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  • 1
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    Requirement of the prolyl isomerase Pin1 for the replication checkpoint (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-03-04
    Description: The peptidyl-prolyl isomerase Pin1 has been implicated in regulating cell cycle progression. Pin1 was found to be required for the DNA replication checkpoint in Xenopus laevis. Egg extracts depleted of Pin1 inappropriately transited from the G2 to the M phase of the cell cycle in the presence of the DNA replication inhibitor aphidicolin. This defect in replication checkpoint function was reversed after the addition of recombinant wild-type Pin1, but not an isomerase-inactive mutant, to the depleted extract. Premature mitotic entry in the absence of Pin1 was accompanied by hyperphosphorylation of Cdc25, activation of Cdc2/cyclin B, and generation of epitopes recognized by the mitotic phosphoprotein antibody, MPM-2. Therefore, Pin1 appears to be required for the checkpoint delaying the onset of mitosis in response to incomplete replication.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Winkler, K E -- Swenson, K I -- Kornbluth, S -- Means, A R -- CA 82845/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2000 Mar 3;287(5458):1644-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology and Cancer Biology, Duke University Medical Center, Box 3813, Durham, NC 27710, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10698738" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Aphidicolin/pharmacology ; Cell Cycle ; *Cell Cycle Proteins ; Cyclin B/metabolism ; *DNA Replication ; Enzyme Inhibitors/pharmacology ; G2 Phase ; *Mitosis ; *Nuclear Proteins ; Nucleic Acid Synthesis Inhibitors ; Oocytes ; Peptidylprolyl Isomerase/genetics/*metabolism/pharmacology ; Point Mutation ; Protein Kinases/metabolism ; Protein-Serine-Threonine Kinases/metabolism ; Protein-Tyrosine Kinases/metabolism ; Recombinant Proteins/metabolism/pharmacology ; *Xenopus Proteins ; Xenopus laevis ; cdc25 Phosphatases/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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    A signaling complex of Ca2+-calmodulin-dependent protein kinase IV and protein phosphatase 2A (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-06-20
    Description: Stimulation of T lymphocytes results in a rapid increase in intracellular calcium concentration ([Ca2+]i) that parallels the activation of Ca2+-calmodulin-dependent protein kinase IV (CaMKIV), a nuclear enzyme that can phosphorylate and activate the cyclic adenosine monophosphate (cAMP) response element-binding protein (CREB). However, inactivation of CaMKIV occurs despite the sustained increase in [Ca2+]i that is required for T cell activation. A stable and stoichiometric complex of CaMKIV with protein serine-threonine phosphatase 2A (PP2A) was identified in which PP2A dephosphorylates CaMKIV and functions as a negative regulator of CaMKIV signaling. In Jurkat T cells, inhibition of PP2A activity by small t antigen enhanced activation of CREB-mediated transcription by CaMKIV. These findings reveal an intracellular signaling mechanism whereby a protein serine-threonine kinase (CaMKIV) is regulated by a tightly associated protein serine-threonine phosphatase (PP2A).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Westphal, R S -- Anderson, K A -- Means, A R -- Wadzinski, B E -- GM33976/GM/NIGMS NIH HHS/ -- GM51366/GM/NIGMS NIH HHS/ -- HD07503/HD/NICHD NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1998 May 22;280(5367):1258-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, Vanderbilt University School of Medicine, Nashville, TN 37232, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9596578" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, Polyomavirus Transforming/metabolism ; Brain/enzymology ; Calcium/metabolism ; Calcium-Calmodulin-Dependent Protein Kinase Type 4 ; Calcium-Calmodulin-Dependent Protein Kinases/genetics/isolation & ; purification/*metabolism ; Calmodulin/metabolism ; Coenzymes/metabolism ; Cyclic AMP Response Element-Binding Protein/metabolism ; Enzyme Activation ; Humans ; Jurkat Cells ; Lymphocyte Activation ; Mutation ; Phosphoprotein Phosphatases/isolation & purification/*metabolism ; Phosphorylation ; Protein Phosphatase 2 ; Rats ; Recombinant Fusion Proteins/metabolism ; *Signal Transduction ; T-Lymphocytes/*enzymology ; Transcription, Genetic
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    Structural basis of the intrasteric regulation of myosin light chain kinases (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-10-02
