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  • Articles  (15)
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  • American Association for the Advancement of Science (AAAS)  (15)
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  • Articles  (15)
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  • American Association for the Advancement of Science (AAAS)  (15)
  • American Chemical Society
  • American Meteorological Society
  • Annual Reviews
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  • 2020-2023
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  • 1
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    A Tumor suppressor complex with GAP activity for the Rag GTPases that signal amino acid sufficiency to mTORC1 (2013)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2013-06-01
    Description: The mTOR complex 1 (mTORC1) pathway promotes cell growth in response to many cues, including amino acids, which act through the Rag guanosine triphosphatases (GTPases) to promote mTORC1 translocation to the lysosomal surface, its site of activation. Although progress has been made in identifying positive regulators of the Rags, it is unknown if negative factors also exist. Here, we identify GATOR as a complex that interacts with the Rags and is composed of two subcomplexes we call GATOR1 and -2. Inhibition of GATOR1 subunits (DEPDC5, Nprl2, and Nprl3) makes mTORC1 signaling resistant to amino acid deprivation. In contrast, inhibition of GATOR2 subunits (Mios, WDR24, WDR59, Seh1L, and Sec13) suppresses mTORC1 signaling, and epistasis analysis shows that GATOR2 negatively regulates DEPDC5. GATOR1 has GTPase-activating protein (GAP) activity for RagA and RagB, and its components are mutated in human cancer. In cancer cells with inactivating mutations in GATOR1, mTORC1 is hyperactive and insensitive to amino acid starvation, and such cells are hypersensitive to rapamycin, an mTORC1 inhibitor. Thus, we identify a key negative regulator of the Rag GTPases and reveal that, like other mTORC1 regulators, Rag function can be deregulated in cancer.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3728654/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3728654/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bar-Peled, Liron -- Chantranupong, Lynne -- Cherniack, Andrew D -- Chen, Walter W -- Ottina, Kathleen A -- Grabiner, Brian C -- Spear, Eric D -- Carter, Scott L -- Meyerson, Matthew -- Sabatini, David M -- AI47389/AI/NIAID NIH HHS/ -- CA103866/CA/NCI NIH HHS/ -- F31 CA180271/CA/NCI NIH HHS/ -- P30 CA014051/CA/NCI NIH HHS/ -- R01 CA103866/CA/NCI NIH HHS/ -- R01 CA129105/CA/NCI NIH HHS/ -- U24CA143867/CA/NCI NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2013 May 31;340(6136):1100-6. doi: 10.1126/science.1232044.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Whitehead Institute for Biomedical Research and Massachusetts Institute of Technology, Department of Biology, Cambridge, MA 02142, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23723238" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acids/*metabolism ; Carrier Proteins/antagonists & inhibitors/genetics/*metabolism ; Cell Line, Tumor ; GTPase-Activating Proteins ; HEK293 Cells ; Humans ; Lysosomes/*enzymology ; Monomeric GTP-Binding Proteins/*metabolism ; Multiprotein Complexes ; Mutation ; Neoplasms/*enzymology/genetics ; Nuclear Proteins/antagonists & inhibitors/genetics/metabolism ; Proteins/*metabolism ; RNA, Small Interfering/genetics ; TOR Serine-Threonine Kinases ; Tumor Suppressor Proteins/antagonists & inhibitors/genetics/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    Real-time dynamics of RNA polymerase II clustering in live human cells (2013)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2013-07-06
