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  • 1
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    Geological setting of vertebrate microfossil localities across the Cretaceous-Paleogene boundary in southwestern Saskatchewan, Canada (2015)
    National Research Council Canada (NRC)
    Details
    Publication Date: 2015-10-14
    Description: The Frenchman and Ravenscrag formations of southwestern Saskatchewan, Canada, record an apparently continuous sequence of nonmarine clastic sediments across the Cretaceous–Paleogene (K–Pg) boundary. Extensive exposures of these fossil-rich sediments occur in the Frenchman River Valley, near the towns of Ravenscrag, Eastend, and Shaunavon, and have been a focus of study since the 1970s. Despite this long history of investigation, a comprehensive account of the geographic and stratigraphic positions of many of the significant fossil localities has yet to be published. Given this state of affairs, the goals of this paper are to ( i ) document the geographic locations, stratigraphic positions, and lithologies of 11 key vertebrate microfossil localities, including several new localities that have been recently discovered, and ( ii ) provide an update on the status of these fossil localities, the majority of which have not been sampled in the last 20 years. Four fossil localities are known from the lower Paleocene Ravenscrag Formation, all of which are Puercan in age: Rav W-1 (Pu2), French Fry (Pu1), Croc Pot (?Pu2), and Pine Cree (?Pu2). With the exception of Rav W-1, which has since been lost as a consequence of quarry reclamation, all of the Ravenscrag Formation localities remain accessible and continue to be productive. Seven vertebrate microfossil localities from the upper Maastrichtian Frenchman Formation are reported here, all of which are Lancian in age: Long Fall, Fr-1, By Gar Gap, Hairpin, Wounded Knee, Wounded C, and Gryde. With the exception of Long Fall and Wounded Knee, which have been lost through reclamation or construction, all of the Frenchman Formation localities are accessible and remain productive.
    Print ISSN: 0008-4077
    Electronic ISSN: 1480-3313
    Topics: Geosciences
    Published by National Research Council Canada (NRC)
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  • 2
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    Diverged composition and regulation of the Trypanosoma brucei origin recognition complex that mediates DNA replication initiation (2016)
    Oxford University Press
    Details
    Publication Date: 2016-06-03
    Description: Initiation of DNA replication depends upon recognition of genomic sites, termed origins, by AAA+ ATPases. In prokaryotes a single factor binds each origin, whereas in eukaryotes this role is played by a six-protein origin recognition complex (ORC). Why eukaryotes evolved a multisubunit initiator, and the roles of each component, remains unclear. In Trypanosoma brucei , an ancient unicellular eukaryote, only one ORC-related initiator, TbORC1/CDC6, has been identified by sequence homology. Here we show that three TbORC1/CDC6-interacting factors also act in T. brucei nuclear DNA replication and demonstrate that TbORC1/CDC6 interacts in a high molecular complex in which a diverged Orc4 homologue and one replicative helicase subunit can also be found. Analysing the subcellular localization of four TbORC1/CDC6-interacting factors during the cell cycle reveals that one factor, TbORC1B, is not a static constituent of ORC but displays S-phase restricted nuclear localization and expression, suggesting it positively regulates replication. This work shows that ORC architecture and regulation are diverged features of DNA replication initiation in T. brucei , providing new insight into this key stage of eukaryotic genome copying.
    Print ISSN: 0305-1048
    Electronic ISSN: 1362-4962
    Topics: Biology
    Published by Oxford University Press
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  • 3
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    Temperature-regulated LPS remodeling by LpxD [Microbiology] (2012)
    National Academy of Sciences
    Details
    Publication Date: 2012-05-30
    Description: Maintenance of membrane function is essential and regulated at the genomic, transcriptional, and translational levels. Bacterial pathogens have a variety of mechanisms to adapt their membrane in response to transmission between environment, vector, and human host. Using a well-characterized model of lipid A diversification (Francisella), we demonstrate temperature-regulated membrane remodeling directed by multiple alleles of the lipid A-modifying N-acyltransferase enzyme, LpxD. Structural analysis of the lipid A at environmental and host temperatures revealed that the LpxD1 enzyme added a 3-OH C18 acyl group at 37 °C (host), whereas the LpxD2 enzyme added a 3-OH C16 acyl group at 18 °C (environment). Mutational analysis of either of the individual Francisella lpxD genes altered outer membrane (OM) permeability, antimicrobial peptide, and antibiotic susceptibility, whereas only the lpxD1-null mutant was attenuated in mice and subsequently exhibited protection against a lethal WT challenge. Additionally, growth-temperature analysis revealed transcriptional control of the lpxD genes and posttranslational control of the LpxD1 and LpxD2 enzymatic activities. These results suggest a direct mechanism for LPS/lipid A-level modifications resulting in alterations of membrane fluidity, as well as integrity and may represent a general paradigm for bacterial membrane adaptation and virulence-state adaptation.
