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  1. Article ; Online: The complementary roles of MPS and CAC in renal patients.

    Lee, Joseph C / Baer, Richard A

    Journal of nuclear cardiology : official publication of the American Society of Nuclear Cardiology

    2022  Volume 29, Issue 3, Page(s) 1446

    MeSH term(s) Coronary Artery Disease ; Humans ; Tomography, Emission-Computed, Single-Photon
    Language English
    Publishing date 2022-04-04
    Publishing country United States
    Document type Letter ; Comment
    ZDB-ID 1212505-2
    ISSN 1532-6551 ; 1071-3581
    ISSN (online) 1532-6551
    ISSN 1071-3581
    DOI 10.1007/s12350-022-02965-y
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 4121: Show issues Location:
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  2. Article ; Online: The practicalities of COVID's impact on nuclear cardiology.

    Lee, Joseph C / Baer, Richard A

    Journal of nuclear cardiology : official publication of the American Society of Nuclear Cardiology

    2022  Volume 29, Issue 5, Page(s) 2739–2740

    MeSH term(s) COVID-19 ; Cardiology ; Cardiovascular System ; Humans ; Nuclear Medicine
    Language English
    Publishing date 2022-07-05
    Publishing country United States
    Document type Letter ; Comment
    ZDB-ID 1212505-2
    ISSN 1532-6551 ; 1071-3581
    ISSN (online) 1532-6551
    ISSN 1071-3581
    DOI 10.1007/s12350-022-03058-6
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    Zs.A 4121: Show issues Location:
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  3. Article ; Online: Differences in bone mineral density of lumbar spine and femur.

    Chong, Jia Wen / Baer, Richard A / Lee, Joseph C

    Peritoneal dialysis international : journal of the International Society for Peritoneal Dialysis

    2023  Volume 43, Issue 4, Page(s) 350

    MeSH term(s) Humans ; Bone Density ; Femur/diagnostic imaging ; Lumbar Vertebrae/diagnostic imaging ; Peritoneal Dialysis
    Language English
    Publishing date 2023-06-19
    Publishing country United States
    Document type Letter
    ZDB-ID 645010-6
    ISSN 1718-4304 ; 0896-8608
    ISSN (online) 1718-4304
    ISSN 0896-8608
    DOI 10.1177/08968608231182113
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    Zs.A 1936: Show issues Location:
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  4. Article ; Online: Luring BRCA1 to the scene of the crime.

    Baer, Richard

    Cancer cell

    2013  Volume 23, Issue 5, Page(s) 565–567

    Abstract: To preserve genome stability, BRCA1 must be recruited to sites of DNA damage, where BRCA1 facilitates repair of double-strand DNA breaks (DSBs). In this issue of Cancer Cell, Li and Yu report that BRCA1 recruitment involves a novel interaction between ... ...

    Abstract To preserve genome stability, BRCA1 must be recruited to sites of DNA damage, where BRCA1 facilitates repair of double-strand DNA breaks (DSBs). In this issue of Cancer Cell, Li and Yu report that BRCA1 recruitment involves a novel interaction between its partner protein BARD1 and poly(ADP-ribose) chains at the DSB.
    MeSH term(s) DNA Damage ; DNA Repair ; Humans ; Ubiquitin-Protein Ligases/physiology
    Chemical Substances BRAP protein, human (EC 2.3.2.27) ; Ubiquitin-Protein Ligases (EC 2.3.2.27)
    Language English
    Publishing date 2013-05-13
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Comment
    ZDB-ID 2078448-X
    ISSN 1878-3686 ; 1535-6108
    ISSN (online) 1878-3686
    ISSN 1535-6108
    DOI 10.1016/j.ccr.2013.04.013
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    Zs.MG 104: Show issues

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  5. Article ; Online: Targeting USP2 regulation of VPRBP-mediated degradation of p53 and PD-L1 for cancer therapy.

    Yi, Jingjie / Tavana, Omid / Li, Huan / Wang, Donglai / Baer, Richard J / Gu, Wei

    Nature communications

    2023  Volume 14, Issue 1, Page(s) 1941

    Abstract: Since Mdm2 (Mouse double minute 2) inhibitors show serious toxicity in clinic studies, different approaches to achieve therapeutic reactivation of p53-mediated tumor suppression in cancers need to be explored. Here, we identify the USP2 (ubiquitin ... ...

