ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

X
feed icon rss

Your email was sent successfully. Check your inbox.

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

Proceed reservation?

Export
Filter
  • Malaysia
  • OBIS
  • Oceanography
  • Phosphorylation
  • American Association for the Advancement of Science (AAAS)  (28)
  • UNESCO
  • 2020-2023
  • 2010-2014  (28)
  • 2000-2004
  • 1995-1999
  • 1975-1979
  • 2010  (28)
Collection
Keywords
Publisher
Years
  • 2020-2023
  • 2010-2014  (28)
  • 2000-2004
  • 1995-1999
  • 1975-1979
Year
  • 1
    facet.materialart.
    Unknown
    The substrate of Greatwall kinase, Arpp19, controls mitosis by inhibiting protein phosphatase 2A (2010)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2010-12-18
    Description: Initiation and maintenance of mitosis require the activation of protein kinase cyclin B-Cdc2 and the inhibition of protein phosphatase 2A (PP2A), which, respectively, phosphorylate and dephosphorylate mitotic substrates. The protein kinase Greatwall (Gwl) is required to maintain mitosis through PP2A inhibition. We describe how Gwl activation results in PP2A inhibition. We identified cyclic adenosine monophosphate-regulated phosphoprotein 19 (Arpp19) and alpha-Endosulfine as two substrates of Gwl that, when phosphorylated by this kinase, associate with and inhibit PP2A, thus promoting mitotic entry. Conversely, in the absence of Gwl activity, Arpp19 and alpha-Endosulfine are dephosphorylated and lose their capacity to bind and inhibit PP2A. Although both proteins can inhibit PP2A, endogenous Arpp19, but not alpha-Endosulfine, is responsible for PP2A inhibition at mitotic entry in Xenopus egg extracts.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gharbi-Ayachi, Aicha -- Labbe, Jean-Claude -- Burgess, Andrew -- Vigneron, Suzanne -- Strub, Jean-Marc -- Brioudes, Estelle -- Van-Dorsselaer, Alain -- Castro, Anna -- Lorca, Thierry -- New York, N.Y. -- Science. 2010 Dec 17;330(6011):1673-7. doi: 10.1126/science.1197048.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Universites Montpellier 2 et 1, Centre de Recherche de Biochimie Macromoleculaire, CNRS UMR 5237, IFR 122, 1919 Route de Mende, 34293 Montpellier cedex 5, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21164014" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; HeLa Cells ; Humans ; Interphase ; *Mitosis ; Molecular Sequence Data ; Oocytes ; Peptides/chemistry/*metabolism ; Phosphoproteins/chemistry/*metabolism ; Phosphorylation ; Protein Binding ; Protein Phosphatase 2/*antagonists & inhibitors/metabolism ; Protein-Serine-Threonine Kinases/*metabolism ; Proto-Oncogene Proteins c-mos/metabolism ; Recombinant Fusion Proteins/metabolism ; Xenopus Proteins/antagonists & inhibitors/*metabolism ; Xenopus laevis
    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)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 2
    facet.materialart.
    Unknown
    Cell biology. Enforcing the Greatwall in mitosis (2010)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2010-12-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Virshup, David M -- Kaldis, Philipp -- New York, N.Y. -- Science. 2010 Dec 17;330(6011):1638-9. doi: 10.1126/science.1199898.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Program in Cancer and Stem Cell Biology, Duke-National University of Singapore Graduate Medical School, Singapore 169857, Republic of Singapore. david.virshup@duke-nus.edu.sg〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21164006" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; CDC2 Protein Kinase/*metabolism ; Feedback, Physiological ; Humans ; *Mitosis ; Peptides/metabolism ; Phosphoproteins/metabolism ; Phosphorylation ; Protein Phosphatase 2/*antagonists & inhibitors/metabolism ; Protein-Serine-Threonine Kinases/*metabolism ; *Signal Transduction ; Xenopus Proteins/*metabolism
    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)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 3
    facet.materialart.
