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  • 1
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    Measurement of the variation of electron-to-proton mass ratio using ultracold molecules produced from laser-cooled atoms (2019)
    Springer Nature
    Details
    Publication Date: 2019
    Electronic ISSN: 2041-1723
    Topics: Biology , Chemistry and Pharmacology , Natural Sciences in General , Physics
    Published by Springer Nature
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  • 2
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    Predicting and verifying transition strengths from weakly bound molecules (2011)
    American Physical Society (APS)
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    Publication Date: 2011-04-12
    Description: Author(s): K. Aikawa, D. Akamatsu, M. Hayashi, J. Kobayashi, M. Ueda, and S. Inouye We investigated transition strengths from ultracold weakly bound ^{41} K ^{87} Rb molecules produced via the photoassociation of laser-cooled atoms. An accurate potential energy curve of the excited state (3)^{1} Σ^{+} was constructed by carrying out direct potential fit analysis of rotational spec... [Phys. Rev. A 83, 042706] Published Mon Apr 11, 2011
    Keywords: Atomic and molecular collisions and interactions
    Print ISSN: 1050-2947
    Electronic ISSN: 1094-1622
    Topics: Physics
    Published by American Physical Society (APS)
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  • 3
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    Superradiant rayleigh scattering from a bose-einstein condensate (1999)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1999-07-27
    Description: Rayleigh scattering off a Bose-Einstein condensate was studied. Exposing an elongated condensate to a single off-resonant laser beam resulted in the observation of highly directional scattering of light and atoms. This collective light scattering is caused by the coherent center-of-mass motion of the atoms in the condensate. A directional beam of recoiling atoms was built up by matter wave amplification.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Inouye -- Chikkatur -- Stamper-Kurn -- Stenger -- Pritchard -- Ketterle -- New York, N.Y. -- Science. 1999 Jul 23;285(5427):571-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physics and Research Laboratory of Electronics, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10417384" 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
    Published by American Association for the Advancement of Science (AAAS)
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  • 4
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    Reverse transcriptase in a clinical strain of Escherichia coli: production of branched RNA-linked msDNA (1989)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1989-02-24
    Description: Branched RNA-linked multicopy single-stranded DNA (msDNA) originally detected in myxobacteria has now been found in a clinical isolate of Escherichia coli. Although lacking homology in the primary structure, the E. coli msDNA is similar in secondary structure to the myxobacterial msDNA's, including the 2',5'-phosphodiester linkage between RNA and DNA. A chromosomal DNA fragment responsible for the production of msDNA was cloned in an E. coli K12 strain; its DNA sequence revealed an open reading frame (ORF) of 586 amino acid residues. The ORF shows sequence similarity with retroviral reverse transcriptases and ribonuclease H. Disruption of the ORF blocked msDNA production, indicating that this gene is essential for msDNA synthesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lampson, B C -- Sun, J -- Hsu, M Y -- Vallejo-Ramirez, J -- Inouye, S -- Inouye, M -- F32 GM11970-01A1/GM/NIGMS NIH HHS/ -- GM26843/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1989 Feb 24;243(4894 Pt 1):1033-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Robert Wood Johnson Medical School, University of Medicine and Dentistry of New Jersey, Piscataway 08854.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2466332" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cloning, Molecular ; DNA Probes ; DNA Restriction Enzymes ; DNA, Bacterial/genetics ; DNA, Single-Stranded/analysis/biosynthesis/*genetics ; Endoribonucleases/genetics ; Escherichia coli/enzymology/*genetics ; Genes, Bacterial ; HIV/enzymology/genetics ; Human T-lymphotropic virus 1/enzymology/genetics ; Molecular Sequence Data ; Myxococcales/genetics ; Nucleic Acid Hybridization ; RNA, Bacterial/analysis/biosynthesis/*genetics ; RNA-Directed DNA Polymerase/*genetics ; Retroviridae/*enzymology/genetics ; Ribonuclease H ; Sequence Homology, Nucleic Acid ; Transformation, Bacterial
    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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    Bosonic stimulation in the formation of a bose-einstein condensate (1998)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1998-02-27
    Description: The formation of a Bose-Einstein condensate of a dilute atomic gas has been studied in situ with a nondestructive, time-resolved imaging technique. Sodium atoms were evaporatively cooled close to the onset of Bose-Einstein condensation and then suddenly quenched to below the transition temperature. The subsequent equilibration and condensate formation showed a slow onset distinctly different from simple relaxation. This behavior provided evidence for the process of bosonic stimulation, or coherent matter-wave amplification, crucial to the concept of an atom laser.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miesner -- Stamper-Kurn -- Andrews -- Durfee -- Inouye -- Ketterle -- New York, N.Y. -- Science. 1998 Feb 13;279(5353):1005-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physics and Research Laboratory of Electronics, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9461427" 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
    Published by American Association for the Advancement of Science (AAAS)
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  • 6
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    Retronphage phi R73: an E. coli phage that contains a retroelement and integrates into a tRNA gene (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-05-17
