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  • 1
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    Structure of the cell wall anchor of surface proteins in Staphylococcus aureus (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-04-07
    Description: Many surface proteins are anchored to the cell wall of Gram-positive bacteria and are involved in the pathogenesis of these organisms. A hybrid molecule was designed that, when expressed in Staphylococcus aureus, was anchored to the cell wall and could be released by controlled enzymatic digestion. By a combination of molecular biology and mass spectrometry techniques, the structure of the cell wall anchor of surface proteins in S. aureus was revealed. After cleavage of surface proteins between threonine and glycine of the conserved LPXTG motif, the carboxyl of threonine is amide-linked to the free amino group of the pentaglycine crossbridge in the staphylococcal cell wall.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schneewind, O -- Fowler, A -- Faull, K F -- AI 33985/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1995 Apr 7;268(5207):103-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, University of California School of Medicine, Los Angeles 90024, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7701329" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Proteins/*chemistry ; Base Sequence ; Carrier Proteins/chemistry ; Cell Wall/*chemistry ; Chromatography, Affinity ; Chromatography, High Pressure Liquid/methods ; Electrophoresis, Polyacrylamide Gel ; Maltose-Binding Proteins ; Membrane Proteins/*chemistry ; Molecular Sequence Data ; Recombinant Fusion Proteins/chemistry ; Staphylococcal Protein A/chemistry ; Staphylococcus aureus/*chemistry
    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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  • 2
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    Human neuroblasts migrate to the olfactory bulb via a lateral ventricular extension (2007)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2007-02-17
    Description: The rostral migratory stream (RMS) is the main pathway by which newly born subventricular zone cells reach the olfactory bulb (OB) in rodents. However, the RMS in the adult human brain has been elusive. We demonstrate the presence of a human RMS, which is unexpectedly organized around a lateral ventricular extension reaching the OB, and illustrate the neuroblasts in it. The RMS ensheathing the lateral olfactory ventricular extension, as seen by magnetic resonance imaging, cell-specific markers, and electron microscopy, contains progenitor cells with migratory characteristics and cells that incorporate 5-bromo-2'-deoxyuridine and become mature neurons in the OB.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Curtis, Maurice A -- Kam, Monica -- Nannmark, Ulf -- Anderson, Michelle F -- Axell, Mathilda Zetterstrom -- Wikkelso, Carsten -- Holtas, Stig -- van Roon-Mom, Willeke M C -- Bjork-Eriksson, Thomas -- Nordborg, Claes -- Frisen, Jonas -- Dragunow, Michael -- Faull, Richard L M -- Eriksson, Peter S -- New York, N.Y. -- Science. 2007 Mar 2;315(5816):1243-9. Epub 2007 Feb 15.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Anatomy with Radiology, Faculty of Medical and Health Sciences, University of Auckland, Private Bag 92019, Auckland, New Zealand.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17303719" target="_blank"〉PubMed〈/a〉
    Keywords: Apoptosis ; Basic Helix-Loop-Helix Transcription Factors/genetics ; Cell Differentiation ; Cell Movement ; Cell Nucleus/chemistry/ultrastructure ; Cell Shape ; Ependyma/cytology ; Eye Proteins/genetics ; Homeodomain Proteins/genetics ; Humans ; Lateral Ventricles/anatomy & histology/*cytology ; Magnetic Resonance Imaging ; Microscopy, Electron ; Microtubule-Associated Proteins/genetics ; Nerve Tissue Proteins/genetics ; Neural Cell Adhesion Molecule L1/analysis ; Neurons/chemistry/cytology/*physiology/ultrastructure ; Neuropeptides/genetics ; Olfactory Bulb/anatomy & histology/*cytology ; Olfactory Pathways/anatomy & histology/*cytology ; Paired Box Transcription Factors/genetics ; Prosencephalon/anatomy & histology/*cytology ; Repressor Proteins/genetics ; Sialic Acids/analysis ; Stem Cells/chemistry/cytology/*physiology/ultrastructure ; Tubulin/analysis
    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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  • 3
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    The MAP kinase pathway coordinates crossover designation with disassembly of synaptonemal complex proteins during meiosis (2016)
    eLife Sciences Publications
    Details
    Publication Date: 2016-02-27
    Description: Asymmetric disassembly of the synaptonemal complex (SC) is crucial for proper meiotic chromosome segregation. However, the signaling mechanisms that directly regulate this process are poorly understood. Here we show that the mammalian Rho GEF homolog, ECT-2, functions through the conserved RAS/ERK MAP kinase signaling pathway in the C. elegans germline to regulate the disassembly of SC proteins. We find that SYP-2, a SC central region component, is a potential target for MPK-1-mediated phosphorylation and that constitutively phosphorylated SYP-2 impairs the disassembly of SC proteins from chromosomal domains referred to as the long arms of the bivalents. Inactivation of MAP kinase at late pachytene is critical for timely disassembly of the SC proteins from the long arms, and is dependent on the crossover (CO) promoting factors ZHP-3/RNF212/Zip3 and COSA-1/CNTD1. We propose that the conserved MAP kinase pathway coordinates CO designation with the disassembly of SC proteins to ensure accurate chromosome segregation.