    Unknown
    Greatwall phosphorylates an inhibitor of protein phosphatase 2A that is essential for mitosis (2010)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2010-12-18
    Description: Entry into mitosis in eukaryotes requires the activity of cyclin-dependent kinase 1 (Cdk1). Cdk1 is opposed by protein phosphatases in two ways: They inhibit activation of Cdk1 by dephosphorylating the protein kinases Wee1 and Myt1 and the protein phosphatase Cdc25 (key regulators of Cdk1), and they also antagonize Cdk1's own phosphorylation of downstream targets. A particular form of protein phosphatase 2A (PP2A) containing a B55delta subunit (PP2A- B55delta) is the major protein phosphatase that acts on model CDK substrates in Xenopus egg extracts and has antimitotic activity. The activity of PP2A-B55delta is high in interphase and low in mitosis, exactly opposite that of Cdk1. We report that inhibition of PP2A-B55delta results from a small protein, known as alpha-endosulfine (Ensa), that is phosphorylated in mitosis by the protein kinase Greatwall (Gwl). This converts Ensa into a potent and specific inhibitor of PP2A-B55delta. This pathway represents a previously unknown element in the control of mitosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mochida, Satoru -- Maslen, Sarah L -- Skehel, Mark -- Hunt, Tim -- New York, N.Y. -- Science. 2010 Dec 17;330(6011):1670-3. doi: 10.1126/science.1195689.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cancer Research UK, London Research Institute, Clare Hall Laboratories, South Mimms, Herts EN6 3LD, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21164013" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; CDC2 Protein Kinase/metabolism ; Cell Cycle ; Interphase ; *Mitosis ; Mutant Proteins/metabolism ; Oocytes/metabolism ; Peptides/*metabolism ; Phosphoproteins/*metabolism ; Phosphorylation ; Protein Phosphatase 2/*antagonists & inhibitors/metabolism ; Protein-Serine-Threonine Kinases/*metabolism ; Serine/metabolism ; Xenopus Proteins/antagonists & inhibitors/*metabolism ; Xenopus laevis
    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)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 4
    facet.materialart.
    Unknown
    Alleviating neuropathic pain hypersensitivity by inhibiting PKMzeta in the anterior cingulate cortex (2010)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2010-12-04
    Description: Synaptic plasticity is a key mechanism for chronic pain. It occurs at different levels of the central nervous system, including spinal cord and cortex. Studies have mainly focused on signaling proteins that trigger these plastic changes, whereas few have addressed the maintenance of plastic changes related to chronic pain. We found that protein kinase M zeta (PKMzeta) maintains pain-induced persistent changes in the mouse anterior cingulate cortex (ACC). Peripheral nerve injury caused activation of PKMzeta in the ACC, and inhibiting PKMzeta by a selective inhibitor, zeta-pseudosubstrate inhibitory peptide (ZIP), erased synaptic potentiation. Microinjection of ZIP into the ACC blocked behavioral sensitization. These results suggest that PKMzeta in the ACC acts to maintain neuropathic pain. PKMzeta could thus be a new therapeutic target for treating chronic pain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, Xiang-Yao -- Ko, Hyoung-Gon -- Chen, Tao -- Descalzi, Giannina -- Koga, Kohei -- Wang, Hansen -- Kim, Susan S -- Shang, Yuze -- Kwak, Chuljung -- Park, Soo-Won -- Shim, Jaehoon -- Lee, Kyungmin -- Collingridge, Graham L -- Kaang, Bong-Kiun -- Zhuo, Min -- CIHR66975/Canadian Institutes of Health Research/Canada -- CIHR84256/Canadian Institutes of Health Research/Canada -- G0601813/Medical Research Council/United Kingdom -- Medical Research Council/United Kingdom -- New York, N.Y. -- Science. 2010 Dec 3;330(6009):1400-4. doi: 10.1126/science.1191792.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, Faculty of Medicine, Center for the Study of Pain, University of Toronto, 1 King's College Circle, Toronto, Ontario M5S 1A8, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21127255" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclases/genetics/metabolism ; Analgesics/administration & dosage/pharmacology ; Animals ; Enzyme Inhibitors/administration & dosage/*pharmacology ; Excitatory Postsynaptic Potentials/drug effects ; Gyrus Cinguli/*enzymology/physiology ; Long-Term Potentiation ; Male ; Memory/drug effects ; Mice ; Mice, Inbred C57BL ; Mice, Transgenic ; Neuralgia/*drug therapy/*enzymology ; Patch-Clamp Techniques ; Peptides/administration & dosage/*pharmacology ; Peroneal Nerve/injuries ; Phosphorylation ; Protein Kinase C/*antagonists & inhibitors/*metabolism ; Receptors, AMPA/metabolism ; Sensory Receptor Cells/physiology ; Somatosensory Cortex/physiology ; Synapses/physiology ; Synaptic Transmission
    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)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 5
    facet.materialart.
