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  • 1
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    The effective yield of a nuclear explosion in a small cavity in geologic material: Enhanced coupling revisited (1989)
    In:  J. Geophys. Res., Jena, Physica-Verlag, vol. 94, no. B6, pp. 12375-12385, pp. L24313, (ISSN: 1340-4202)
    Details
    Publication Date: 1989
    Keywords: Nuclear explosion ; DeconvolutionP ; JGR
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    BIBLIOGRAPHY SEISMOLOGY
  • 2
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    Structure and function of a human TAFII250 double bromodomain module (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-05-29
    Description: TFIID is a large multiprotein complex that initiates assembly of the transcription machinery. It is unclear how TFIID recognizes promoters in vivo when templates are nucleosome-bound. Here, it is shown that TAFII250, the largest subunit of TFIID, contains two tandem bromodomain modules that bind selectively to multiply acetylated histone H4 peptides. The 2.1 angstrom crystal structure of the double bromodomain reveals two side-by-side, four-helix bundles with a highly polarized surface charge distribution. Each bundle contains an Nepsilon-acetyllysine binding pocket at its center, which results in a structure ideally suited for recognition of diacetylated histone H4 tails. Thus, TFIID may be targeted to specific chromatin-bound promoters and may play a role in chromatin recognition.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jacobson, R H -- Ladurner, A G -- King, D S -- Tjian, R -- New York, N.Y. -- Science. 2000 May 26;288(5470):1422-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Molecular and Cell Biology, 401 Barker Hall, University of California, Berkeley, CA 94720-3204, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10827952" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylation ; Amino Acid Motifs ; Amino Acid Sequence ; Binding Sites ; Cloning, Molecular ; Crystallography, X-Ray ; DNA-Binding Proteins/*chemistry/genetics/*metabolism ; Histone Acetyltransferases ; Histones/metabolism ; Humans ; Lysine/analogs & derivatives/chemistry/metabolism ; Models, Molecular ; Molecular Sequence Data ; Nuclear Proteins/*chemistry/genetics/*metabolism ; Nucleosomes/metabolism ; Promoter Regions, Genetic ; Protein Binding ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Recombinant Proteins/chemistry/metabolism ; *TATA-Binding Protein Associated Factors ; *Transcription Factor TFIID ; *Transcription, Genetic
    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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    Phase transitions in the assembly of multivalent signalling proteins (2012)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2012-03-09
    Description: Cells are organized on length scales ranging from angstrom to micrometres. However, the mechanisms by which angstrom-scale molecular properties are translated to micrometre-scale macroscopic properties are not well understood. Here we show that interactions between diverse synthetic, multivalent macromolecules (including multi-domain proteins and RNA) produce sharp liquid-liquid-demixing phase separations, generating micrometre-sized liquid droplets in aqueous solution. This macroscopic transition corresponds to a molecular transition between small complexes and large, dynamic supramolecular polymers. The concentrations needed for phase transition are directly related to the valency of the interacting species. In the case of the actin-regulatory protein called neural Wiskott-Aldrich syndrome protein (N-WASP) interacting with its established biological partners NCK and phosphorylated nephrin, the phase transition corresponds to a sharp increase in activity towards an actin nucleation factor, the Arp2/3 complex. The transition is governed by the degree of phosphorylation of nephrin, explaining how this property of the system can be controlled to regulatory effect by kinases. The widespread occurrence of multivalent systems suggests that phase transitions may be used to spatially organize and biochemically regulate information throughout biology.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3343696/" 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/PMC3343696/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, Pilong -- Banjade, Sudeep -- Cheng, Hui-Chun -- Kim, Soyeon -- Chen, Baoyu -- Guo, Liang -- Llaguno, Marc -- Hollingsworth, Javoris V -- King, David S -- Banani, Salman F -- Russo, Paul S -- Jiang, Qiu-Xing -- Nixon, B Tracy -- Rosen, Michael K -- P30 CA142543/CA/NCI NIH HHS/ -- P41 GM103622/GM/NIGMS NIH HHS/ -- R01 GM056322/GM/NIGMS NIH HHS/ -- R01 GM056322-13/GM/NIGMS NIH HHS/ -- R01-GM088745/GM/NIGMS NIH HHS/ -- R01-GM56322/GM/NIGMS NIH HHS/ -- RR-08630/RR/NCRR NIH HHS/ -- Howard Hughes Medical Institute/ -- England -- Nature. 2012 Mar 7;483(7389):336-40. doi: 10.1038/nature10879.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas, Texas 75390-8812, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22398450" target="_blank"〉PubMed〈/a〉
