-1
    detail.hit.zdb_id: 2066996-3
    detail.hit.zdb_id: 2060783-0
    SSG: 11
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Online Resource
  • 5
    Online Resource
    Online Resource
    Feasibility study of photovoltaic powered reverse osmosis and pumping plant configurations
    Institution of Engineering and Technology (IET) ; 2013
    In:  IET Renewable Power Generation Vol. 7, No. 2 ( 2013-03), p. 134-143
    Details
    In: IET Renewable Power Generation, Institution of Engineering and Technology (IET), Vol. 7, No. 2 ( 2013-03), p. 134-143
    Type of Medium: Online Resource
    ISSN: 1752-1416 , 1752-1424
    URL: Issue
    URL: Article
    DOI: 10.1049/rpg2.v7.2
    DOI: 10.1049/iet-rpg.2012.0228
    Language: English
    Publisher: Institution of Engineering and Technology (IET)
    Publication Date: 2013
    detail.hit.zdb_id: 2264540-8
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Online Resource
  • 6
    Online Resource
    Online Resource
    Abstract 1117: Characterization of BAT1 (UAP56) interaction with BARD1
    American Association for Cancer Research (AACR) ; 2010
    In:  Cancer Research Vol. 70, No. 8_Supplement ( 2010-04-15), p. 1117-1117
    Details
    In: Cancer Research, American Association for Cancer Research (AACR), Vol. 70, No. 8_Supplement ( 2010-04-15), p. 1117-1117
    Abstract: BARD1 (BRCA1-associated ring domain 1) was originally identified in a yeast-two-hybrid screen as a binding partner of BRCA1. The functional heterodimer BRCA1-BARD1 is required for several of the cellular and tumour-suppressor functions of BRCA1. Both proteins interact through the N-terminal RING domain to form a heterodimeric E3 ubiquitin ligase that constitutes the major catalytic activity of the BRCA1-BARD1 complex. BARD1 is also associated to p53-mediated apoptosis, in a BRCA1-independent manner. The carboxy terminus of BRCA1 is highly acidic and contains two tandem BRCA1 C-terminal (BRCT) domains, which are characteristic of members of a large superfamily of proteins involved in DNA repair and cell cycle checkpoint control. These domains are protein-protein interacting regions that mediate the association with a number of other proteins with a role in DNA replication, DNA damage repair (DDR) pathway, transcription, cell cycle control, and ubiquitination. BARD1 also contains two tandem BRCT repeats at its C-terminus, a region shown to bind serine-phosphorylated peptides in vitro. In order to identify putative interaction-proteins with BARD1 C-terminal region we performed a yeast two hybrid (Y2H) screening using BARD1 BRCT tandem domain (aa 554-777) to screen a human testis cDNA library. We identified, among other hits, a cDNA coding for residues 308-418 of BAT1 (UAP56, C-terminal region [OMIM 142560]). UAP56 is a member of DEAD box family of ATP-dependent RNA helicases. Several studies indicate that UAP56 protein is not only essential in pre-mRNA splicing but is also important in mRNA nuclear export and cytoplasmic mRNA localization. We confirmed BAT1-BARD1 interaction by conducting co-IP analysis of ectopic expressed BARD1 and BAT1 in HEK293T cells. We are using a Y2H system approach to determine the minimal region of interaction between BARD1 and BAT1; in parallel, we are also checking for the presence of a multicomponent complex, investigating the presence of BRCA1. In order to assess the biological significance of the interaction between BARD1 and BAT1 we will determine whether this interaction is important for the activation of, or recovery from, the G2/M cell cycle checkpoint after IR and also investigate its putative involvement in p53-dependent apoptosis pathway. Citation Format: {Authors}. {Abstract title} [abstract]. In: Proceedings of the 101st Annual Meeting of the American Association for Cancer Research; 2010 Apr 17-21; Washington, DC. Philadelphia (PA): AACR; Cancer Res 2010;70(8 Suppl):Abstract nr 1117.