    Unknown
    Cell biology. Puzzled by PML (2010)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2010-11-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Culjkovic-Kraljacic, Bijana -- Borden, Katherine L B -- R01 CA080728/CA/NCI NIH HHS/ -- R01 CA098571/CA/NCI NIH HHS/ -- Canadian Institutes of Health Research/Canada -- New York, N.Y. -- Science. 2010 Nov 26;330(6008):1183-4. doi: 10.1126/science.1199405.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Research in Immunology and Cancer, Department of Pathology and Cell Biology, Universite de Montreal, Pavillion Marcelle-Coutu, Chemin Polytechnique, Montreal, QC, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21109655" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Apoptosis ; Calcium/*metabolism ; *Calcium Signaling ; Endoplasmic Reticulum/*metabolism ; Inositol 1,4,5-Trisphosphate/metabolism ; Inositol 1,4,5-Trisphosphate Receptors/metabolism ; Intranuclear Space/metabolism ; Mice ; Mitochondria/metabolism ; Nuclear Proteins/*metabolism ; Phosphorylation ; Protein Isoforms/metabolism ; Transcription Factors/*metabolism ; Tumor Suppressor Proteins/*metabolism
    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)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 6
    facet.materialart.
    Unknown
    PML regulates apoptosis at endoplasmic reticulum by modulating calcium release (2010)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2010-10-30
    Description: The promyelocytic leukemia (PML) tumor suppressor is a pleiotropic modulator of apoptosis. However, the molecular basis for such a diverse proapoptotic role is currently unknown. We show that extranuclear Pml was specifically enriched at the endoplasmic reticulum (ER) and at the mitochondria-associated membranes, signaling domains involved in ER-to-mitochondria calcium ion (Ca(2+)) transport and in induction of apoptosis. We found Pml in complexes of large molecular size with the inositol 1,4,5-trisphosphate receptor (IP(3)R), protein kinase Akt, and protein phosphatase 2a (PP2a). Pml was essential for Akt- and PP2a-dependent modulation of IP(3)R phosphorylation and in turn for IP(3)R-mediated Ca(2+) release from ER. Our findings provide a mechanistic explanation for the pleiotropic role of Pml in apoptosis and identify a pharmacological target for the modulation of Ca(2+) signals.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3017677/" 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/PMC3017677/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Giorgi, Carlotta -- Ito, Keisuke -- Lin, Hui-Kuan -- Santangelo, Clara -- Wieckowski, Mariusz R -- Lebiedzinska, Magdalena -- Bononi, Angela -- Bonora, Massimo -- Duszynski, Jerzy -- Bernardi, Rosa -- Rizzuto, Rosario -- Tacchetti, Carlo -- Pinton, Paolo -- Pandolfi, Pier Paolo -- GGP05284/Telethon/Italy -- K99 CA139009/CA/NCI NIH HHS/ -- K99 CA139009-01A1/CA/NCI NIH HHS/ -- K99 CA139009-02/CA/NCI NIH HHS/ -- R01 CA071692/CA/NCI NIH HHS/ -- R01 CA071692-04S1/CA/NCI NIH HHS/ -- R01 CA102142/CA/NCI NIH HHS/ -- R01 CA102142-07/CA/NCI NIH HHS/ -- R01 CA142874/CA/NCI NIH HHS/ -- R01 CA142874-01/CA/NCI NIH HHS/ -- R01 CA142874-02/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2010 Nov 26;330(6008):1247-51. doi: 10.1126/science.1189157. Epub 2010 Oct 28.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Experimental and Diagnostic Medicine, Section of General Pathology, Interdisciplinary Center for the Study of Inflammation (ICSI), Emilia Romagna Laboratory BioPharmaNet, and Laboratory for Technologies of Advanced Therapies (LTTA) University of Ferrara, Ferrara, Italy.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21030605" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Animals ; *Apoptosis ; Calcium/*metabolism ; *Calcium Signaling ; Cell Line ; Cell Nucleus/metabolism ; Cells, Cultured ; Cytosol/metabolism ; Endoplasmic Reticulum/*metabolism ; Homeostasis ; Humans ; Inositol 1,4,5-Trisphosphate/metabolism ; Inositol 1,4,5-Trisphosphate Receptors/metabolism ; Intracellular Membranes/metabolism ; Mice ; Mitochondria/metabolism ; Nuclear Proteins/genetics/*metabolism ; Phosphorylation ; Protein Phosphatase 2/metabolism ; Proto-Oncogene Proteins c-akt/metabolism ; Recombinant Fusion Proteins/metabolism ; Stress, Physiological ; Transcription Factors/genetics/*metabolism ; Tumor Suppressor Proteins/genetics/*metabolism
    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)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 7
    facet.materialart.