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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  • 4
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    Architecture and dynamics of an A-kinase anchoring protein 79 (AKAP79) signaling complex [Biochemistry] (2011)
    National Academy of Sciences
    Details
    Publication Date: 2011-04-20
    Description: A-kinase anchoring protein 79 (AKAP79) is a human anchoring protein that organizes cAMP-dependent protein kinase (PKA), Ca2+/calmodulin (CaM)-dependent protein phosphatase (PP2B), and protein kinase C (PKC) for phosphoregulation of synaptic signaling. Quantitative biochemical analyses of selected AKAP79 complexes have determined the quaternary structure of these signaling complexes. We show that AKAP79 dimerizes, and we demonstrate that, upon addition of a lysine-reactive cross-linker, parallel homomeric dimers are stabilized through K328–K328 and K333–K333 cross-links. An assembly of greater complexity comprising AKAP79, PP2B, a type II regulatory subunit fragment (RII 1–45) of PKA, and CaM was reconstituted in vitro. Using native MS, we determined the molecular mass of this complex as 466 kDa. This indicates that dimeric AKAP79 coordinates two RII 1–45 homodimers, four PP2B heterodimers, and two CaM molecules. Binding of Ca2+/CaM to AKAP79 stabilizes the complex by generating a second interface for PP2B. This leads to activation of the anchored phosphatases. Our architectural model reveals how dimeric AKAP79 concentrates pockets of second messenger responsive enzyme activities at the plasma membrane.
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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  • 5
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    Regulation of NMDA receptors by an associated phosphatase-kinase signaling complex (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-07-03
    Description: Regulation of N-methyl-D-aspartate (NMDA) receptor activity by kinases and phosphatases contributes to the modulation of synaptic transmission. Targeting of these enzymes near the substrate is proposed to enhance phosphorylation-dependent modulation. Yotiao, an NMDA receptor-associated protein, bound the type I protein phosphatase (PP1) and the adenosine 3',5'-monophosphate (cAMP)-dependent protein kinase (PKA) holoenzyme. Anchored PP1 was active, limiting channel activity, whereas PKA activation overcame constitutive PP1 activity and conferred rapid enhancement of NMDA receptor currents. Hence, yotiao is a scaffold protein that physically attaches PP1 and PKA to NMDA receptors to regulate channel activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Westphal, R S -- Tavalin, S J -- Lin, J W -- Alto, N M -- Fraser, I D -- Langeberg, L K -- Sheng, M -- Scott, J D -- F32 NS010202/NS/NINDS NIH HHS/ -- GM 48231/GM/NIGMS NIH HHS/ -- NS10202/NS/NINDS NIH HHS/ -- NS10543/NS/NINDS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1999 Jul 2;285(5424):93-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Vollum Institute, Oregon Health Sciences University, 3181 S.W. Sam Jackson Road, Portland, OR 97201, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10390370" target="_blank"〉PubMed〈/a〉
    Keywords: A Kinase Anchor Proteins ; *Adaptor Proteins, Signal Transducing ; Amino Acid Sequence ; Animals ; Binding Sites ; Carrier Proteins/*metabolism ; Cell Line ; Cyclic AMP/analogs & derivatives/pharmacology ; Cyclic AMP-Dependent Protein Kinases/*metabolism ; Cytoskeletal Proteins/*metabolism ; Enzyme Inhibitors/pharmacology ; Holoenzymes/metabolism ; Humans ; Molecular Sequence Data ; Okadaic Acid/pharmacology ; Patch-Clamp Techniques ; Peptide Fragments/pharmacology ; Phosphoprotein Phosphatases/*metabolism ; Phosphorylation ; Rats ; Receptors, N-Methyl-D-Aspartate/*metabolism ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; Thionucleotides/pharmacology ; Transfection
    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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  • 6
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    Signaling through scaffold, anchoring, and adaptor proteins (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-02-12
