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  • Life Sciences (General)  (5)
  • Molecular Sequence Data  (4)
  • AEROSPACE MEDICINE  (3)
  • 2015-2019  (2)
  • 2000-2004  (7)
  • 1980-1984  (3)
  • 1940-1944
  • 1
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    Isolating "uncultivable" microorganisms in pure culture in a simulated natural environment (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-05-11
    Description: The majority (〉99%) of microorganisms from the environment resist cultivation in the laboratory. Ribosomal RNA analysis suggests that uncultivated organisms are found in nearly every prokaryotic group, and several divisions have no known cultivable representatives. We designed a diffusion chamber that allowed the growth of previously uncultivated microorganisms in a simulated natural environment. Colonies of representative marine organisms were isolated in pure culture. These isolates did not grow on artificial media alone but formed colonies in the presence of other microorganisms. This observation may help explain the nature of microbial uncultivability.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaeberlein, T -- Lewis, K -- Epstein, S S -- New York, N.Y. -- Science. 2002 May 10;296(5570):1127-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biology Department, Northeastern University, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12004133" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteria/classification/cytology/*growth & development/*isolation & purification ; *Bacteriological Techniques ; Colony Count, Microbial ; Culture Media ; DNA, Bacterial/analysis/genetics ; DNA, Ribosomal/analysis/genetics ; Diffusion Chambers, Culture ; Geologic Sediments/*microbiology ; Molecular Sequence Data ; RNA, Ribosomal, 16S/genetics ; *Seawater ; Silicon Dioxide
    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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    Role of the myosin assembly protein UNC-45 as a molecular chaperone for myosin (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-01-26
    Description: The organization of myosin into motile cellular structures requires precise temporal and spatial regulation. Proteins containing a UCS (UNC-45/CRO1/She4p) domain are necessary for the incorporation of myosin into the contractile ring during cytokinesis and into thick filaments during muscle development. We report that the carboxyl-terminal regions of UNC-45 bound and exerted chaperone activity on the myosin head. The amino-terminal tetratricopeptide repeat domain of UNC-45 bound the molecular chaperone Hsp90. Thus, UNC-45 functions both as a molecular chaperone and as an Hsp90 co-chaperone for myosin, which can explain previous findings of altered assembly and decreased accumulation of myosin in UNC-45 mutants of Caenorhabditis elegans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barral, Jose M -- Hutagalung, Alex H -- Brinker, Achim -- Hartl, F Ulrich -- Epstein, Henry F -- New York, N.Y. -- Science. 2002 Jan 25;295(5555):669-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11809970" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Binding Sites ; Caenorhabditis elegans/genetics/*metabolism ; Caenorhabditis elegans Proteins/chemistry/genetics/*metabolism ; Cell Line ; Cloning, Molecular ; HSP70 Heat-Shock Proteins/genetics/metabolism ; HSP90 Heat-Shock Proteins/genetics/metabolism ; Molecular Chaperones/chemistry/genetics/*metabolism ; Molecular Sequence Data ; Myosins/*metabolism ; Peptide Fragments/metabolism ; Protein Binding ; Protein Structure, Tertiary ; Recombinant Proteins/chemistry/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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  • 3
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    HEART DEVELOPMENT. Integration of Bmp and Wnt signaling by Hopx specifies commitment of cardiomyoblasts (2015)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2015-06-27
    Description: Cardiac progenitor cells are multipotent and give rise to cardiac endothelium, smooth muscle, and cardiomyocytes. Here, we define and characterize the cardiomyoblast intermediate that is committed to the cardiomyocyte fate, and we characterize the niche signals that regulate commitment. Cardiomyoblasts express Hopx, which functions to coordinate local Bmp signals to inhibit the Wnt pathway, thus promoting cardiomyogenesis. Hopx integrates Bmp and Wnt signaling by physically interacting with activated Smads and repressing Wnt genes. The identification of the committed cardiomyoblast that retains proliferative potential will inform cardiac regenerative therapeutics. In addition, Bmp signals characterize adult stem cell niches in other tissues where Hopx-mediated inhibition of Wnt is likely to contribute to stem cell quiescence and to explain the role of Hopx as a tumor suppressor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jain, Rajan -- Li, Deqiang -- Gupta, Mudit -- Manderfield, Lauren J -- Ifkovits, Jamie L -- Wang, Qiaohong -- Liu, Feiyan -- Liu, Ying -- Poleshko, Andrey -- Padmanabhan, Arun -- Raum, Jeffrey C -- Li, Li -- Morrisey, Edward E -- Lu, Min Min -- Won, Kyoung-Jae -- Epstein, Jonathan A -- 5-T32-GM-007170/GM/NIGMS NIH HHS/ -- K08 HL119553/HL/NHLBI NIH HHS/ -- K08 HL119553-02/HL/NHLBI NIH HHS/ -- R01 HL071546/HL/NHLBI NIH HHS/ -- U01 HL100405/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 2015 Jun 26;348(6242):aaa6071. doi: 10.1126/science.aaa6071.