    Unknown
    Molecular biology. Surfing chromosomes (and Survivin) (2010)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2010-10-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Musacchio, Andrea -- New York, N.Y. -- Science. 2010 Oct 8;330(6001):183-4. doi: 10.1126/science.1197261.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Experimental Oncology, European Institute of Oncology, Via Adamello 16, I-20139 Milan, Italy. andrea.musacchio@ifom-ieo-campus.it〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20929762" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Aurora Kinases ; Autoantigens/metabolism ; Cell Cycle Proteins/metabolism ; Centromere/enzymology/*metabolism ; Chromosomal Proteins, Non-Histone/metabolism ; Chromosome Segregation ; Chromosomes/metabolism ; Chromosomes, Fungal/metabolism ; Chromosomes, Human/metabolism ; Histones/*metabolism ; Humans ; Inhibitor of Apoptosis Proteins ; Intracellular Signaling Peptides and Proteins/*metabolism ; Kinesin/metabolism ; Kinetochores/metabolism/physiology ; Microtubule-Associated Proteins/*metabolism ; *Mitosis ; Phosphorylation ; Protein-Serine-Threonine Kinases/*metabolism ; Schizosaccharomyces/metabolism ; Schizosaccharomyces pombe Proteins/metabolism
    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)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 8
    facet.materialart.
    Unknown
    Two histone marks establish the inner centromere and chromosome bi-orientation (2010)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2010-10-12
    Description: For proper partitioning of chromosomes in mitosis, the chromosomal passenger complex (CPC) including Aurora B and survivin must be localized at the center of paired kinetochores, at the site called the inner centromere. It is largely unknown what defines the inner centromere and how the CPC is targeted to this site. Here, we show that the phosphorylation of histone H3-threonine 3 (H3-pT3) mediated by Haspin cooperates with Bub1-mediated histone 2A-serine 121 (H2A-S121) phosphorylation in targeting the CPC to the inner centromere in fission yeast and human cells. H3-pT3 promotes nucleosome binding of survivin, whereas phosphorylated H2A-S121 facilitates the binding of shugoshin, the centromeric CPC adaptor. Haspin colocalizes with cohesin by associating with Pds5, whereas Bub1 localizes at kinetochores. Thus, the inner centromere is defined by intersection of two histone kinases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yamagishi, Yuya -- Honda, Takashi -- Tanno, Yuji -- Watanabe, Yoshinori -- New York, N.Y. -- Science. 2010 Oct 8;330(6001):239-43. doi: 10.1126/science.1194498.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Chromosome Dynamics, Institute of Molecular and Cellular Biosciences, University of Tokyo, Yayoi, Tokyo 113-0032, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20929775" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Aurora Kinase B ; Aurora Kinases ; Cell Cycle Proteins/metabolism ; Centromere/*metabolism ; Chromatin/metabolism ; Chromosomal Proteins, Non-Histone/metabolism ; Chromosome Segregation ; Chromosomes, Fungal/*physiology ; Chromosomes, Human/*physiology ; HeLa Cells ; Heterochromatin/metabolism ; Histones/*metabolism ; Humans ; Inhibitor of Apoptosis Proteins ; Intracellular Signaling Peptides and Proteins/chemistry/genetics/*metabolism ; Kinetochores/metabolism ; Microtubule-Associated Proteins/metabolism ; Mitosis ; Molecular Sequence Data ; Mutation ; Nucleosomes/metabolism ; Phosphorylation ; Protein Binding ; Protein Interaction Domains and Motifs ; Protein-Serine-Threonine Kinases/chemistry/genetics/*metabolism ; Schizosaccharomyces/*genetics/metabolism ; Schizosaccharomyces pombe Proteins/genetics/*metabolism ; Serine/metabolism ; Threonine/metabolism
    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)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 9
    facet.materialart.
