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Book ; Online: Novel repumping on $^{3}$P$_{0}$$\rightarrow$$^{3}$D$_{1}$ for Sr magneto-optical trap and Land\'e g factor measurement of $^{3}$D$_{1}$

Zhang, Shengnan / Ramchurn, Preetam / Menchetti, Marco / Ubaid, Qasim / Jones, Jonathan / Bongs, Kai / Singh, Yeshpal

2020

Abstract: ... the Land\'e g factor of $^{3}$D$_{1}$ of $^{88}$Sr. Thanks to a novel repumping scheme with the $^{3}$P$_{2 ... the resolved-sideband Zeeman spectroscopy, the Land\'e g factor of $^{3}$D$_{1}$ is measured to be 0.4995(88 ...

Abstract	We realize an experimental facility for cooling and trapping strontium (Sr) atoms and measure the Land\'e g factor of $^{3}$D$_{1}$ of $^{88}$Sr. Thanks to a novel repumping scheme with the $^{3}$P$_{2}$$\rightarrow$$^{3}$S$_{1}$ and $^{3}$P$_{0}$$\rightarrow$$^{3}$D$_{1}$ combination and the permanent magnets based self-assembled Zeeman slower, the peak atom number in the continuously repumped blue MOT is enhanced by a factor of 15 with respect to the non-repumping case, and reaches $\sim$1 billion. Furthermore, using the resolved-sideband Zeeman spectroscopy, the Land\'e g factor of $^{3}$D$_{1}$ is measured to be 0.4995(88) showing a good agreement with the theoretical value of 0.4988. The results will have an impact on various applications including atom laser, dipolar interactions, quantum information and precision measurements. Comment: 8 pages, 9 figures
Keywords	Physics - Atomic Physics
Subject code	306
Publishing date	2020-07-20
Publishing country	us
Document type	Book ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Novel tricyclics (e.g., GSK945237) as potent inhibitors of bacterial type IIA topoisomerases.

Bioorganic & medicinal chemistry letters

2016 Volume 26, Issue 10, Page(s) 2464–2469

Abstract: During the course of our research on the lead optimisation of the NBTI (Novel Bacterial Type II Topoisomerase Inhibitors) class of antibacterials, we discovered a series of tricyclic compounds that showed good Gram-positive and Gram-negative potency. ... ...

Abstract	During the course of our research on the lead optimisation of the NBTI (Novel Bacterial Type II Topoisomerase Inhibitors) class of antibacterials, we discovered a series of tricyclic compounds that showed good Gram-positive and Gram-negative potency. Herein we will discuss the various subunits that were investigated in this series and report advanced studies on compound 1 (GSK945237) which demonstrates good PK and in vivo efficacy properties.
Language	English
Publishing date	2016-05-15
Publishing country	England
Document type	Journal Article
ZDB-ID	1063195-1
ISSN	1464-3405 ; 0960-894X
ISSN (online)	1464-3405
ISSN	0960-894X
DOI	10.1016/j.bmcl.2016.03.106
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Article ; Online: Novel hydroxyl tricyclics (e.g., GSK966587) as potent inhibitors of bacterial type IIA topoisomerases.

Bioorganic & medicinal chemistry letters

2013 Volume 23, Issue 19, Page(s) 5437–5441

Abstract: During the course of our research to find novel mode of action antibacterials, we discovered a series of hydroxyl tricyclic compounds that showed good potency against Gram-positive and Gram-negative pathogens. These compounds inhibit bacterial type IIA ... ...