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell and Developmental Biology, Penn Cardiovascular Institute, Institute of Regenerative Medicine, Perelman School of Medicine at the University of Pennsylvania, Philadelphia, PA 19104, USA. ; Department of Genetics, Institute for Diabetes, Obesity, and Metabolism, Perelman School of Medicine at the University of Pennsylvania, Philadelphia, PA 19104, USA. ; Department of Cell and Developmental Biology, Penn Cardiovascular Institute, Institute of Regenerative Medicine, Perelman School of Medicine at the University of Pennsylvania, Philadelphia, PA 19104, USA. epsteinj@upenn.edu.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/26113728" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Bone Morphogenetic Proteins/genetics/*metabolism ; Cell Lineage/genetics ; Gene Expression ; *Gene Expression Regulation, Developmental ; Heart/*embryology ; Homeodomain Proteins/genetics/*metabolism ; Mice ; Mice, Mutant Strains ; Molecular Sequence Data ; Muscle, Smooth/cytology/metabolism ; Myoblasts, Cardiac/cytology/*metabolism ; Organogenesis/*genetics ; Stem Cell Niche/genetics/physiology ; Tumor Suppressor Proteins/genetics/*metabolism ; Wnt Signaling Pathway/*genetics
    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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    A new antibiotic kills pathogens without detectable resistance (2015)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2015-01-07
    Description: Antibiotic resistance is spreading faster than the introduction of new compounds into clinical practice, causing a public health crisis. Most antibiotics were produced by screening soil microorganisms, but this limited resource of cultivable bacteria was overmined by the 1960s. Synthetic approaches to produce antibiotics have been unable to replace this platform. Uncultured bacteria make up approximately 99% of all species in external environments, and are an untapped source of new antibiotics. We developed several methods to grow uncultured organisms by cultivation in situ or by using specific growth factors. Here we report a new antibiotic that we term teixobactin, discovered in a screen of uncultured bacteria. Teixobactin inhibits cell wall synthesis by binding to a highly conserved motif of lipid II (precursor of peptidoglycan) and lipid III (precursor of cell wall teichoic acid). We did not obtain any mutants of Staphylococcus aureus or Mycobacterium tuberculosis resistant to teixobactin. The properties of this compound suggest a path towards developing antibiotics that are likely to avoid development of resistance.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ling, Losee L -- Schneider, Tanja -- Peoples, Aaron J -- Spoering, Amy L -- Engels, Ina -- Conlon, Brian P -- Mueller, Anna -- Schaberle, Till F -- Hughes, Dallas E -- Epstein, Slava -- Jones, Michael -- Lazarides, Linos -- Steadman, Victoria A -- Cohen, Douglas R -- Felix, Cintia R -- Fetterman, K Ashley -- Millett, William P -- Nitti, Anthony G -- Zullo, Ashley M -- Chen, Chao -- Lewis, Kim -- AI085612/AI/NIAID NIH HHS/ -- T-RO1AI085585/AI/NIAID NIH HHS/ -- England -- Nature. 2015 Jan 22;517(7535):455-9. doi: 10.1038/nature14098. Epub 2015 Jan 7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉NovoBiotic Pharmaceuticals, Cambridge, Massachusetts 02138, USA. ; 1] Institute of Medical Microbiology, Immunology and Parasitology-Pharmaceutical Microbiology Section, University of Bonn, Bonn 53115, Germany [2] German Centre for Infection Research (DZIF), Partner Site Bonn-Cologne, 53115 Bonn, Germany. ; Antimicrobial Discovery Center, Northeastern University, Department of Biology, Boston, Massachusetts 02115, USA. ; 1] German Centre for Infection Research (DZIF), Partner Site Bonn-Cologne, 53115 Bonn, Germany [2] Institute for Pharmaceutical Biology, University of Bonn, Bonn 53115, Germany. ; Department of Biology, Northeastern University, Boston, Massachusetts 02115, USA. ; Selcia, Ongar, Essex CM5 0GS, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25561178" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anti-Bacterial Agents/biosynthesis/chemistry/isolation & ; purification/*pharmacology ; Betaproteobacteria/chemistry/genetics ; Biological Products/chemistry/isolation & purification/pharmacology ; Cell Wall/chemistry/drug effects/metabolism ; Depsipeptides/biosynthesis/chemistry/isolation & purification/*pharmacology ; Disease Models, Animal ; *Drug Resistance, Microbial/genetics ; Female ; Mice ; Microbial Sensitivity Tests ; Microbial Viability/*drug effects ; Molecular Sequence Data ; Multigene Family/genetics ; Mycobacterium tuberculosis/cytology/*drug effects/genetics ; Peptidoglycan/biosynthesis ; Staphylococcal Infections/drug therapy/microbiology ; Staphylococcus aureus/chemistry/cytology/*drug effects/genetics ; Teichoic Acids/biosynthesis ; Time Factors