    Description: Transcription is reported to be spatially compartmentalized in nuclear transcription factories with clusters of RNA polymerase II (Pol II). However, little is known about when these foci assemble or their relative stability. We developed a quantitative single-cell approach to characterize protein spatiotemporal organization, with single-molecule sensitivity in live eukaryotic cells. We observed that Pol II clusters form transiently, with an average lifetime of 5.1 (+/- 0.4) seconds, which refutes the notion that they are statically assembled substructures. Stimuli affecting transcription yielded orders-of-magnitude changes in the dynamics of Pol II clusters, which implies that clustering is regulated and plays a role in the cell's ability to effect rapid response to external signals. Our results suggest that transient crowding of enzymes may aid in rate-limiting steps of gene regulation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cisse, Ibrahim I -- Izeddin, Ignacio -- Causse, Sebastien Z -- Boudarene, Lydia -- Senecal, Adrien -- Muresan, Leila -- Dugast-Darzacq, Claire -- Hajj, Bassam -- Dahan, Maxime -- Darzacq, Xavier -- New York, N.Y. -- Science. 2013 Aug 9;341(6146):664-7. doi: 10.1126/science.1239053. Epub 2013 Jul 4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Functional Imaging of Transcription, CNRS UMR8197, Ecole Normale Superieure, Institut de Biologie de l'ENS, IBENS, Paris, 75005 France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23828889" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Line, Tumor ; Flavonoids/pharmacology ; *Gene Expression Regulation ; Humans ; Piperidines/pharmacology ; RNA Polymerase II/*metabolism ; Single-Cell Analysis/methods ; Time Factors ; Transcription Elongation, Genetic/drug effects ; *Transcription, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    A secreted PTEN phosphatase that enters cells to alter signaling and survival (2013)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2013-06-08
    Description: Phosphatase and tensin homolog on chromosome ten (PTEN) is a tumor suppressor and an antagonist of the phosphoinositide-3 kinase (PI3K) pathway. We identified a 576-amino acid translational variant of PTEN, termed PTEN-Long, that arises from an alternative translation start site 519 base pairs upstream of the ATG initiation sequence, adding 173 N-terminal amino acids to the normal PTEN open reading frame. PTEN-Long is a membrane-permeable lipid phosphatase that is secreted from cells and can enter other cells. As an exogenous agent, PTEN-Long antagonized PI3K signaling and induced tumor cell death in vitro and in vivo. By providing a means to restore a functional tumor-suppressor protein to tumor cells, PTEN-Long may have therapeutic uses.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3935617/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3935617/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hopkins, Benjamin D -- Fine, Barry -- Steinbach, Nicole -- Dendy, Meaghan -- Rapp, Zachary -- Shaw, Jacquelyn -- Pappas, Kyrie -- Yu, Jennifer S -- Hodakoski, Cindy -- Mense, Sarah -- Klein, Joshua -- Pegno, Sarah -- Sulis, Maria-Luisa -- Goldstein, Hannah -- Amendolara, Benjamin -- Lei, Liang -- Maurer, Matthew -- Bruce, Jeffrey -- Canoll, Peter -- Hibshoosh, Hanina -- Parsons, Ramon -- 2T32 CA09503/CA/NCI NIH HHS/ -- CA082783/CA/NCI NIH HHS/ -- CA097403/CA/NCI NIH HHS/ -- P01 CA097403/CA/NCI NIH HHS/ -- R01 CA082783/CA/NCI NIH HHS/ -- R01 CA155117/CA/NCI NIH HHS/ -- R01 NS066955/NS/NINDS NIH HHS/ -- R01 NS073610/NS/NINDS NIH HHS/ -- R01NS066955/NS/NINDS NIH HHS/ -- T32 CA009503/CA/NCI NIH HHS/ -- T32 GM008224/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2013 Jul 26;341(6144):399-402. doi: 10.1126/science.1234907. Epub 2013 Jun 6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Oncological Sciences, Icahn School of Medicine at Mount Sinai, 1470 Madison Avenue, New York, NY 10029, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23744781" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Line, Tumor ; *Cell Survival ; Embryonic Stem Cells ; Glioblastoma/drug therapy/metabolism/pathology ; HEK293 Cells ; Humans ; Mice ; Mice, Nude ; Molecular Sequence Data ; Mutation ; PTEN Phosphohydrolase/*chemistry/genetics/*metabolism/pharmacology ; Peptide Chain Initiation, Translational ; Phosphatidylinositol 3-Kinase/*metabolism ; Phosphorylation ; Proto-Oncogene Proteins c-akt/metabolism ; RNA, Messenger/genetics/metabolism ; *Signal Transduction/drug effects ; Xenograft Model Antitumor Assays
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    Highly recurrent TERT promoter mutations in human melanoma (2013)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2013-01-26