Abstract	During the course of our research to find novel mode of action antibacterials, we discovered a series of hydroxyl tricyclic compounds that showed good potency against Gram-positive and Gram-negative pathogens. These compounds inhibit bacterial type IIA topoisomerases. Herein we will discuss structure-activity relationships in this series and report advanced studies on compound 1 (GSK966587) which demonstrates good PK and in vivo efficacy properties. X-ray crystallographic studies were used to provide insight into the structural basis for the difference in antibacterial potency between enantiomers.
MeSH term(s)	Animals ; Bacteria/enzymology ; Crystallography, X-Ray ; Dogs ; Enzyme Activation/drug effects ; Haplorhini ; Humans ; Microbial Sensitivity Tests ; Molecular Structure ; Naphthyridines/chemistry ; Naphthyridines/pharmacology ; Rats ; Topoisomerase II Inhibitors/chemistry ; Topoisomerase II Inhibitors/pharmacology
Chemical Substances	GSK966587 ; Naphthyridines ; Topoisomerase II Inhibitors
Language	English
Publishing date	2013-10-01
Publishing country	England
Document type	Journal Article
ZDB-ID	1063195-1
ISSN	1464-3405 ; 0960-894X
ISSN (online)	1464-3405
ISSN	0960-894X
DOI	10.1016/j.bmcl.2013.07.013
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Article ; Conference proceedings: Real-World-Ergebnisse der Zugabe von Insulin glargin 300 E/ml (Gla-300) zur GLP-1RA-Therapie bei Menschen mit Typ-2-Diabetes (T2D): Die DELIVER-G-Studie

Bailey, Timothy / Blüher, Matthias / Westerbacka, Jukka / Nicholls, Charlie / Gill, Jasvinder / Merwyn, Jones S / Shenoy, Laxmi

Diabetologie und Stoffwechsel

2022 Volume 17, Issue S 01

Event/congress	Diabetes Kongress 2022 - 56. Jahrestagung der DDG, CityCube Berlin, 2022-05-25
Language	German
Publishing date	2022-05-01
Publisher	Georg Thieme Verlag KG
Publishing place	Stuttgart ; New York
Document type	Article ; Conference proceedings
ZDB-ID	2222993-0
ISSN	1861-9010 ; 1861-9002
ISSN (online)	1861-9010
ISSN	1861-9002
DOI	10.1055/s-0042-1746337
Database	Thieme publisher's database

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Zs.A 6479: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular ab Jg. 2022: Lesesaal (EG)
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Article: Measurement of G(E(p))/G(M(p)) in e(-->)p---> e(-->)p to Q(2) = 5.6 GeV(2).

Gayou, O / Aniol, K A / Averett, T / Benmokhtar, F / Bertozzi, W / Bimbot, L / Brash, E J / Calarco, J R / Cavata, C / Chai, Z / Chang, C-C / Chang, T / Chen, J-P / Chudakov, E / De Leo, R / Dieterich, S / Endres, R / Epstein, M B / Escoffier, S /

Fissum, K G / Fonvieille, H / Frullani, S / Gao, J / Garibaldi, F / Gilad, S / Gilman, R / Glamazdin, A / Glashausser, C / Gomez, J / Gorbenko, V / Hansen, J-O / Higinbotham, D W / Huber, G M / Iodice, M / de Jager, C W / Jiang, X / Jones, M K / Kelly, J J / Khandaker, M / Kozlov, A / Kramer, K M / Kumbartzki, G / LeRose, J J / Lhuillier, D / Lindgren, R A / Liyanage, N / Lolos, G J / Margaziotis, D J / Marie, F / Markowitz, P / McCormick, K / Michaels, R / Milbrath, B D / Nanda, S K / Neyret, D / Papandreou, Z / Pentchev, L / Perdrisat, C F / Piskunov, N M / Punjabi, V / Pussieux, T / Quéméner, G / Ransome, R D / Raue, B A / Roché, R / Rvachev, M / Saha, A / Salgado, C / Sirca, S / Sitnik, I / Strauch, S / Todor, L / Tomasi-Gustafsson, E / Urciuoli, G M / Voskanyan, H / Wijesooriya, K / Wojtsekhowski, B B / Zheng, X / Zhu, L

Physical review letters

2002 Volume 88, Issue 9, Page(s) 92301

Abstract: The ratio of the electric and magnetic form factors of the proton G(E(p))/G(M(p)), which is ... in the elastic e(-->)p---> e(-->)p reaction. The new data presented span the range 3.5< Q(2)< 5.6 GeV(2) and are ...