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 5
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    Rac-1 and Raf-1 kinases, components of distinct signaling pathways, activate myotonic dystrophy protein kinase (2000)
    In:  Other Sources
    Details
    Publication Date: 2011-08-24
    Description: Myotonic dystrophy protein kinase (DMPK) is a serine-threonine protein kinase encoded by the myotonic dystrophy (DM) locus on human chromosome 19q13.3. It is a close relative of other kinases that interact with members of the Rho family of small GTPases. We show here that the actin cytoskeleton-linked GTPase Rac-1 binds to DMPK, and coexpression of Rac-1 and DMPK activates its transphosphorylation activity in a GTP-sensitive manner. DMPK can also bind Raf-1 kinase, the Ras-activated molecule of the MAP kinase pathway. Purified Raf-1 kinase phosphorylates and activates DMPK. The interaction of DMPK with these distinct signals suggests that it may play a role as a nexus for cross-talk between their respective pathways and may partially explain the remarkable pleiotropy of DM.
    Keywords: Life Sciences (General)
    Type: FEBS letters (ISSN 0014-5793); Volume 475; 3; 273-7
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  • 6
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    Myotonic dystrophy protein kinase (DMPK) induces actin cytoskeletal reorganization and apoptotic-like blebbing in lens cells (2000)
    In:  Other Sources
    Details
    Publication Date: 2011-08-24
    Description: DMPK, the product of the DM locus, is a member of the same family of serine-threonine protein kinases as the Rho-associated enzymes. In DM, membrane inclusions accumulate in lens fiber cells producing cataracts. Overexpression of DMPK in cultured lens epithelial cells led to apoptotic-like blebbing of the plasma membrane and reorganization of the actin cytoskeleton. Enzymatically active DMPK was necessary for both effects; inactive mutant DMPK protein did not produce either effect. Active RhoA but not constitutive GDP-state mutant protein produced similar effects as DMPK. The similar actions of DMPK and RhoA suggest that they may function in the same regulatory network. The observed effects of DMPK may be relevant to the removal of membrane organelles during normal lens differentiation and the retention of intracellular membranes in DM lenses. Copyright 2000 Wiley-Liss, Inc.
    Keywords: Life Sciences (General)
    Type: Cell motility and the cytoskeleton (ISSN 0886-1544); Volume 45; 2; 133-48
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  • 7
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    Differential assembly of alpha- and gamma-filagenins into thick filaments in Caenorhabditis elegans (2000)
    In:  Other Sources
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    Publication Date: 2011-08-24
    Description: Muscle thick filaments are highly organized supramolecular assemblies of myosin and associated proteins with lengths, diameters and flexural rigidities characteristic of their source. The cores of body wall muscle thick filaments of the nematode Caenorhabditis elegans are tubular structures of paramyosin sub-filaments coupled by filagenins and have been proposed to serve as templates for the assembly of native thick filaments. We have characterized alpha- and gamma-filagenins, two novel proteins of the cores with calculated molecular masses of 30,043 and 19,601 and isoelectric points of 10.52 and 11.49, respectively. Western blot and immunoelectron microscopy using affinity-purified antibodies confirmed that the two proteins are core components. Immunoelectron microscopy of the cores revealed that they assemble with different periodicities. Immunofluorescence microscopy showed that alpha-filagenin is localized in the medial regions of the A-bands of body wall muscle cells whereas gamma-filagenin is localized in the flanking regions, and that alpha-filagenin is expressed in 1.5-twofold embryos while gamma-filagenin becomes detectable only in late vermiform embryos. The expression of both proteins continues throughout later stages of development. C. elegans body wall muscle thick filaments of these developmental stages have distinct lengths. Our results suggest that the differential assembly of alpha- and gamma-filagenins into thick filaments of distinct lengths may be developmentally regulated.