    Description: Systematic sequencing of human cancer genomes has identified many recurrent mutations in the protein-coding regions of genes but rarely in gene regulatory regions. Here, we describe two independent mutations within the core promoter of telomerase reverse transcriptase (TERT), the gene coding for the catalytic subunit of telomerase, which collectively occur in 50 of 70 (71%) melanomas examined. These mutations generate de novo consensus binding motifs for E-twenty-six (ETS) transcription factors, and in reporter assays, the mutations increased transcriptional activity from the TERT promoter by two- to fourfold. Examination of 150 cancer cell lines derived from diverse tumor types revealed the same mutations in 24 cases (16%), with preliminary evidence of elevated frequency in bladder and hepatocellular cancer cells. Thus, somatic mutations in regulatory regions of the genome may represent an important tumorigenic mechanism.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4423787/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4423787/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huang, Franklin W -- Hodis, Eran -- Xu, Mary Jue -- Kryukov, Gregory V -- Chin, Lynda -- Garraway, Levi A -- DP2 OD002750/OD/NIH HHS/ -- DP2OD002750/OD/NIH HHS/ -- R33 CA126674/CA/NCI NIH HHS/ -- R33CA126674/CA/NCI NIH HHS/ -- T32 CA009172/CA/NCI NIH HHS/ -- T32 GM007753/GM/NIGMS NIH HHS/ -- T32GM07753/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2013 Feb 22;339(6122):957-9. doi: 10.1126/science.1229259. Epub 2013 Jan 24.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Broad Institute of Harvard and MIT, Cambridge, MA 02142, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23348506" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Carcinoma, Hepatocellular/genetics ; Cell Line, Tumor ; Cell Transformation, Neoplastic ; *Gene Expression Regulation, Neoplastic ; Humans ; Liver Neoplasms/genetics ; Melanoma/*genetics ; *Mutation ; *Promoter Regions, Genetic ; Proto-Oncogene Proteins c-ets/metabolism ; Telomerase/chemistry/*genetics/metabolism ; Transcription, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    Lenalidomide causes selective degradation of IKZF1 and IKZF3 in multiple myeloma cells (2013)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2013-12-03
    Description: Lenalidomide is a drug with clinical efficacy in multiple myeloma and other B cell neoplasms, but its mechanism of action is unknown. Using quantitative proteomics, we found that lenalidomide causes selective ubiquitination and degradation of two lymphoid transcription factors, IKZF1 and IKZF3, by the CRBN-CRL4 ubiquitin ligase. IKZF1 and IKZF3 are essential transcription factors in multiple myeloma. A single amino acid substitution of IKZF3 conferred resistance to lenalidomide-induced degradation and rescued lenalidomide-induced inhibition of cell growth. Similarly, we found that lenalidomide-induced interleukin-2 production in T cells is due to depletion of IKZF1 and IKZF3. These findings reveal a previously unknown mechanism of action for a therapeutic agent: alteration of the activity of an E3 ubiquitin ligase, leading to selective degradation of specific targets.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4077049/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4077049/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kronke, Jan -- Udeshi, Namrata D -- Narla, Anupama -- Grauman, Peter -- Hurst, Slater N -- McConkey, Marie -- Svinkina, Tanya -- Heckl, Dirk -- Comer, Eamon -- Li, Xiaoyu -- Ciarlo, Christie -- Hartman, Emily -- Munshi, Nikhil -- Schenone, Monica -- Schreiber, Stuart L -- Carr, Steven A -- Ebert, Benjamin L -- P01 CA078378/CA/NCI NIH HHS/ -- P01 CA108631/CA/NCI NIH HHS/ -- P01 CA155258/CA/NCI NIH HHS/ -- P50 CA100707/CA/NCI NIH HHS/ -- R01 HL082945/HL/NHLBI NIH HHS/ -- R01HL082945/HL/NHLBI NIH HHS/ -- RL1- HG004671/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 2014 Jan 17;343(6168):301-5. doi: 10.1126/science.1244851. Epub 2013 Nov 29.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Brigham and Women's Hospital, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24292625" target="_blank"〉PubMed〈/a〉
    Keywords: Antineoplastic Agents/*pharmacology ; Cell Line, Tumor ; HEK293 Cells ; Humans ; Ikaros Transcription Factor/genetics/*metabolism ; Interleukin-2/biosynthesis ; Multiple Myeloma/*metabolism ; Proteolysis ; T-Lymphocytes/drug effects/metabolism ; Thalidomide/*analogs & derivatives/pharmacology ; Ubiquitination