Abstract	The ratio of the electric and magnetic form factors of the proton G(E(p))/G(M(p)), which is an image of its charge and magnetization distributions, was measured at the Thomas Jefferson National Accelerator Facility (JLab) using the recoil polarization technique. The ratio of the form factors is directly proportional to the ratio of the transverse to longitudinal components of the polarization of the recoil proton in the elastic e(-->)p---> e(-->)p reaction. The new data presented span the range 3.5< Q(2)< 5.6 GeV(2) and are well described by a linear Q(2) fit. Also, the ratio sqrt[Q(2)] F(2(p))/F(1(p)) reaches a constant value above Q(2) = 2 GeV(2).
Language	English
Publishing date	2002-03-04
Publishing country	United States
Document type	Journal Article
ZDB-ID	208853-8
ISSN	1079-7114 ; 0031-9007
ISSN (online)	1079-7114
ISSN	0031-9007
DOI	10.1103/PhysRevLett.88.092301
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Article: Measurements of the proton elastic-form-factor ratio mu pG p E/G p M at low momentum transfer.

Ron, G / Glister, J / Lee, B / Allada, K / Armstrong, W / Arrington, J / Beck, A / Benmokhtar, F / Berman, B L / Boeglin, W / Brash, E / Camsonne, A / Calarco, J / Chen, J P / Choi, Seonho / Chudakov, E / Coman, L / Craver, B / Cusanno, F /

Dumas, J / Dutta, C / Feuerbach, R / Freyberger, A / Frullani, S / Garibaldi, F / Gilman, R / Hansen, O / Higinbotham, D W / Holmstrom, T / Hyde, C E / Ibrahim, H / Ilieva, Y / de Jager, C W / Jiang, X / Jones, M K / Kang, H / Kelleher, A / Khrosinkova, E / Kuchina, E / Kumbartzki, G / LeRose, J J / Lindgren, R / Markowitz, P / May-Tal Beck, S / McCullough, E / Meekins, D / Meziane, M / Meziani, Z-E / Michaels, R / Moffit, B / Norum, B E / Oh, Y / Olson, M / Paolone, M / Paschke, K / Perdrisat, C F / Piasetzky, E / Potokar, M / Pomatsalyuk, R / Pomerantz, I / Puckett, A / Punjabi, V / Qian, X / Qiang, Y / Ransome, R / Reyhan, M / Roche, J / Rousseau, Y / Saha, A / Sarty, A J / Sawatzky, B / Schulte, E / Shabestari, M / Shahinyan, A / Shneor, R / Sirca, S / Slifer, K / Solvignon, P / Song, J / Sparks, R / Subedi, R / Strauch, S / Urciuoli, G M / Wang, K / Wojtsekhowski, B / Yan, X / Yao, H / Zhan, X / Zhu, X

Physical review letters

2007 Volume 99, Issue 20, Page(s) 202002

Abstract: High-precision measurements of the proton elastic form-factor ratio, mu pG p E/G p M, have been ... measurement, one finds that in this Q2 range the deviation from unity is primarily due to G p E being smaller ...

Abstract	High-precision measurements of the proton elastic form-factor ratio, mu pG p E/G p M, have been made at four-momentum transfer, Q2, values between 0.2 and 0.5 GeV2. The new data, while consistent with previous results, clearly show a ratio less than unity and significant differences from the central values of several recent phenomenological fits. By combining the new form-factor ratio data with an existing cross-section measurement, one finds that in this Q2 range the deviation from unity is primarily due to G p E being smaller than expected.
Language	English
Publishing date	2007-11-16
Publishing country	United States
Document type	Journal Article
ZDB-ID	208853-8
ISSN	1079-7114 ; 0031-9007
ISSN (online)	1079-7114
ISSN	0031-9007
DOI	10.1103/PhysRevLett.99.202002
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Article ; Online: A site-directed cross-linking approach to the characterization of subunit E-subunit G contacts in the vacuolar H+-ATPase stator.

Jones, Richard P O / Durose, Lyndsey J / Phillips, Clair / Keen, Jeffrey N / Findlay, John B C / Harrison, Michael A

Molecular membrane biology

2010 Volume 27, Issue 4-6, Page(s) 147–159

Abstract: ... resolution structural data and spectroscopic analysis indicate that a filament-like subunit E/subunit G ... type ATPases, the N-terminal alpha-helical segments of the G and E subunits are closely aligned over ... end of G is anchored at the C-terminal globular domain of subunit E. These data are consistent ...