    Description: The process by which extracellular signals are relayed from the plasma membrane to specific intracellular sites is an essential facet of cellular regulation. Many signaling pathways do so by altering the phosphorylation state of tyrosine, serine, or threonine residues of target proteins. Recently, it has become apparent that regulatory mechanisms exist to influence where and when protein kinases and phosphatases are activated in the cell. The role of scaffold, anchoring, and adaptor proteins that contribute to the specificity of signal transduction events by recruiting active enzymes into signaling networks or by placing enzymes close to their substrates is discussed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pawson, T -- Scott, J D -- GM48231/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Dec 19;278(5346):2075-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario M5G 1X5, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9405336" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Ligands ; Phospholipids/metabolism ; Phosphoprotein Phosphatases/metabolism ; Phosphoproteins/*metabolism ; Phosphorylation ; Phosphoserine/metabolism ; Phosphothreonine/metabolism ; Phosphotyrosine/metabolism ; Protein-Serine-Threonine Kinases/metabolism ; Protein-Tyrosine Kinases/metabolism ; Proteins/chemistry/*metabolism ; *Signal Transduction ; src Homology Domains
    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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  • 7
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    Association of protein kinase A and protein phosphatase 2B with a common anchoring protein (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-01-06
    Description: Specificity of protein kinases and phosphatases may be achieved through compartmentalization with preferred substrates. In neurons, adenosine 3', 5'-monophosphate (cAMP)-dependent protein kinase (PKA) is localized at postsynaptic densities by association of its regulatory subunit with an A kinase anchor protein, AKAP79. Interaction cloning experiments demonstrated that AKAP79 also binds protein phosphatase 2B, or calcineurin (CaN). A ternary complex of PKA, AKAP, and CaN was isolated from bovine brain, and colocalization of the kinase and the phosphatase was established in neurites of cultured hippocampal neurons. The putative CaN-binding domain of AKAP79 is similar to that of the immunophilin FKBP-12, and AKAP79 inhibited CaN phosphatase activity. These results suggest that both PKA and CaN are targeted to subcellular sites by association with a common anchor protein and thereby regulate the phosphorylation state of key neuronal substrates.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Coghlan, V M -- Perrino, B A -- Howard, M -- Langeberg, L K -- Hicks, J B -- Gallatin, W M -- Scott, J D -- DK09059/DK/NIDDK NIH HHS/ -- GM48231/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Jan 6;267(5194):108-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Vollum Institute, Oregon Health Sciences University, Portland 97201.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7528941" target="_blank"〉PubMed〈/a〉
    Keywords: A Kinase Anchor Proteins ; *Adaptor Proteins, Signal Transducing ; Amino Acid Sequence ; Animals ; Binding Sites ; *Brain Chemistry ; Calcineurin ; Calmodulin-Binding Proteins/analysis/antagonists & inhibitors/*metabolism ; Carrier Proteins/analysis ; Cattle ; Cells, Cultured ; Cyclic AMP-Dependent Protein Kinases/analysis/*metabolism ; Hippocampus/chemistry ; Molecular Sequence Data ; Neurites/chemistry ; Phosphoprotein Phosphatases/analysis/antagonists & inhibitors/*metabolism ; Phosphorylation ; Proteins/*metabolism/pharmacology ; Rats ; Recombinant Proteins/pharmacology ; Tacrolimus/pharmacology
    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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    Coordination of three signaling enzymes by AKAP79, a mammalian scaffold protein (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-03-15