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
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  • 6
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    Tight coordination of protein translation and HSF1 activation supports the anabolic malignant state (2013)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2013-07-23
    Description: The ribosome is centrally situated to sense metabolic states, but whether its activity, in turn, coherently rewires transcriptional responses is unknown. Here, through integrated chemical-genetic analyses, we found that a dominant transcriptional effect of blocking protein translation in cancer cells was inactivation of heat shock factor 1 (HSF1), a multifaceted transcriptional regulator of the heat-shock response and many other cellular processes essential for anabolic metabolism, cellular proliferation, and tumorigenesis. These analyses linked translational flux to the regulation of HSF1 transcriptional activity and to the modulation of energy metabolism. Targeting this link with translation initiation inhibitors such as rocaglates deprived cancer cells of their energy and chaperone armamentarium and selectively impaired the proliferation of both malignant and premalignant cells with early-stage oncogenic lesions.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3959726/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3959726/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Santagata, Sandro -- Mendillo, Marc L -- Tang, Yun-chi -- Subramanian, Aravind -- Perley, Casey C -- Roche, Stephane P -- Wong, Bang -- Narayan, Rajiv -- Kwon, Hyoungtae -- Koeva, Martina -- Amon, Angelika -- Golub, Todd R -- Porco, John A Jr -- Whitesell, Luke -- Lindquist, Susan -- 5U54HG006093/HG/NHGRI NIH HHS/ -- K08 NS064168/NS/NINDS NIH HHS/ -- K08NS064168/NS/NINDS NIH HHS/ -- R01 CA175744/CA/NCI NIH HHS/ -- R01 CA175744-01/CA/NCI NIH HHS/ -- R01 GM073855/GM/NIGMS NIH HHS/ -- R03 DA027713/DA/NIDA NIH HHS/ -- R03 DA027713-01/DA/NIDA NIH HHS/ -- R03 MH086465-01/MH/NIMH NIH HHS/ -- U54 HG006093/HG/NHGRI NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2013 Jul 19;341(6143):1238303. doi: 10.1126/science.1238303.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Brigham and Women's Hospital, and Harvard Medical School, Boston, MA 02215, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23869022" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antineoplastic Agents/chemistry/isolation & purification/pharmacology ; Benzofurans/pharmacology ; Cell Line, Tumor ; Cell Proliferation ; Cell Transformation, Neoplastic/drug effects/metabolism/pathology ; DNA-Binding Proteins/antagonists & inhibitors/*biosynthesis ; Energy Metabolism/drug effects ; Gene Expression Regulation, Neoplastic ; High-Throughput Screening Assays ; Humans ; Mice ; NIH 3T3 Cells ; Neoplasm Transplantation ; Neoplasms/genetics/*metabolism/*pathology ; Protein Biosynthesis/drug effects/genetics/*physiology ; Ribosomes/drug effects/*metabolism ; Transcription Factors/antagonists & inhibitors/*biosynthesis
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
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  • 7
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    Latency-associated degradation of the MRP1 drug transporter during latent human cytomegalovirus infection (2013)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2013-04-13
    Description: The reactivation of latent human cytomegalovirus (HCMV) infection after transplantation is associated with high morbidity and mortality. In vivo, myeloid cells and their progenitors are an important site of HCMV latency, whose establishment and/or maintenance require expression of the viral transcript UL138. Using stable isotope labeling by amino acids in cell culture-based mass spectrometry, we found a dramatic UL138-mediated loss of cell surface multidrug resistance-associated protein-1 (MRP1) and the reduction of substrate export by this transporter. Latency-associated loss of MRP1 and accumulation of the cytotoxic drug vincristine, an MRP1 substrate, depleted virus from naturally latent CD14(+) and CD34(+) progenitors, all of which are in vivo sites of latency. The UL138-mediated loss of MRP1 provides a marker for detecting latent HCMV infection and a therapeutic target for eliminating latently infected cells before transplantation.