Abstract	To operate as a rotary motor, the ATP-hydrolyzing domain of the vacuolar H(+)-ATPase must be connected to a fixed structure in its membrane-bound proton pump domain by a mechanical stator. Although low-resolution structural data and spectroscopic analysis indicate that a filament-like subunit E/subunit G heterodimer performs this role, more detailed information about the relative arrangement of these subunits is limited. We have used a site-directed cross-linking approach to show that, in both bacterial and yeast V-type ATPases, the N-terminal alpha-helical segments of the G and E subunits are closely aligned over a distance of up to 40 A. Furthermore, cross-linking coupled to mass spectrometry shows that the C-terminal end of G is anchored at the C-terminal globular domain of subunit E. These data are consistent with a stator model comprising two approximately 150 A long parallel alpha-helices linked to each other at both ends, stabilized by a coiled-coil arrangement and capped by the globular C-terminal domain of E that connects the cytoplasmic end of the helical structure to the V-ATPase catalytic domain.
MeSH term(s)	Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Circular Dichroism ; Cross-Linking Reagents/chemistry ; Disulfides/chemistry ; Enterococcus/enzymology ; Enterococcus/genetics ; Immunoblotting ; Models, Molecular ; Mutagenesis, Site-Directed ; Peptide Fragments/chemistry ; Peptide Fragments/metabolism ; Protein Subunits/chemistry ; Protein Subunits/genetics ; Protein Subunits/metabolism ; Recombinant Proteins/biosynthesis ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Saccharomyces cerevisiae/enzymology ; Saccharomyces cerevisiae Proteins/chemistry ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Vacuolar Proton-Translocating ATPases/chemistry ; Vacuolar Proton-Translocating ATPases/genetics ; Vacuolar Proton-Translocating ATPases/metabolism
Chemical Substances	Bacterial Proteins ; Cross-Linking Reagents ; Disulfides ; Peptide Fragments ; Protein Subunits ; Recombinant Proteins ; Saccharomyces cerevisiae Proteins ; Vacuolar Proton-Translocating ATPases (EC 3.6.1.-)
Language	English
Publishing date	2010-08
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1186324-9
ISSN	1464-5203 ; 0968-7688
ISSN (online)	1464-5203
ISSN	0968-7688
DOI	10.3109/09687681003796441
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Article: Novel hydroxyl tricyclics (e.g., GSK966587) as potent inhibitors of bacterial type IIA topoisomerases

Bioorganic & medicinal chemistry letters. 2013 Oct. 1, v. 23, no. 19

2013

Abstract	During the course of our research to find novel mode of action antibacterials, we discovered a series of hydroxyl tricyclic compounds that showed good potency against Gram-positive and Gram-negative pathogens. These compounds inhibit bacterial type IIA topoisomerases. Herein we will discuss structure–activity relationships in this series and report advanced studies on compound 1 (GSK966587) which demonstrates good PK and in vivo efficacy properties. X-ray crystallographic studies were used to provide insight into the structural basis for the difference in antibacterial potency between enantiomers.
Keywords	X-ray diffraction ; enantiomers ; mechanism of action ; pathogens ; structure-activity relationships
Language	English
Dates of publication	2013-1001
Size	p. 5437-5441.
Publishing place	Elsevier Ltd
Document type	Article
ZDB-ID	1063195-1
ISSN	1464-3405 ; 0960-894X
ISSN (online)	1464-3405
ISSN	0960-894X
DOI	10.1016/j.bmcl.2013.07.013
Database	NAL-Catalogue (AGRICOLA)

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Article: Defined sites of interaction between subunits E (Vma4p), C (Vma5p), and G (Vma10p) within the stator structure of the vacuolar H+-ATPase.

Jones, Richard P O / Durose, Lyndsey J / Findlay, John B C / Harrison, Michael A

Biochemistry

2005 Volume 44, Issue 10, Page(s) 3933–3941

Abstract: ... that subunits Vma5p (subunit C) and Vma10p (subunit G), expressed as glutathione-S-transferase fusion proteins ... in E. coli, are both able to interact strongly with Vma4p (subunit E) expressed in a cell-free system ...