    Description: Multivalent binding proteins, such as the yeast scaffold protein Sterile-5, coordinate the location of kinases by serving as platforms for the assembly of signaling units. Similarly, in mammalian cells the cyclic adenosine 3',5'-monophosphate-dependent protein kinase (PKA) and phosphatase 2B [calcineurin (CaN)] are complexed by an A kinase anchoring protein, AKAP79. Deletion analysis and binding studies demonstrate that a third enzyme, protein kinase C (PKC), binds AKAP79 at a site distinct from those bound by PKA or CaN. The subcellular distributions of PKC and AKAP79 were similar in neurons. Thus, AKAP79 appears to function as a scaffold protein for three multifunctional enzymes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Klauck, T M -- Faux, M C -- Labudda, K -- Langeberg, L K -- Jaken, S -- Scott, J D -- CA538841/CA/NCI NIH HHS/ -- GM48231/GM/NIGMS NIH HHS/ -- GM50152/GM/NIGMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1996 Mar 15;271(5255):1589-92.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Vollum Institute, Oregon Health Sciences University, Portland, 97201, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8599116" target="_blank"〉PubMed〈/a〉
    Keywords: A Kinase Anchor Proteins ; *Adaptor Proteins, Signal Transducing ; Amino Acid Sequence ; Animals ; Brain/enzymology ; Calcineurin ; Calmodulin/pharmacology ; Calmodulin-Binding Proteins/*metabolism ; *Carrier Proteins ; Cattle ; Cell Line ; Cyclic AMP-Dependent Protein Kinases/analysis/antagonists & ; inhibitors/*metabolism ; Fungal Proteins/metabolism ; Humans ; Molecular Sequence Data ; Neurons/chemistry ; Phosphoprotein Phosphatases/*metabolism ; Phosphorylation ; Protein Kinase C/analysis/antagonists & inhibitors/*metabolism ; Proteins/analysis/*metabolism/pharmacology ; Recombinant Proteins ; *Saccharomyces cerevisiae Proteins ; Signal Transduction ; Synapses/physiology
    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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    Cell signaling in space and time: where proteins come together and when they're apart (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-12-08
    Description: Signal transduction can be defined as the coordinated relay of messages derived from extracellular cues to intracellular effectors. More simply put, information received on the cell surface is processed across the plasma membrane and transmitted to intracellular targets. This requires that the activators, effectors, enzymes, and substrates that respond to cellular signals come together when they need to.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3041271/" 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/PMC3041271/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Scott, John D -- Pawson, Tony -- 57793/Canadian Institutes of Health Research/Canada -- 6849/Canadian Institutes of Health Research/Canada -- GM48231/GM/NIGMS NIH HHS/ -- R37 GM048231/GM/NIGMS NIH HHS/ -- R37 GM048231-19/GM/NIGMS NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2009 Nov 27;326(5957):1220-4. doi: 10.1126/science.1175668.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, Howard Hughes Medical Institute, Box 357750, University of Washington School of Medicine, Seattle, WA 98195, USA. scottjdw@u.washington.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19965465" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Compartmentation ; Cell Membrane/*metabolism ; Cell Nucleus/*metabolism ; Cytoplasm/*metabolism ; Enzymes/metabolism ; Humans ; MAP Kinase Signaling System ; Models, Biological ; Multiprotein Complexes/metabolism ; Protein Interaction Domains and Motifs ; Proteins/*metabolism ; *Signal Transduction ; Time Factors ; 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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  • 10
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    Retrospective. Edwin G. Krebs (1918-2009) (2010)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2010-01-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Catterall, William A -- Scott, John D -- New York, N.Y. -- Science. 2010 Jan 29;327(5965):537. doi: 10.1126/science.1186913.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, School of Medicine, University of Washington, Seattle, WA 98195-7280, USA. wcatt@u.washington.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20110494" target="_blank"〉PubMed〈/a〉
    Keywords: Biochemistry/*history ; History, 20th Century ; History, 21st Century ; Nobel Prize ; Phosphorylases/history/metabolism ; Phosphorylation ; Protein Kinases/history/metabolism ; Proteins/metabolism ; Signal Transduction ; United States
    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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