    Description: The smooth muscle myosin light chain kinase (smMLCK) catalytic core was modeled by using the crystallographic coordinates of the cyclic AMP-dependent protein kinase catalytic subunit (cAPK) and a bound pseudosubstrate inhibitor peptide, PKI(5-24). Despite only 30% identity in amino acid sequence, the MLCK sequence can be readily accommodated in this structure. With the exception of the short B-helix, all major elements of secondary structure in the core are very likely conserved. The active site of the modeled MLCK complements the known requirements for peptide substrate recognition. MLCK contains a pseudosubstrate sequence that overlaps the calmodulin binding domain and has been proposed to act as an intrasteric inhibitor and occupy the substrate binding site in the absence of Ca(2+)-calmodulin. The pseudosubstrate sequence can be modeled easily into the entire backbone of PKI(5-24). The results demonstrate that the intrasteric model for regulation of MLCK by intramolecular competitive inhibition is structurally plausible.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Knighton, D R -- Pearson, R B -- Sowadski, J M -- Means, A R -- Ten Eyck, L F -- Taylor, S S -- Kemp, B E -- T32CA09523/CA/NCI NIH HHS/ -- T32DK07233/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1992 Oct 2;258(5079):130-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of California San Diego, La Jolla 92093-0654.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1439761" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Chromosome Mapping ; Crystallography ; *Gene Expression Regulation, Enzymologic ; Models, Molecular ; Molecular Sequence Data ; Molecular Structure ; Myosin-Light-Chain Kinase/*chemistry ; Oligopeptides/genetics/metabolism ; Peptide Fragments ; Peptides/genetics/metabolism ; Protein Binding/physiology ; Protein Kinases/chemistry ; Sequence Alignment ; Sequence Homology
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    Target enzyme recognition by calmodulin: 2.4 A structure of a calmodulin-peptide complex (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-08-28
    Description: The crystal structure of calcium-bound calmodulin (Ca(2+)-CaM) bound to a peptide analog of the CaM-binding region of chicken smooth muscle myosin light chain kinase has been determined and refined to a resolution of 2.4 angstroms (A). The structure is compact and has the shape of an ellipsoid (axial ratio approximately 2:1). The bound CaM forms a tunnel diagonal to its long axis that engulfs the helical peptide, with the hydrophobic regions of CaM melded into a single area that closely covers the hydrophobic side of the peptide. There is a remarkably high pseudo-twofold symmetry between the closely associated domains. The central helix of the native CaM is unwound and expanded into a bend between residues 73 and 77. About 185 contacts (less than 4 A) are formed between CaM and the peptide, with van der Waals contacts comprising approximately 80% of this total.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Meador, W E -- Means, A R -- Quiocho, F A -- New York, N.Y. -- Science. 1992 Aug 28;257(5074):1251-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Baylor College of Medicine, Houston, TX 77030.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1519061" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Calmodulin/*chemistry ; Crystallography ; Models, Molecular ; Molecular Sequence Data ; Myosin-Light-Chain Kinase/*metabolism ; Protein Conformation
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  • 5
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    Through the glass lightly (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-03-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Means, A R -- New York, N.Y. -- Science. 1995 Mar 17;267(5204):1610-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17808126" target="_blank"〉PubMed〈/a〉
    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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  • 6
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    Modulation of calmodulin plasticity in molecular recognition on the basis of x-ray structures (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-12-10
    Description: Calmodulin is the primary calcium-dependent signal transducer and regulator of a wide variety of essential cellular functions. The structure of calcium-calmodulin bound to the peptide corresponding to the calmodulin-binding domain of brain calmodulin-dependent protein kinase II alpha was determined to 2 angstrom resolution. A comparison to two other calcium-calmodulin structures reveals how the central helix unwinds in order to position the two domains optimally in the recognition of different target enzymes and clarifies the role of calcium in maintaining recognition-competent domain structures.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Meador, W E -- Means, A R -- Quiocho, F A -- New York, N.Y. -- Science. 1993 Dec 10;262(5140):1718-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Baylor College of Medicine, Houston, TX 77030.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8259515" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Calcium/*metabolism ; Calcium-Calmodulin-Dependent Protein Kinases/chemistry/*metabolism ; Calmodulin/*chemistry/metabolism ; Computer Graphics ; Crystallography, X-Ray ; Models, Molecular ; Molecular Sequence Data ; Peptides/chemistry/*metabolism ; Protein Structure, Secondary ; Signal Transduction
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
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    Autoregulation of enzymes by pseudosubstrate prototopes: myosin light chain kinase (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-08-19