    Unknown
    Evidence for an alternative glycolytic pathway in rapidly proliferating cells (2010)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2010-09-18
    Description: Proliferating cells, including cancer cells, require altered metabolism to efficiently incorporate nutrients such as glucose into biomass. The M2 isoform of pyruvate kinase (PKM2) promotes the metabolism of glucose by aerobic glycolysis and contributes to anabolic metabolism. Paradoxically, decreased pyruvate kinase enzyme activity accompanies the expression of PKM2 in rapidly dividing cancer cells and tissues. We demonstrate that phosphoenolpyruvate (PEP), the substrate for pyruvate kinase in cells, can act as a phosphate donor in mammalian cells because PEP participates in the phosphorylation of the glycolytic enzyme phosphoglycerate mutase (PGAM1) in PKM2-expressing cells. We used mass spectrometry to show that the phosphate from PEP is transferred to the catalytic histidine (His11) on human PGAM1. This reaction occurred at physiological concentrations of PEP and produced pyruvate in the absence of PKM2 activity. The presence of histidine-phosphorylated PGAM1 correlated with the expression of PKM2 in cancer cell lines and tumor tissues. Thus, decreased pyruvate kinase activity in PKM2-expressing cells allows PEP-dependent histidine phosphorylation of PGAM1 and may provide an alternate glycolytic pathway that decouples adenosine triphosphate production from PEP-mediated phosphotransfer, allowing for the high rate of glycolysis to support the anabolic metabolism observed in many proliferating cells.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3030121/" 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/PMC3030121/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vander Heiden, Matthew G -- Locasale, Jason W -- Swanson, Kenneth D -- Sharfi, Hadar -- Heffron, Greg J -- Amador-Noguez, Daniel -- Christofk, Heather R -- Wagner, Gerhard -- Rabinowitz, Joshua D -- Asara, John M -- Cantley, Lewis C -- 1K08CA136983/CA/NCI NIH HHS/ -- 1P01CA120964-01A/CA/NCI NIH HHS/ -- 5 T32 CA009361-28/CA/NCI NIH HHS/ -- 5P30CA006516-43/CA/NCI NIH HHS/ -- K08 CA136983/CA/NCI NIH HHS/ -- K08 CA136983-02/CA/NCI NIH HHS/ -- P01 CA089021/CA/NCI NIH HHS/ -- P01 CA089021-10/CA/NCI NIH HHS/ -- P01 CA120964/CA/NCI NIH HHS/ -- P01 CA120964-01A1/CA/NCI NIH HHS/ -- P01 GM047467/GM/NIGMS NIH HHS/ -- P01 GM047467-20/GM/NIGMS NIH HHS/ -- P01CA089021/CA/NCI NIH HHS/ -- P01GM047467/GM/NIGMS NIH HHS/ -- P30 CA006516/CA/NCI NIH HHS/ -- P30 CA006516-43S1/CA/NCI NIH HHS/ -- R01 AI078063/AI/NIAID NIH HHS/ -- R01 GM056203/GM/NIGMS NIH HHS/ -- R01-GM56302/GM/NIGMS NIH HHS/ -- R21 CA128620/CA/NCI NIH HHS/ -- R21/R33 DK070299/DK/NIDDK NIH HHS/ -- R33 DK070299/DK/NIDDK NIH HHS/ -- R33 DK070299-03/DK/NIDDK NIH HHS/ -- T32 CA009172/CA/NCI NIH HHS/ -- T32 CA009361/CA/NCI NIH HHS/ -- T32 CA009361-28/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2010 Sep 17;329(5998):1492-9. doi: 10.1126/science.1188015.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Dana Farber Cancer Institute, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20847263" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Animals ; Cell Line ; Cell Line, Tumor ; *Cell Proliferation ; Female ; Glucose/*metabolism ; Glyceric Acids/metabolism ; *Glycolysis ; Histidine/metabolism ; Humans ; Isoenzymes/metabolism ; Kinetics ; Male ; Mammary Neoplasms, Animal/metabolism ; Mice ; Neoplasms/*metabolism/pathology ; Phosphoenolpyruvate/metabolism ; Phosphoglycerate Mutase/*metabolism ; Phosphopyruvate Hydratase/metabolism ; Phosphorylation ; Prostatic Neoplasms/metabolism ; Pyruvate Kinase/*metabolism ; Pyruvic Acid/metabolism ; Recombinant Proteins/metabolism
    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)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 10
    facet.materialart.
    Unknown
    Transcription. Targeting the core of transcription (2010)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2010-09-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hardie, D Grahame -- New York, N.Y. -- Science. 2010 Sep 3;329(5996):1158-9. doi: 10.1126/science.1195447.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉College of Life Science, University of Dundee, Dow Street, Dundee DD1 5EH, Scotland, UK. d.g.hardie@dundee.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20813944" target="_blank"〉PubMed〈/a〉
    Keywords: AMP-Activated Protein Kinases/*metabolism ; Amino Acid Motifs ; Animals ; Chromatin/*metabolism ; *Gene Expression Regulation ; Histones/chemistry/*metabolism ; Mice ; Phosphorylation ; Promoter Regions, Genetic ; Protein-Serine-Threonine Kinases/metabolism ; Serine/metabolism ; *Stress, Physiological ; Transcription Factors/metabolism ; *Transcription, Genetic ; Tumor Suppressor Protein p53/metabolism
    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)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...