    Keywords: Life Sciences (General)
    Type: Journal of cell science (ISSN 0021-9533); Volume 113 ( Pt 22); 4001-12
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  • 8
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    STEM Analysis of Caenorhabditis elegans muscle thick filaments: evidence for microdifferentiated substructures (2001)
    In:  Other Sources
    Details
    Publication Date: 2011-08-24
    Description: In the thick filaments of body muscle in Caenorhabditis elegans, myosin A and myosin B isoforms and a subpopulation of paramyosin, a homologue of myosin heavy chain rods, are organized about a tubular core. As determined by scanning transmission electron microscopy, the thick filaments show a continuous decrease in mass-per-length (MPL) from their central zones to their polar regions. This is consistent with previously reported morphological studies and suggests that both their content and structural organization are microdifferentiated as a function of position. The cores are composed of a second distinct subpopulation of paramyosin in association with the alpha, beta, and gamma-filagenins. MPL measurements suggest that cores are formed from seven subfilaments containing four strands of paramyosin molecules, rather than the two originally proposed. The periodic locations of the filagenins within different regions and the presence of a central zone where myosin A is located, implies that the cores are also microdifferentiated with respect to molecular content and structure. This differentiation may result from a novel "induced strain" assembly mechanism based upon the interaction of the filagenins, paramyosin and myosin A. The cores may then serve as "differentiated templates" for the assembly of myosin B and paramyosin in the tapering, microdifferentiated polar regions of the thick filaments.
    Keywords: Life Sciences (General)
    Type: Journal of molecular biology (ISSN 0022-2836); Volume 305; 5; 1035-44
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  • 9
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    Effects of water immersion on plasma catecholamines in normal humans (1983)
    In:  Other Sources
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    Publication Date: 2019-06-28
    Description: An investigation was conducted in order to determine whether water immersion to the neck (NI) alters plasma catecholamines in normal humans. Eight normal subjects were studied during a seated control study (C) and during 4 hr of NI, and the levels of norepinephrine (NE) and epinephrine (E) as determined by radioenzymatic assay were measured hourly. Results show that despite the induction of a marked natriuresis and diuresis indicating significant central hypervolemia, NI failed to alter plasma NE or E levels compared with those of either C or the corresponding prestudy 1.5 hr. In addition, the diuresis and natriuresis was found to vary independently of NE. These results indicate that the response of the sympathetic nervous system to acute volume alteration may differ from the reported response to chronic volume expansion.
    Keywords: AEROSPACE MEDICINE
    Type: Journal of Applied Physiology: Respiratory, Environmental and Exercise Physiology (ISSN 0161-7567); 54; Jan. 198
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  • 10
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    Characterization of renal response to prolonged immersion in normal man (1980)
    In:  Other Sources
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    Publication Date: 2019-06-27
    Description: ?jDuring the initial phase of space flight, there is a translocation of fluid from the lower parts of the body to the central vascular compartment with a resultant natriuresis, diuresis, and weight loss. Because water immersion is regarded as an appropriate model for studying the redistribution of fluid that occurs in weightlessness, an immersion study of relatively prolonged duration was carried out in order to characterize the temporal profile of the renal adaptation to central hypervolemia. Twelve normal male subjects underwent an immersion study of 8-h duration in the sodium-replete state. Immersion resulted in marked natriuresis and diuresis which were sustained throughout the immersion period. The failure of that natriuresis and diuresis of immersion to abate or cease despite marked extracellular fluid volume contraction as evidenced by a mean weight loss of -2.2 + or - 0.3 kg suggests that central blood volume was not restored to normal and that some degree of central hypervolemia probably persisted.
    Keywords: AEROSPACE MEDICINE
    Type: Journal of Applied Physiology: Respiratory; vol. 49
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