    Description: The myosin light chain kinase requires calmodulin for activation. Tryptic cleavage of the enzyme generates an inactive 64-kilodalton (kD) fragment that can be further cleaved to form a constitutively active, calmodulin-independent, 61-kD fragment. Microsequencing and amino acid analysis of purified peptides after proteolysis of the 61- and 64-kD fragments were used to determine the amino-terminal and carboxyl-terminal sequences of the 64-kD fragment. Cleavage within the calmodulin-binding region at Arg505 generates the catalytically inactive 64-kD fragment, which is incapable of binding calmodulin. Further digestion removes a carboxyl-terminal fragment, including the pseudosubstrate sequence Ser484-Lys-Asp-Arg-Met-Lys-Lys-Tyr-Met- Ala-Arg-Arg-Lys-Trp-Gln-Lys-Thr-Gly-His-Ala-Val-Arg505 and results in a calmodulin-independent 61-kD fragment. Both the 61- and 64-kD fragments have the same primary amino-terminal sequences. These results provide direct support for the concept that the pseudosubstrate structure binds the active site and that the role of calmodulin is to modulate this interaction. Pseudosubstrates may be utilized in analogous ways by other allosterically regulated enzymes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pearson, R B -- Wettenhall, R E -- Means, A R -- Hartshorne, D J -- Kemp, B E -- New York, N.Y. -- Science. 1988 Aug 19;241(4868):970-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of Melbourne, Repatriation General Hospital, Heidelberg, Victoria, Australia.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3406746" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Calmodulin/*metabolism ; Chromatography, High Pressure Liquid ; Enzyme Activation ; Molecular Sequence Data ; Muscle, Smooth/*enzymology ; Myosin-Light-Chain Kinase/analysis/*metabolism ; Peptide Mapping ; Substrate Specificity
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  • 8
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    Migration of radioactive wastes: radionuclide mobilization by complexing agents (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-06-30
    Description: Ion exchange, gel filtration chromatography, and gas chromatographymass spectrometry analyses have demonstrated that ethylenediaminetetraacetic acid (EDTA), an extremely strong complexing agent commonly used in decontamination operations at nuclear facilities, is causing the low-level migration of cobalt-60 from intermediate-level liquid waste disposal pits and trenches in the Oak Ridge National Laboratory burial grounds. Because it forms extremely strong complexes with rare earths and actinides, EDTA or similar chelates may also be contributing to the mobilization of these radionuclides from various terrestrial radioactive waste burial sites around the country.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Means, J L -- Crerar, D A -- Duguid, J O -- New York, N.Y. -- Science. 1978 Jun 30;200(4349):1477-81.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17757689" target="_blank"〉PubMed〈/a〉
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  • 9
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    Potentiation of bleomycin lethality by anticalmodulin drugs: a role for calmodulin in DNA repair (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-06-22
    Description: Treatment of exponentially growing Chinese hamster ovary cells with bleomycin causes a dose-dependent decrease in cell survival due to DNA damage. This lethal effect can be potentiated by the addition of a nonlethal dose of the anticalmodulin drug N-(4-aminobutyl)-5-chloro-2-naphthalenesulfonamide ( W13 ) but not its inactive analog N-(4-aminobutyl)-2-naphthalenesulfonamide ( W12 ). By preventing the repair of damaged DNA, W13 also inhibits recovery from potentially lethal damage induced by bleomycin. These data suggest a role for calmodulin in the DNA repair pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chafouleas, J G -- Bolton, W E -- Means, A R -- RR-05425/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1984 Jun 22;224(4655):1346-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6203171" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bleomycin/*pharmacology ; Calmodulin/*antagonists & inhibitors/*physiology ; Cell Division/drug effects ; Cell Line ; Cell Survival/drug effects ; Cricetinae ; Cricetulus ; DNA Repair/*drug effects ; Dose-Response Relationship, Drug ; Drug Synergism ; Sulfonamides/pharmacology
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  • 10
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    Methylation of tin by estuarine microorganisms (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-03-19
    Description: Mixed inoculums of microorganisms from Chesapeake Bay sediments transformed inorganic tin (SnCl(4) . 5H(2)O) to organotin compounds. Dimethyltin and trimethyltin species were identified as products by gas chromatography-mass spectrometry. Methylated tin species were not observed in sterile controls or in poisoned controls. Thus, estuarine microorganisms have the potential for transforming tin to toxic organotins and for mobilizing tin in the ecosystem.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hallas, L E -- Means, J C -- Cooney, J J -- New York, N.Y. -- Science. 1982 Mar 19;215(4539):1505-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17788676" target="_blank"〉PubMed〈/a〉
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