Abstract	Vacuolar H(+)-ATPases (V-ATPases) are multi-subunit membrane proteins that couple ATP hydrolysis to the extrusion of protons from the cytoplasm. Although they share a common macromolecular architecture and rotational mechanism with the F(1)F(0)-ATPases, the organization of many of the specialized V-ATPase subunits within this rotary molecular motor remains uncertain. In this study, we have identified sequence segments involved in linking putative stator subunits in the Saccharomyces V-ATPase. Precipitation assays revealed that subunits Vma5p (subunit C) and Vma10p (subunit G), expressed as glutathione-S-transferase fusion proteins in E. coli, are both able to interact strongly with Vma4p (subunit E) expressed in a cell-free system. GST-Vma10p also associated with Vma2p and Vma1p, the core subunits of the ATP-hydrolyzing domain, and was able to self-associate to form a dimer. Mutations within the first 19-residue region of Vma4p, which disrupted interaction with Vma5p in vitro, also prevented the Vma4p polypeptide from restoring V-ATPase function in a complementation assay in vivo. These mutations did not prevent assembly of Vma5p (subunit C) and Vma2p (subunit B) into an inactive complex at the vacuolar membrane, indicating that Vma5p must make multiple interactions involving other V-ATPase subunits. A second, highly conserved region of Vma4p between residues 19 and 38 is involved in binding Vma10p. This region is highly enriched in charged residues, suggesting a role for electrostatic effects in Vma4p-Vma10p interaction. These protein interaction studies show that the N-terminal region of Vma4p is a key factor not only in the stator structure of the V-ATPase rotary molecular motor, but also in mediating interactions with putative regulatory subunits.
MeSH term(s)	Amino Acid Sequence ; Animals ; Cell-Free System/enzymology ; Escherichia coli/enzymology ; Escherichia coli/genetics ; Genetic Complementation Test ; Humans ; Molecular Motor Proteins/biosynthesis ; Molecular Motor Proteins/genetics ; Molecular Motor Proteins/metabolism ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Protein Interaction Mapping ; Protein Processing, Post-Translational/genetics ; Protein Subunits/biosynthesis ; Protein Subunits/genetics ; Protein Subunits/metabolism ; Recombinant Fusion Proteins/biosynthesis ; Recombinant Fusion Proteins/genetics ; Recombinant Fusion Proteins/metabolism ; Saccharomyces cerevisiae/enzymology ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae Proteins/biosynthesis ; Saccharomyces cerevisiae Proteins/chemistry ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Vacuolar Proton-Translocating ATPases/biosynthesis ; Vacuolar Proton-Translocating ATPases/chemistry ; Vacuolar Proton-Translocating ATPases/genetics ; Vacuolar Proton-Translocating ATPases/metabolism
Chemical Substances	Molecular Motor Proteins ; Protein Subunits ; Recombinant Fusion Proteins ; Saccharomyces cerevisiae Proteins ; VMA3 protein, S cerevisiae ; VMA5 protein, S cerevisiae ; Vma4 protein, S cerevisiae ; VMA10 protein, S cerevisiae (EC 3.6.1.-) ; Vacuolar Proton-Translocating ATPases (EC 3.6.1.-)
Language	English
Publishing date	2005-01-26
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1108-3
ISSN	1520-4995 ; 0006-2960
ISSN (online)	1520-4995
ISSN	0006-2960
DOI	10.1021/bi048402x
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Article: Low-frequency spectral analysis of the e.m.g.

Lago, P J / Jones, N B

Medical & biological engineering & computing

1981 Volume 19, Issue 6, Page(s) 779–782

MeSH term(s)	Action Potentials ; Electromyography/methods ; Humans ; Motor Neurons/physiology ; Muscle Contraction ; Muscles/innervation
Language	English
Publishing date	1981-11
Publishing country	United States
Document type	Journal Article
ZDB-ID	282327-5
ISSN	1741-0444 ; 0140-0118 ; 0025-696X
ISSN (online)	1741-0444
ISSN	0140-0118 ; 0025-696X
DOI	10.1007/bf02441342
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