    Description: Some strains of Escherichia coli contain retroelements (retrons) that encode genes for reverse transcriptase and branched, multicopy, single-stranded DNA (msDNA) linked to RNA. However, the origin of retrons is unknown. A P4-like cryptic prophage was found that contains a retroelement (retron Ec73) for msDNA-Ec73 in an E. coli clinical strain. The entire genome of this prophage, named phi R73, is 12.7 kilobase pairs and is flanked by 29-base pair direct repeats derived from the 3' end of the selenocystyl transfer RNA gene (selC). P2 bacteriophage caused excision of the phi R73 prophage and acted as a helper to package phi R73 DNA into an infectious virion. The newly formed phi R73 closely resembled P4 as a virion and in its lytic growth. Retronphage phi R73 lysogenized a new host strain, reintegrating its genome into the selC gene of the host chromosome and enabling the newly formed lysogens to produce msDNA-Ec73. Hence, retron Ec73 can be transferred intercellularly as part of the genome of a helper-dependent retronphage.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Inouye, S -- Sunshine, M G -- Six, E W -- Inouye, M -- AI04043/AI/NIAID NIH HHS/ -- GM44012/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1991 May 17;252(5008):969-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Robert Wood Johnson Medical School, University of Medicine and Dentistry of New Jersey at Rutgers, Piscataway 08854.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1709758" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Blotting, Southern ; Chromosome Mapping ; Coliphages/*genetics/ultrastructure ; DNA, Bacterial/genetics ; DNA, Viral/genetics ; Escherichia coli/*genetics ; *Genes, Bacterial ; *Genes, Viral ; Microscopy, Electron ; Molecular Sequence Data ; Nucleic Acid Hybridization ; Oligonucleotide Probes ; Open Reading Frames ; RNA, Transfer/*genetics ; RNA-Directed DNA Polymerase/genetics
    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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    Requirement for signal peptide cleavage of Escherichia coli prolipoprotein (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1983-07-01
    Description: Oligonucleotide-directed site-specific mutagenesis was applied to alter the cleavage site in the signal peptide of the major outer membrane lipoprotein of Escherichia coli. Replacing the glycine residue at the cleavage site with an alanine residue did not affect the processing of the signal peptide. However, when the same cleavage site was constructed by the deletion of the glycine residue, the signal peptide was no longer cleaved. These results indicate that stringent structural integrity at the cleavage site in the lipoprotein signal sequence is required for correct processing of prolipoprotein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Inouye, S -- Hsu, C P -- Itakura, K -- Inouye, M -- GM19043/GM/NIGMS NIH HHS/ -- GM30395/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1983 Jul 1;221(4605):59-61.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6344218" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Bacterial Outer Membrane Proteins ; Base Sequence ; DNA, Bacterial/metabolism ; Electrophoresis, Polyacrylamide Gel ; Escherichia coli/*metabolism ; *Escherichia coli Proteins ; Lipoproteins/*biosynthesis ; Membrane Proteins/biosynthesis ; Mutation ; Protein Precursors/*biosynthesis
    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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    Role of talin in membrane-cytoskeleton linkage [Cell Biology] (2012)
    National Academy of Sciences
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    Publication Date: 2012-08-08
    Description: Contraction of the cortical actin cytoskeleton underlies both rear retraction in directed cell migration and cytokinesis. Here, we show that talin, a central component of focal adhesions, has a major role in these processes. We found that Dictyostelium talin A colocalized with myosin II in the rear of migrating cells and the cleavage furrow. During directed cell migration, talin A-null cells displayed a long thin tail devoid of actin filaments, whereas additional depletion of SibA, a transmembrane adhesion molecule that binds to talin A, reverted this phenotype, suggesting a requirement of the link between actomyosin and SibA by talin A for rear retraction. Disruptions of talin A also resulted in detachment of the actomyosin contractile ring from the cell membrane and concomitant regression of the cleavage furrow under certain conditions. The C-terminal actin-binding domain (ABD) of talin A exhibited a localization pattern identical to that of full-length talin A. The N-terminal FERM domain was found to bind phosphatidylinositol 4,5-bisphosphate [PtdIns(4,5)P2] and phosphatidylinositol 3,4,5-trisphosphate [PtdIns(3,4,5)P3] in vitro. In vivo, however, PtdIns(4,5)P2, which is known to activate talin, is believed to be enriched in the rear of migrating cells and the cleavage furrow in Dictyostelium. From these results, we propose that talin A activated by PtdIns(4,5)P2 in the cell posterior or cleavage furrow links actomyosin cytoskeleton to adhesion molecules or other membrane proteins, and that the force is transmitted through these links to retract the tail during cell migration or to cause efficient ingression of the equator during cytokinesis.
    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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  • 9
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    Prospects for narrow-line cooling of KRb molecules in the rovibrational ground state (2014)
    American Physical Society (APS)
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    Publication Date: 2014-02-06
    Description: Author(s): J. Kobayashi, K. Aikawa, K. Oasa, and S. Inouye We propose and experimentally investigate a scheme for narrow-line cooling of KRb molecules in the rovibrational ground state. We show that the spin-forbidden X1Σ+→b3Π0+ transition of KRb is well suited for realizing narrow-line laser cooling of molecules because it has highly diagonal Franck-Condon... [Phys. Rev. A 89, 021401] Published Wed Feb 05, 2014
    Keywords: Atomic and molecular processes in external fields, including interactions with strong fields and short pulses
    Print ISSN: 1050-2947
    Electronic ISSN: 1094-1622
    Topics: Physics
    Published by American Physical Society (APS)
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  • 10
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    Isotopic Shift of Atom-Dimer Efimov Resonances in K-Rb Mixtures: Critical Effect of Multichannel Feshbach Physics (2017)
    American Physical Society (APS)
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    Publication Date: 2017-04-18
    Description: Author(s): K. Kato, Yujun Wang, J. Kobayashi, P. S. Julienne, and S. Inouye Multichannel Efimov physics is investigated in ultracold heteronuclear admixtures of K and Rb atoms. We observe a shift in the scattering length where the first atom-dimer resonance appears in the K 41 − Rb 87 system relative to the position of the previously observed atom-dimer resonance in the K 40 − Rb 8… [Phys. Rev. Lett. 118, 163401] Published Mon Apr 17, 2017
    Keywords: Atomic, Molecular, and Optical Physics
    Print ISSN: 0031-9007
    Electronic ISSN: 1079-7114
    Topics: Physics
    Published by American Physical Society (APS)
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