    Keywords: Actin-Related Protein 2-3 Complex/metabolism ; Adaptor Proteins, Signal Transducing/chemistry/metabolism ; Binding Sites ; Biopolymers/chemistry/metabolism ; Fluorescence Recovery After Photobleaching ; HeLa Cells ; Humans ; Ligands ; Membrane Proteins/chemistry/metabolism ; Multiprotein Complexes/*chemistry/*metabolism ; Oncogene Proteins/chemistry/metabolism ; *Phase Transition ; Phosphorylation ; Proline-Rich Protein Domains ; Protein Structure, Quaternary ; Proteins/*chemistry/*metabolism ; *Signal Transduction ; Wiskott-Aldrich Syndrome Protein, Neuronal/chemistry/metabolism ; src Homology Domains
    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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  • 4
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    Insertion of a coiled-coil peptide from influenza virus hemagglutinin into membranes (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-10-14
    Description: The trimeric protein hemagglutinin (HA) of the influenza viral envelope is essential for cell entry. To investigate the interaction of HA with membranes, two 40-residue, cysteine-substituted peptides comprising the loop region and the first part of the coiled-coil stem were synthesized and modified with a nitroxide spin label. Electron paramagnetic resonance analysis revealed that the peptide inserts reversibly into phospholipid vesicles under endosomal pH conditions. This result suggests that some or all of the long coiled-coil trimer of HA may insert into membranes, which could bring the viral and cell membranes closer together and facilitate fusion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yu, Y G -- King, D S -- Shin, Y K -- New York, N.Y. -- Science. 1994 Oct 14;266(5183):274-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of California, Berkeley.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7939662" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Electron Spin Resonance Spectroscopy ; Endocytosis ; Hemagglutinin Glycoproteins, Influenza Virus ; Hemagglutinins, Viral/chemistry/*metabolism ; Hydrogen-Ion Concentration ; Lipid Bilayers/*metabolism ; *Membrane Fusion ; Molecular Sequence Data ; Orthomyxoviridae/physiology ; Protein Conformation ; Protein Structure, Secondary ; Temperature ; Viral Envelope Proteins/chemistry/*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)
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  • 5
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    Phase separation of signaling molecules promotes T cell receptor signal transduction (2016)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2016-04-09
    Description: Activation of various cell surface receptors triggers the reorganization of downstream signaling molecules into micrometer- or submicrometer-sized clusters. However, the functional consequences of such clustering have been unclear. We biochemically reconstituted a 12-component signaling pathway on model membranes, beginning with T cell receptor (TCR) activation and ending with actin assembly. When TCR phosphorylation was triggered, downstream signaling proteins spontaneously separated into liquid-like clusters that promoted signaling outputs both in vitro and in human Jurkat T cells. Reconstituted clusters were enriched in kinases but excluded phosphatases and enhanced actin filament assembly by recruiting and organizing actin regulators. These results demonstrate that protein phase separation can create a distinct physical and biochemical compartment that facilitates signaling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Su, Xiaolei -- Ditlev, Jonathon A -- Hui, Enfu -- Xing, Wenmin -- Banjade, Sudeep -- Okrut, Julia -- King, David S -- Taunton, Jack -- Rosen, Michael K -- Vale, Ronald D -- 5-F32-DK101188/DK/NIDDK NIH HHS/ -- F32 DK101188/DK/NIDDK NIH HHS/ -- R01 GM056322/GM/NIGMS NIH HHS/ -- R01-GM56322/GM/NIGMS NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2016 Apr 29;352(6285):595-9. doi: 10.1126/science.aad9964. Epub 2016 Apr 7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute (HHMI) Summer Institute, Marine Biological Laboratory, Woods Hole, MA 02543, USA. Department of Cellular and Molecular Pharmacology and Howard Hughes Medical Institute, University of California, San Francisco, CA 94158, USA. ; Howard Hughes Medical Institute (HHMI) Summer Institute, Marine Biological Laboratory, Woods Hole, MA 02543, USA. Department of Biophysics and Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA. ; HHMI Mass Spectrometry Laboratory and Department of Molecular and Cellular Biology, University of California, Berkeley, CA 94720, USA. ; Howard Hughes Medical Institute (HHMI) Summer Institute, Marine Biological Laboratory, Woods Hole, MA 02543, USA. Department of Biophysics and Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA. ron.vale@ucsf.edu michael.rosen@utsouthwestern.edu. ; Howard Hughes Medical Institute (HHMI) Summer Institute, Marine Biological Laboratory, Woods Hole, MA 02543, USA. Department of Cellular and Molecular Pharmacology and Howard Hughes Medical Institute, University of California, San Francisco, CA 94158, USA. ron.vale@ucsf.edu michael.rosen@utsouthwestern.edu.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/27056844" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/*metabolism ; Adaptor Proteins, Signal Transducing/*metabolism ; Fluorescence Recovery After Photobleaching ; Humans ; Jurkat Cells ; Membrane Proteins/*metabolism ; Mitogen-Activated Protein Kinase Kinases ; Phosphorylation ; Polymerization ; Receptors, Antigen, T-Cell/*agonists ; Signal Transduction ; T-Lymphocytes/*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)
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  • 6