    Type of Medium: Online Resource
    ISSN: 0008-5472 , 1538-7445
    URL: Article
    DOI: 10.1158/1538-7445.AM10-1117
    RVK:
    XA 36000
    RVK:
    XA 10000
    Language: English
    Publisher: American Association for Cancer Research (AACR)
    Publication Date: 2010
    detail.hit.zdb_id: 2036785-5
    detail.hit.zdb_id: 1432-1
    detail.hit.zdb_id: 410466-3
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Online Resource
  • 7
    Online Resource
    Online Resource
    Abstract 632: Characterization of BCCIP as a novel BARD1 interaction partner.
    American Association for Cancer Research (AACR) ; 2013
    In:  Cancer Research Vol. 73, No. 8_Supplement ( 2013-04-15), p. 632-632
    Details
    In: Cancer Research, American Association for Cancer Research (AACR), Vol. 73, No. 8_Supplement ( 2013-04-15), p. 632-632
    Abstract: BARD1 (BRCA1-Associated Ring Domain 1) was originally identified in a yeast-two-hybrid (Y2H) screen as a binding partner of BRCA1. The functional heterodimer BRCA1/BARD1 is required for several of the cellular and tumor-suppressor functions of BRCA1. Both proteins interact through the N-terminal RING domain to form a heterodimeric E3 ubiquitin ligase that constitutes the major catalytic activity of the BRCA1-BARD1 complex. BARD1 is also associated to p53-mediated apoptosis, in a BRCA1-independent manner. The carboxy terminus of BRCA1 is highly acidic and contains two tandem BRCA1 C-terminal (BRCT) domains, which are characteristic of members of a large superfamily of proteins involved in DNA repair and cell cycle checkpoint control. These domains are protein-protein interacting regions that mediate the association with a number of other proteins with a role in DNA replication, DNA damage repair pathway, transcription, cell cycle control, and ubiquitination. Although several BRCA1-interacting proteins were reported, few proteins were described to interact with BARD1. In order to identify putative interaction-proteins with BARD1 C-terminal region we performed a Y2H assay using BARD1 BRCT tandem domain (aa 554-777) to screen a human testis cDNA library. We identified, among other hits, a cDNA coding for BCCIP (BRCA2 and CDKN1A Interacting Protein) C-terminal region. BCCIP is known for its involvement in DNA damage repair and the cell cycle control. BCCIP interacts with BRCA2, and both proteins are important for RAD51 focus formation after ionizing radiation and homologous recombination (HR) repair of double-strand-breaks (DSBs). BCCIP enhances the p21 suppression activity towards CDK2, and BCCIP downregulation reduces p21 expression by abrogating p53 transcription activity. We confirmed BCCIP/BARD1 interaction by pull-down and co-immunoprecipitation (co-IP) analysis of ectopically expressed BARD1 and BCCIP. We also identified the constitutive BCCIP/BARD1 complex in human cells by co-IP assays. Interestingly the BCCIP observed in complex with BARD1 corresponds to a mono-ubiquitinated form, suggesting that BCCIP may be a putative natural target for BRCA1/BARD1 heterodimer E3 ubiquitin ligase. BRCA1 participation in a multicomponent complex with BCCIP is under investigation. In order to assess the biological significance of the interaction between BCCIP and BARD1 we are investigating its role in DNA damage repair, cell cycle control and apoptosis. We are also evaluating the BCCIP protein interaction network using a tandem affinity purification approach. Citation Format: Joao Séllos, Thales C. Nepomuceno, Renato S. Carvalho, Guilherme Suarez-Kurtz, Alvaro N.A. Monteiro, Marcelo A. Carvalho. Characterization of BCCIP as a novel BARD1 interaction partner. [abstract]. In: Proceedings of the 104th Annual Meeting of the American Association for Cancer Research; 2013 Apr 6-10; Washington, DC. Philadelphia (PA): AACR; Cancer Res 2013;73(8 Suppl):Abstract nr 632. doi:10.1158/1538-7445.AM2013-632