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3683642/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3683642/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weekes, Michael P -- Tan, Shireen Y L -- Poole, Emma -- Talbot, Suzanne -- Antrobus, Robin -- Smith, Duncan L -- Montag, Christina -- Gygi, Steven P -- Sinclair, John H -- Lehner, Paul J -- 084957/Wellcome Trust/United Kingdom -- 084957/Z/08/Z/Wellcome Trust/United Kingdom -- 093966/Wellcome Trust/United Kingdom -- 093966/Z/10/Z/Wellcome Trust/United Kingdom -- 100140/Wellcome Trust/United Kingdom -- G0701279/Medical Research Council/United Kingdom -- New York, N.Y. -- Science. 2013 Apr 12;340(6129):199-202. doi: 10.1126/science.1235047.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cambridge Institute for Medical Research, University of Cambridge, Cambridge, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23580527" target="_blank"〉PubMed〈/a〉
    Keywords: Antigens, CD34/analysis ; Cell Line, Tumor ; Cytomegalovirus/genetics/*physiology ; Cytomegalovirus Infections/*metabolism/*virology ; Dendritic Cells/physiology ; Down-Regulation ; Humans ; Lysosomes/metabolism ; Monocyte-Macrophage Precursor Cells/metabolism/virology ; Monocytes/metabolism/virology ; Multidrug Resistance-Associated Proteins/genetics/*metabolism ; Vincristine/metabolism/pharmacology ; Viral Proteins/*metabolism ; *Virus Latency
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
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    (R)-2-hydroxyglutarate is sufficient to promote leukemogenesis and its effects are reversible (2013)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2013-02-09
    Description: Mutations in IDH1 and IDH2, the genes coding for isocitrate dehydrogenases 1 and 2, are common in several human cancers, including leukemias, and result in overproduction of the (R)-enantiomer of 2-hydroxyglutarate [(R)-2HG]. Elucidation of the role of IDH mutations and (R)-2HG in leukemogenesis has been hampered by a lack of appropriate cell-based models. Here, we show that a canonical IDH1 mutant, IDH1 R132H, promotes cytokine independence and blocks differentiation in hematopoietic cells. These effects can be recapitulated by (R)-2HG, but not (S)-2HG, despite the fact that (S)-2HG more potently inhibits enzymes, such as the 5'-methylcytosine hydroxylase TET2, that have previously been linked to the pathogenesis of IDH mutant tumors. We provide evidence that this paradox relates to the ability of (S)-2HG, but not (R)-2HG, to inhibit the EglN prolyl hydroxylases. Additionally, we show that transformation by (R)-2HG is reversible.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3836459/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3836459/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Losman, Julie-Aurore -- Looper, Ryan E -- Koivunen, Peppi -- Lee, Sungwoo -- Schneider, Rebekka K -- McMahon, Christine -- Cowley, Glenn S -- Root, David E -- Ebert, Benjamin L -- Kaelin, William G Jr -- P30 DK049216/DK/NIDDK NIH HHS/ -- R01 CA068490/CA/NCI NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2013 Mar 29;339(6127):1621-5. doi: 10.1126/science.1231677. Epub 2013 Feb 7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medical Oncology, Dana-Farber Cancer Institute, Boston, MA 02215, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23393090" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Line, Tumor ; Cell Transformation, Neoplastic/genetics/*metabolism ; Glutarates/*metabolism ; *Hematopoiesis ; Humans ; Isocitrate Dehydrogenase/genetics/*metabolism ; Leukemia/*enzymology/genetics ; Models, Biological ; Procollagen-Proline Dioxygenase/*antagonists & inhibitors
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 9
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    Monitoring drug target engagement in cells and tissues using the cellular thermal shift assay (2013)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2013-07-06