    Electronic Resource
    Electronic Resource
    Dynamics of nonthermal reactions: femtosecond surface chemistry (1993)
    s.l. : American Chemical Society
    The @journal of physical chemistry 〈Washington, DC〉 97 (1993), S. 786-798 
    Details
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/j100106a002
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    Paper (German National Licenses)
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  • 7
    Electronic Resource
    Electronic Resource
    Laser-induced desorption: Thermal and nonthermal pathways (1988)
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 88 (1988), S. 6556-6569 
    Details
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Notes: Distributions of internal states and kinetic energies are reported for the laser-induced desorption of NO from a platinum foil. Two desorption channels are observed, one with internal-state populations which are well fit by Boltzmann distribution functions that correspond to the peak surface temperature. The second desorption channel displays population distributions which are non-Boltzmann: kinetic energies exceed the peak surface temperature by a factor of (approximate)5; kinetic energies depend on J; the spin–orbit states are inverted; and the vibrational population exceeds that associated with the maximum surface temperature by a factor of 50. The wavelength dependence of the non-Boltzmann desorption signal suggests that a substrate mediated desorption process is operative.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.454442
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  • 8
    Electronic Resource
    Electronic Resource
    Dynamics of the laser-induced thermal desorption of nitric oxide from a platinum foil (1986)
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 85 (1986), S. 3123-3124 
    Details
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Notes: The internal and translational energy distributions of nitric oxide, which was desorbed from a cold polycrystalline platinum foil by laser-induced thermal desorption, were measured using a laser-excited fluorescence, time-of-flight technique. Under irradiation conditions which are estimated to produce a maximum surface temperature of 320 K, desorbed NO in quantum states with 25〈ER〈2162 cm−1 were represented by two distributions of molecules: a translationally energetic component with a mean kinetic energy 〈ET〉/2k which continuously increased from 1400 to 2650 K with increasing ER, a rotational temperature of TR=410 K, and a vibrational temperature of TV(approximate)900 K; and a slower component with 〈ET〉/2k=300 K and TR=170 K.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.451021
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  • 9
    Electronic Resource
    Electronic Resource
    Dissociation lifetimes and level mixing in overtone-excited HN3(X˜ 1A') (1989)
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 90 (1989), S. 7037-7045 
    Details
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Notes: Vibrational overtone photodissociation is used to examine the spectroscopy and vibrational predissociation lifetimes of HN3 in its ground electronic state. Direct overtone pumping of the N–H stretching levels 5νNH and 6νNH prepares molecules in selected states (v,J,K) near 15 100 and 17 700 cm−1 of vibrational energy; spin-forbidden NH(X 3 Σ−) dissociation fragments are detected by laser-induced fluorescence. Photodissociation spectra of beam-cooled HN3 display mixing of individual rotational levels of the nνNH vibrations with several background states, with derived coupling matrix elements in the range 0.01–0.1 cm−1. Vibrational predissociation lifetimes of mixed components of 5νNH are state specific, with variations of a factor of 2 for only 0.1 cm−1 energy differences. Average lifetimes for low J, K are 210 ns for 5νNH and 0.95 ns for 6νNH. The ratio of decay rates for the two overtone levels, k(6νNH)/k(5νNH)=220, is much greater than predicted by statistical theory, which gives a ratio of 4.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.456230
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  • 10
    Electronic Resource
    Electronic Resource
    A nomenclature for Λ-doublet levels in rotating linear molecules (1988)
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 89 (1988), S. 1749-1753 
    Details
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Notes: It is proposed that the two Λ-doublet levels of linear molecules with nonzero electronic orbital angular momentum be labeled Λ(A') and Λ(A‘), e.g., Π(A') and Π(A‘) for Π states, etc., according to the following prescription: All series of levels in which the electronic wave function at high J is symmetric with reflection of the spatial coordinates of the electrons in the plane of rotation will be designated Λ(A') for all values of J, and all those for which the electronic wave function is antisymmetric with respect to reflection will be denoted Λ(A‘). It is emphasized that this notation is meant to supplement, and not replace, the accepted spectroscopic e/f labeling and the parity quantum number. The utility of the Λ(A')/Λ(A‘) notation is that it is of most relevance in the mechanistic interpretation of reactive or photodissociative processes involving open-shell molecules.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.455121
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