    Type of Medium: Online Resource
    ISSN: 0008-5472 , 1538-7445
    URL: Article
    DOI: 10.1158/1538-7445.AM2013-632
    RVK:
    XA 36000
    RVK:
    XA 10000
    Language: English
    Publisher: American Association for Cancer Research (AACR)
    Publication Date: 2013
    detail.hit.zdb_id: 2036785-5
    detail.hit.zdb_id: 1432-1
    detail.hit.zdb_id: 410466-3
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Online Resource
  • 8
    Online Resource
    Online Resource
    Abstract 480: CDK9 (a novel BRCA1/BARD1 interaction partner) downregulates BRCA1-mediated transcription
    American Association for Cancer Research (AACR) ; 2014
    In:  Cancer Research Vol. 74, No. 19_Supplement ( 2014-10-01), p. 480-480
    Details
    In: Cancer Research, American Association for Cancer Research (AACR), Vol. 74, No. 19_Supplement ( 2014-10-01), p. 480-480
    Abstract: BRCA1 gene encodes a 1863 amino-acid protein comprising a RING finger domain in the N-terminus and two tandem BRCT domains (tBRCT) in C-terminal region. When fused to a heterologous DNA-binding domain, BRCA1 C-terminal region is capable of activating transcription. In addition, BRCA1 was found associated with the RNA polymerase II holoenzyme (RNApolII), a number of transcription factors and regulators. BRCA1 cancer-associated mutations located in the C-terminal region of the protein lead to an impaired transcriptional activation phenotype - the ability to trigger transcription seems to be an important feature of BRCA1 tumor suppression function. BARD1 (BRCA1 associated RING domain 1) also encloses a N-terminal RING finger and a C-terminal tBRCT domains. The BRCA1/BARD1 heterodimer was found to ubiquitinate RNApolII leading to a reduced transcription initiation. Recently, our group described a protein interaction network that identified putative interacting partners of seven different proteins enclosing the tBRCT domain. Among other hits, Cyclin-Dependent Kinase 9 (CDK9) was identified as a common interaction partner of BRCA1 and also BARD1 tBRCTs. CDK9 is a component of the positive transcription elongation factor b complex (P-TEFb), which is involved in co-transcriptional histone modification, mRNA processing, mRNA export and transcriptional elongation. The interaction between constitutive CDK9 and BARD1 was confirmed through co-immunoprecipitation (Co-IP) assay using HEK293FT cells nuclear extracts. We also demonstrated that CDK9 isoforms were able to interact both with BARD1 N- and C-terminal regions in a GST pulldown assay. In addition, the BRCA1/CDK9 constitutive interaction was confirmed by Co-IP assay in HeLa cells. We showed that, differently from BARD1, BRCA1 tBRCT interacts only with the 42KDa isoform of CDK9. In order to investigate CDK9 role in BRCA1 mediated transcription, the kinase expression was downregulated (by shRNA methodology) in HeLa cells, resulting in a two-fold increase in transcription (observed in a luciferase reporter assay). On the other hand, the super expression of CDK9 42KDa isoform leads to the suppression of BRCA1 mediated transcription. These data suggest that the CDK9 42KDa isoform modulates BRCA1 mediated transcription through its tBRCT domain. Now, we are extending our approach to investigate which genes are regulated by this complex. We also ought to investigate the role of BARD1 in the CDK9 regulation function. A better understanding of these interactions will help to unravel the BRCA1 mediated transcription and its tumor suppression function. Citation Format: Thales C. Nepomuceno, Vanessa C. Fernandes, Giuliana De Gregoris, Renato S. Carvalho, Álvaro N. Monteiro, Marcelo A. Carvalho. CDK9 (a novel BRCA1/BARD1 interaction partner) downregulates BRCA1-mediated transcription. [abstract]. In: Proceedings of the 105th Annual Meeting of the American Association for Cancer Research; 2014 Apr 5-9; San Diego, CA. Philadelphia (PA): AACR; Cancer Res 2014;74(19 Suppl):Abstract nr 480. doi:10.1158/1538-7445.AM2014-480