    Description: The efficacy of therapeutics is dependent on a drug binding to its cognate target. Optimization of target engagement by drugs in cells is often challenging, because drug binding cannot be monitored inside cells. We have developed a method for evaluating drug binding to target proteins in cells and tissue samples. This cellular thermal shift assay (CETSA) is based on the biophysical principle of ligand-induced thermal stabilization of target proteins. Using this assay, we validated drug binding for a set of important clinical targets and monitored processes of drug transport and activation, off-target effects and drug resistance in cancer cell lines, as well as drug distribution in tissues. CETSA is likely to become a valuable tool for the validation and optimization of drug target engagement.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Martinez Molina, Daniel -- Jafari, Rozbeh -- Ignatushchenko, Marina -- Seki, Takahiro -- Larsson, E Andreas -- Dan, Chen -- Sreekumar, Lekshmy -- Cao, Yihai -- Nordlund, Par -- New York, N.Y. -- Science. 2013 Jul 5;341(6141):84-7. doi: 10.1126/science.1233606.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medical Biochemistry and Biophysics, Karolinska Institute, Stockholm, Sweden.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23828940" target="_blank"〉PubMed〈/a〉
    Keywords: Antimetabolites, Antineoplastic/metabolism ; Cell Line, Tumor ; Dose-Response Relationship, Drug ; Drug Monitoring/*methods ; Folic Acid Antagonists/metabolism ; *Hot Temperature ; Humans ; Kidney/metabolism ; Ligands ; Liver/metabolism ; *Molecular Targeted Therapy ; Pharmaceutical Preparations/*metabolism ; Protein Binding ; Protein Stability ; Proteins/*metabolism ; Quinazolines/metabolism ; Thiophenes/metabolism ; Tissue Distribution
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
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    Autonomic nerve development contributes to prostate cancer progression (2013)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2013-07-13
    Description: Nerves are a common feature of the microenvironment, but their role in tumor growth and progression remains unclear. We found that the formation of autonomic nerve fibers in the prostate gland regulates prostate cancer development and dissemination in mouse models. The early phases of tumor development were prevented by chemical or surgical sympathectomy and by genetic deletion of stromal beta2- and beta3-adrenergic receptors. Tumors were also infiltrated by parasympathetic cholinergic fibers that promoted cancer dissemination. Cholinergic-induced tumor invasion and metastasis were inhibited by pharmacological blockade or genetic disruption of the stromal type 1 muscarinic receptor, leading to improved survival of the mice. A retrospective blinded analysis of prostate adenocarcinoma specimens from 43 patients revealed that the densities of sympathetic and parasympathetic nerve fibers in tumor and surrounding normal tissue, respectively, were associated with poor clinical outcomes. These findings may lead to novel therapeutic approaches for prostate cancer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Magnon, Claire -- Hall, Simon J -- Lin, Juan -- Xue, Xiaonan -- Gerber, Leah -- Freedland, Stephen J -- Frenette, Paul S -- DK056638/DK/NIDDK NIH HHS/ -- HL069438/HL/NHLBI NIH HHS/ -- HL097819/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 2013 Jul 12;341(6142):1236361. doi: 10.1126/science.1236361.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Ruth L. and David S. Gottesman Institute for Stem Cell and Regenerative Medicine Research, Albert Einstein College of Medicine, Bronx, NY 10461, USA. clairemagnon@free.fr〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23846904" target="_blank"〉PubMed〈/a〉
    Keywords: Adenocarcinoma/*pathology ; Adrenergic Fibers/physiology ; Animals ; Autonomic Nervous System/*growth & development ; Cell Line, Tumor ; Cell Transformation, Neoplastic/pathology ; Cholinergic Fibers/physiology ; Disease Progression ; Genes, myc/genetics ; Humans ; Male ; Mice ; Mice, Transgenic ; Neoplasm Invasiveness ; Neoplasm Transplantation ; Nerve Net/pathology/physiology ; *Neurogenesis ; Parasympathetic Nervous System/growth & development ; Promoter Regions, Genetic ; Prostate/*innervation/*pathology ; Prostatic Neoplasms/*pathology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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