    Abstract Since Mdm2 (Mouse double minute 2) inhibitors show serious toxicity in clinic studies, different approaches to achieve therapeutic reactivation of p53-mediated tumor suppression in cancers need to be explored. Here, we identify the USP2 (ubiquitin specific peptidase 2)-VPRBP (viral protein R binding protein) axis as an important pathway for p53 regulation. Like Mdm2, VPRBP is a potent repressor of p53 but VPRBP stability is controlled by USP2. Interestingly, the USP2-VPRBP axis also regulates PD-L1 (programmed death-ligand 1) expression. Strikingly, the combination of a small-molecule USP2 inhibitor and anti-PD1 monoclonal antibody leads to complete regression of the tumors expressing wild-type p53. In contrast to Mdm2, knockout of Usp2 in mice has no obvious effect in normal tissues. Moreover, no obvious toxicity is observed upon the USP2 inhibitor treatment in vivo as Mdm2-mediated regulation of p53 remains intact. Our study reveals a promising strategy for p53-based therapy by circumventing the toxicity issue.
    MeSH term(s) Mice ; Animals ; Tumor Suppressor Protein p53/genetics ; Tumor Suppressor Protein p53/metabolism ; B7-H1 Antigen/genetics ; B7-H1 Antigen/metabolism ; Proto-Oncogene Proteins c-mdm2/metabolism ; Neoplasms/drug therapy ; Neoplasms/genetics ; Carrier Proteins ; Ubiquitin Thiolesterase/genetics ; Ubiquitin Thiolesterase/metabolism ; Protein Serine-Threonine Kinases/metabolism
    Chemical Substances Tumor Suppressor Protein p53 ; CD274 protein, human ; B7-H1 Antigen ; Proto-Oncogene Proteins c-mdm2 (EC 2.3.2.27) ; Carrier Proteins ; Usp2 protein, mouse (EC 3.4.19.12) ; Ubiquitin Thiolesterase (EC 3.4.19.12) ; VprBP protein, mouse (EC 2.7.11.1) ; Protein Serine-Threonine Kinases (EC 2.7.11.1)
    Language English
    Publishing date 2023-04-06
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-023-37617-3
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  6. Article ; Online: Silent renal infarcts prompt further investigation.

    Peoples, Aine / Baer, Richard / Schweitzer, Daniel / Amos, Gregory

    BMJ case reports

    2020  Volume 13, Issue 3

    MeSH term(s) Aged ; Cerebral Infarction/diagnostic imaging ; Cerebral Infarction/drug therapy ; Delirium ; Factor Xa Inhibitors/therapeutic use ; Female ; Humans ; Infarction/diagnostic imaging ; Infarction/drug therapy ; Kidney Diseases/diagnostic imaging ; Kidney Diseases/drug therapy ; Magnetic Resonance Imaging ; Pyrazoles/therapeutic use ; Pyridones/therapeutic use
    Chemical Substances Factor Xa Inhibitors ; Pyrazoles ; Pyridones ; apixaban (3Z9Y7UWC1J)
    Language English
    Publishing date 2020-03-10
    Publishing country England
    Document type Case Reports ; Journal Article
    ISSN 1757-790X
    ISSN (online) 1757-790X
    DOI 10.1136/bcr-2020-234650
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  7. Article ; Online: ATM/ATR Phosphorylation of CtIP on Its Conserved Sae2-like Domain Is Required for Genotoxin-Induced DNA Resection but Dispensable for Animal Development.

    Wu-Baer, Foon / Wong, Madeline / Tschoe, Lydia / Lin, Chyuan-Sheng / Jiang, Wenxia / Zha, Shan / Baer, Richard

    Cells

    2023  Volume 12, Issue 23

    Abstract: Homology-directed repair (HDR) of double-strand DNA breaks (DSBs) is dependent on enzymatic resection of DNA ends by the Mre11/Rad50/Nbs1 complex. DNA resection is triggered by the CtIP/Sae2 protein, which allosterically promotes Mre11-mediated ... ...