    Type of Medium: Online Resource
    ISSN: 0008-5472 , 1538-7445
    URL: Article
    DOI: 10.1158/1538-7445.AM2014-480
    RVK:
    XA 36000
    RVK:
    XA 10000
    Language: English
    Publisher: American Association for Cancer Research (AACR)
    Publication Date: 2014
    detail.hit.zdb_id: 2036785-5
    detail.hit.zdb_id: 1432-1
    detail.hit.zdb_id: 410466-3
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Online Resource
  • 9
    Online Resource
    Online Resource
    Abstract A04: Structural and functional caracterization of BARD1/CDK13 interaction
    American Association for Cancer Research (AACR) ; 2018
    In:  Clinical Cancer Research Vol. 24, No. 1_Supplement ( 2018-01-01), p. A04-A04
    Details
    In: Clinical Cancer Research, American Association for Cancer Research (AACR), Vol. 24, No. 1_Supplement ( 2018-01-01), p. A04-A04
    Abstract: DNA damage response (DDR) is crucial for cell survivor through genomic integrity maintenance. Dysfunctions in proteins implicated in DDR prompt cell to diseases, such as cancer. BRCA1 is a central protein involved in DDR and, once damaged, plays a pivotal role in cancer development. BRCA1 structure comprises two major domains, a RING finger domain and two tandem BRCT domains (tBRCT). This structure is shared by BRCA1 major interaction partner: BARD1. The tBRCT domain is commonly found in DDR-associated proteins. To study interactions in DDR, our group charted the tBRCT interactome for 7 different proteins, using three different strategies: tandem affinity purification followed by mass spectrometry (TAP-MS), yeast two hybrid (Y2H) screening, and literature curation. CDK13 was identified as a putative BARD1 tBRCT interactor by both TAP-MS and Y2H strategies. CDK13 is described as involved in several processes, such as chromatin remodeling, transcription regulation, and splicing coordination; however, its biological role remains unclear. To confirm BARD1/CDK13 interaction, whole cell extracts obtained from MCF-7 cells were used in coimmunoprecipitation assays using anti-CDK13 and anti-BARD1. Constructs encoding the HA-tagged regions 1-706aa (N-terminal), 706-982aa (kinase domain), and 1006-1452aa (C-terminal) of CDK13 were ectopically coexpressed with Flag-tagged full-length BARD1 or GFP-tagged BARD1 tBRCT in HEK293Tcells; whole cellular extracts were used in coimmunoprecipitation assays. BARD1 and CDK13 interaction was confirmed both in ectopic and constitutive expression approaches. CDK13 silencing was performed using lentiviral constructs encoding five different short hairpin RNAs (shRNA); MCF-7 cells were transduced and submitted to puromycin selection; extracts were used to evaluate CDK13 silencing by immunoblotting. Our data suggest that BARD1 tBRCT and the CDK13 N-terminal region, as well as the kinase domain, are critical for the formation of BARD1/CDK13 complex. MCF-7 cells lacking CDK13 expression will be used to investigate the kinase role during DDR. Citation Format: Vanessa C. Fernandes, Thales C. Nepomuceno, Renato S. Carvalho, Guilherme Suarez-Kurtz, Alvaro N. Monteiro, Marcelo A. Carvalho. Structural and functional caracterization of BARD1/CDK13 interaction [abstract]. In: Proceedings of the AACR International Conference held in cooperation with the Latin American Cooperative Oncology Group (LACOG) on Translational Cancer Medicine; May 4-6, 2017; São Paulo, Brazil. Philadelphia (PA): AACR; Clin Cancer Res 2018;24(1_Suppl):Abstract nr A04.