    Electronic ISSN: 2050-084X
    Topics: Biology , Medicine , Natural Sciences in General
    Published by eLife Sciences Publications
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  • 4
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    Oxidation of cellular amino acid pools leads to cytotoxic mistranslation of the genetic code (2014)
    eLife Sciences Publications
    Details
    Publication Date: 2014-06-02
    Description: Aminoacyl-tRNA synthetases use a variety of mechanisms to ensure fidelity of the genetic code and ultimately select the correct amino acids to be used in protein synthesis. The physiological necessity of these quality control mechanisms in different environments remains unclear, as the cost vs benefit of accurate protein synthesis is difficult to predict. We show that in Escherichia coli, a non-coded amino acid produced through oxidative damage is a significant threat to the accuracy of protein synthesis and must be cleared by phenylalanine-tRNA synthetase in order to prevent cellular toxicity caused by mis-synthesized proteins. These findings demonstrate how stress can lead to the accumulation of non-canonical amino acids that must be excluded from the proteome in order to maintain cellular viability.
    Electronic ISSN: 2050-084X
    Topics: Biology , Medicine , Natural Sciences in General
    Published by eLife Sciences Publications
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  • 5
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    Conditioned respiratory threat in the subdivisions of the human periaqueductal gray (2016)
    eLife Sciences Publications
    Details
    Publication Date: 2016-02-27
    Description: The sensation of breathlessness is the most threatening symptom of respiratory disease. The different subdivisions of the midbrain periaqueductal gray (PAG) are intricately (and differentially) involved in integrating behavioural responses to threat in animals, while the PAG has previously only been considered as a single entity in human research. Here we investigate how these individual PAG columns are differently involved with respiratory threat. Eighteen healthy subjects were conditioned to associate shapes with certain or uncertain impending respiratory load, and scanned the following day during anticipation and application of inspiratory loading using 7 T functional MRI. We showed activity in the ventrolateral PAG (vlPAG) during anticipation of resistive loading, with activity in the lateral PAG (lPAG) during resistive loading, revealing spatially and temporally distinct functions within this structure. We propose that lPAG is involved with sensorimotor responses to breathlessness, while the vlPAG operates within the threat perception network for impending breathlessness.
    Electronic ISSN: 2050-084X
    Topics: Biology , Medicine , Natural Sciences in General
    Published by eLife Sciences Publications
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  • 6
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    TRF1 averts chromatin remodelling, recombination and replication dependent-break induced replication at mouse telomeres (2020)
    eLife Sciences Publications
    Details
    Publication Date: 2020-01-14
    Description: Telomeres are a significant challenge to DNA replication and are prone to replication stress and telomere fragility. The shelterin component TRF1 facilitates telomere replication but the molecular mechanism remains uncertain. By interrogating the proteomic composition of telomeres, we show that mouse telomeres lacking TRF1 undergo protein composition reorganisation associated with the recruitment of DNA damage response and chromatin remodellers. Surprisingly, mTRF1 suppresses the accumulation of promyelocytic leukemia (PML) protein, BRCA1 and the SMC5/6 complex at telomeres, which is associated with increased Homologous Recombination (HR) and TERRA transcription. We uncovered a previously unappreciated role for mTRF1 in the suppression of telomere recombination, dependent on SMC5 and also POLD3 dependent Break Induced Replication at telomeres. We propose that TRF1 facilitates S-phase telomeric DNA synthesis to prevent illegitimate mitotic DNA recombination and chromatin rearrangement.
    Electronic ISSN: 2050-084X
    Topics: Biology , Medicine , Natural Sciences in General
    Published by eLife Sciences Publications
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  • 7
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    The cortical connectivity of the periaqueductal gray and the conditioned response to the threat of breathlessness (2017)
    eLife Sciences Publications
    Details
    Publication Date: 2017-02-17
    Description: Previously we observed differential activation in individual columns of the periaqueductal grey (PAG) during breathlessness and its conditioned anticipation (Faull et al., 2016b). Here, we have extended this work by determining how the individual columns of the PAG interact with higher cortical centres, both at rest and in the context of breathlessness threat. Activation was observed in ventrolateral PAG (vlPAG) and lateral PAG (lPAG), where activity scaled with breathlessness intensity ratings, revealing a potential interface between sensation and cognition during breathlessness. At rest the lPAG was functionally correlated with cortical sensorimotor areas, conducive to facilitating fight/flight responses, and demonstrated increased synchronicity with the amygdala during breathlessness. The vlPAG showed fronto-limbic correlations at rest, whereas during breathlessness anticipation, reduced functional synchronicity was seen to both lPAG and motor structures, conducive to freezing behaviours. These results move us towards understanding how the PAG might be intricately involved in human responses to threat.
    Electronic ISSN: 2050-084X
    Topics: Biology , Medicine , Natural Sciences in General
    Published by eLife Sciences Publications
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