    Abstract Homology-directed repair (HDR) of double-strand DNA breaks (DSBs) is dependent on enzymatic resection of DNA ends by the Mre11/Rad50/Nbs1 complex. DNA resection is triggered by the CtIP/Sae2 protein, which allosterically promotes Mre11-mediated endonuclease DNA cleavage at a position internal to the DSB. Although the mechanics of resection, including the initial endonucleolytic step, are largely conserved in eucaryotes, CtIP and its functional counterpart in
    MeSH term(s) Animals ; Mice ; Carrier Proteins/metabolism ; Cell Cycle Proteins/metabolism ; DNA/metabolism ; DNA-Binding Proteins/metabolism ; Mutagens ; Phosphorylation ; Saccharomyces cerevisiae/metabolism
    Chemical Substances Carrier Proteins ; Cell Cycle Proteins ; CtIP protein, mouse ; DNA (9007-49-2) ; DNA-Binding Proteins ; Mutagens
    Language English
    Publishing date 2023-12-04
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
    ZDB-ID 2661518-6
    ISSN 2073-4409 ; 2073-4409
    ISSN (online) 2073-4409
    ISSN 2073-4409
    DOI 10.3390/cells12232762
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  8. Article ; Online: BRCA1 and 53BP1 regulate reprogramming efficiency by mediating DNA repair pathway choice at replication-associated double-strand breaks.

    Georgieva, Daniela / Wang, Ning / Taglialatela, Angelo / Jerabek, Stepan / Reczek, Colleen R / Lim, Pei Xin / Sung, Julie / Du, Qian / Horiguchi, Michiko / Jasin, Maria / Ciccia, Alberto / Baer, Richard / Egli, Dieter

    Cell reports

    2024  Volume 43, Issue 4, Page(s) 114006

    Abstract: Reprogramming to pluripotency is associated with DNA damage and requires the functions of the BRCA1 tumor suppressor. Here, we leverage separation-of-function mutations in BRCA1/2 as well as the physical and/or genetic interactions between BRCA1 and its ... ...

    Abstract Reprogramming to pluripotency is associated with DNA damage and requires the functions of the BRCA1 tumor suppressor. Here, we leverage separation-of-function mutations in BRCA1/2 as well as the physical and/or genetic interactions between BRCA1 and its associated repair proteins to ascertain the relevance of homology-directed repair (HDR), stalled fork protection (SFP), and replication gap suppression (RGS) in somatic cell reprogramming. Surprisingly, loss of SFP and RGS is inconsequential for the transition to pluripotency. In contrast, cells deficient in HDR, but proficient in SFP and RGS, reprogram with reduced efficiency. Conversely, the restoration of HDR function through inactivation of 53bp1 rescues reprogramming in Brca1-deficient cells, and 53bp1 loss leads to elevated HDR and enhanced reprogramming in mouse and human cells. These results demonstrate that somatic cell reprogramming is especially dependent on repair of replication-associated double-strand breaks (DSBs) by the HDR activity of BRCA1 and BRCA2 and can be improved in the absence of 53BP1.
    MeSH term(s) Animals ; Humans ; Mice ; BRCA1 Protein/metabolism ; BRCA1 Protein/genetics ; Cellular Reprogramming ; DNA Breaks, Double-Stranded ; DNA Repair ; DNA Replication ; Recombinational DNA Repair ; Tumor Suppressor p53-Binding Protein 1/metabolism ; Tumor Suppressor p53-Binding Protein 1/genetics
    Chemical Substances BRCA1 Protein ; BRCA1 protein, human ; Brca1 protein, mouse ; TP53BP1 protein, human ; Trp53bp1 protein, mouse ; Tumor Suppressor p53-Binding Protein 1
    Language English
    Publishing date 2024-03-30
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
    ZDB-ID 2649101-1
    ISSN 2211-1247 ; 2211-1247
    ISSN (online) 2211-1247
    ISSN 2211-1247
    DOI 10.1016/j.celrep.2024.114006
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  9. Article ; Online: Inactive PARP1 causes embryonic lethality and genome instability in a dominant-negative manner.

    Shao, Zhengping / Lee, Brian J / Zhang, Hanwen / Lin, Xiaohui / Li, Chen / Jiang, Wenxia / Chirathivat, Napon / Gershik, Steven / Shen, Michael M / Baer, Richard / Zha, Shan

    Proceedings of the National Academy of Sciences of the United States of America

    2023  Volume 120, Issue 31, Page(s) e2301972120

    Abstract: PARP1 (poly-ADP ribose polymerase 1) is recruited and activated by DNA strand breaks, catalyzing the generation of poly-ADP-ribose (PAR) chains from NAD+. PAR relaxes chromatin and recruits other DNA repair factors, including XRCC1 and DNA Ligase 3, to ... ...