    Type of Medium: Online Resource
    ISSN: 1078-0432 , 1557-3265
    URL: Article
    DOI: 10.1158/1557-3265.TCM17-A04
    RVK:
    XA 36791
    Language: English
    Publisher: American Association for Cancer Research (AACR)
    Publication Date: 2018
    detail.hit.zdb_id: 1225457-5
    detail.hit.zdb_id: 2036787-9
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Online Resource
  • 10
    Online Resource
    Online Resource
    Abstract 2132: Characterization of galectin 3 as a novel BARD1 interaction partner
    American Association for Cancer Research (AACR) ; 2012
    In:  Cancer Research Vol. 72, No. 8_Supplement ( 2012-04-15), p. 2132-2132
    Details
    In: Cancer Research, American Association for Cancer Research (AACR), Vol. 72, No. 8_Supplement ( 2012-04-15), p. 2132-2132
    Abstract: BARD1 (BRCA1-associated ring domain 1) was originally identified in a yeast-two-hybrid (Y2H) screen as a binding partner of BRCA1. The functional heterodimer BRCA1/BARD1 is required for several of the cellular and tumor-suppressor functions of BRCA1. Both proteins interact through the N-terminal RING domain to form a heterodimeric E3 ubiquitin ligase that constitutes the major catalytic activity of the BRCA1-BARD1 complex. BARD1 is also associated to p53-mediated apoptosis, in a BRCA1-independent manner. The carboxy terminus of BRCA1 is highly acidic and contains two tandem BRCA1 C-terminal (BRCT) domains, which are characteristic of members of a large superfamily of proteins involved in DNA repair and cell cycle checkpoint control. These domains are protein-protein interacting regions that mediate the association with a number of other proteins with a role in DNA replication, DNA damage repair pathway, transcription, cell cycle control, and ubiquitination. In order to identify putative interaction-proteins with BARD1 C-terminal region we performed a Y2H screening using BARD1 BRCT tandem domain (aa 554-777) to screen a human testis cDNA library. We identified, among other hits, a cDNA coding for galectin 3 C-terminal region, residues 170-250 (OMIM 153619). Galectin 3 is a galactoside binding protein involved in several cellular processes including apoptosis control and RNA splicing. Moreover there are evidences that galectin 3 variants are correlated with tumor development and progression in breast and thyroid cancer. We confirmed galectin 3/BARD1 interaction conducting co-immunoprecipitation analysis of ectopically expressed BARD1 and galectin-3 in HEK293T cells. The interaction between endogenous galectin 3 and BARD1 were validated in HeLa nuclear extracts, and by confocal microscopy. Using ectopically expressed galectin 3 fragments we determined the interaction region (aa 100-215). Moreover, galectin 3 fragment comprising aminoacids 100-165 is able to disrupt the endogenous interaction with BARD1. Co-immunoprecipitation assays suggested the presence of BRCA1, BARD1 and galectin-3 in the same complex. Interestingly the galectin 3 observed in this complex corresponds to a mono-ubiquitinated form. This ubiquitination reaction occurs mainly in the nucleus but is not BRCA1 dependent. The role of galectin 3 in DNA damage pathway was investigated using galectin 3 silenced HeLa cells exposed to increasing doses of ionizing radiation. These cells exhibited a slightly increase in radioresistance, but no effect was observed in cell cycle control. In addition the phosphorylation of histone H2AX seems to be delayed after damage in cells lacking galectin 3. Other DNA damage agents, such as carboplatin and etoposide did not affected differently the cell viability of these cells. We are now evaluating the protein interaction network of galectin 3 using a tandem affinity purification approach. Citation Format: {Authors}. {Abstract title} [abstract]. In: Proceedings of the 103rd Annual Meeting of the American Association for Cancer Research; 2012 Mar 31-Apr 4; Chicago, IL. Philadelphia (PA): AACR; Cancer Res 2012;72(8 Suppl):Abstract nr 2132. doi:1538-7445.AM2012-2132
    Type of Medium: Online Resource
    ISSN: 0008-5472 , 1538-7445
    URL: Article
    DOI: 10.1158/1538-7445.AM2012-2132
    RVK:
    XA 36000
    RVK:
    XA 10000
    Language: English
    Publisher: American Association for Cancer Research (AACR)
    Publication Date: 2012
    detail.hit.zdb_id: 2036785-5
    detail.hit.zdb_id: 1432-1
    detail.hit.zdb_id: 410466-3
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Online Resource
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...