    Abstract PARP1 (poly-ADP ribose polymerase 1) is recruited and activated by DNA strand breaks, catalyzing the generation of poly-ADP-ribose (PAR) chains from NAD+. PAR relaxes chromatin and recruits other DNA repair factors, including XRCC1 and DNA Ligase 3, to maintain genomic stability. Here we show that, in contrast to the normal development of Parp1-null mice, heterozygous expression of catalytically inactive Parp1 (E988A,
    MeSH term(s) Female ; Pregnancy ; Animals ; Mice ; Causality ; Alleles ; Genotype ; Genomic Instability ; ADP-Ribosylation
    Language English
    Publishing date 2023-07-24
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.2301972120
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    Zs.A 1148: Show issues Location:
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  10. Article ; Online: MRN, CtIP, and BRCA1 mediate repair of topoisomerase II-DNA adducts.

    Aparicio, Tomas / Baer, Richard / Gottesman, Max / Gautier, Jean

    The Journal of cell biology

    2016  Volume 212, Issue 4, Page(s) 399–408

    Abstract: Repair of DNA double-strand breaks (DSBs) with complex ends poses a special challenge, as additional processing is required before DNA ligation. For example, protein-DNA adducts must be removed to allow repair by either nonhomologous end joining or ... ...

    Abstract Repair of DNA double-strand breaks (DSBs) with complex ends poses a special challenge, as additional processing is required before DNA ligation. For example, protein-DNA adducts must be removed to allow repair by either nonhomologous end joining or homology-directed repair. Here, we investigated the processing of topoisomerase II (Top2)-DNA adducts induced by treatment with the chemotherapeutic agent etoposide. Through biochemical analysis in Xenopus laevis egg extracts, we establish that the MRN (Mre11, Rad50, and Nbs1) complex, CtIP, and BRCA1 are required for both the removal of Top2-DNA adducts and the subsequent resection of Top2-adducted DSB ends. Moreover, the interaction between CtIP and BRCA1, although dispensable for resection of endonuclease-generated DSB ends, is required for resection of Top2-adducted DSBs, as well as for cellular resistance to etoposide during genomic DNA replication.
    MeSH term(s) Animals ; Antigens, Neoplasm/biosynthesis ; Antigens, Neoplasm/genetics ; Antigens, Neoplasm/metabolism ; BRCA1 Protein/genetics ; BRCA1 Protein/metabolism ; Carrier Proteins/genetics ; Carrier Proteins/metabolism ; DNA Adducts/genetics ; DNA Adducts/metabolism ; DNA Breaks, Double-Stranded ; DNA Repair ; DNA Repair Enzymes ; DNA Replication ; DNA Topoisomerases, Type II/biosynthesis ; DNA Topoisomerases, Type II/genetics ; DNA Topoisomerases, Type II/metabolism ; DNA-Binding Proteins/biosynthesis ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; Etoposide/pharmacology ; Female ; MRE11 Homologue Protein ; Multiprotein Complexes ; Time Factors ; Topoisomerase II Inhibitors/pharmacology ; Tumor Suppressor Proteins/genetics ; Tumor Suppressor Proteins/metabolism ; Xenopus Proteins/genetics ; Xenopus Proteins/metabolism ; Xenopus laevis
    Chemical Substances Antigens, Neoplasm ; BRCA1 Protein ; Carrier Proteins ; DNA Adducts ; DNA-Binding Proteins ; Mre11 protein, Xenopus ; Multiprotein Complexes ; NBN protein, Xenopus ; RBBP8 protein, Xenopus ; Rad50 protein, Xenopus ; Topoisomerase II Inhibitors ; Tumor Suppressor Proteins ; Xenopus Proteins ; Etoposide (6PLQ3CP4P3) ; MRE11 Homologue Protein (EC 3.1.-) ; DNA Topoisomerases, Type II (EC 5.99.1.3) ; DNA Repair Enzymes (EC 6.5.1.-)
    Language English
    Publishing date 2016-02-12
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Webcast
    ZDB-ID 218154-x
    ISSN 1540-8140 ; 0021-9525
    ISSN (online) 1540-8140
    ISSN 0021-9525
    DOI 10.1083/jcb.201504005
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