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  • 1
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    Biophysics: Transporter in the spotlight (2010)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2010-05-14
    Description: 〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2883250/" 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/PMC2883250/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Karpowich, Nathan K -- Wang, Da-Neng -- F32 HL091618-03/HL/NHLBI NIH HHS/ -- R01 DK053973/DK/NIDDK NIH HHS/ -- R01 DK053973-12/DK/NIDDK NIH HHS/ -- R01 GM093825/GM/NIGMS NIH HHS/ -- R01 GM093825-01/GM/NIGMS NIH HHS/ -- R01 MH083840/MH/NIMH NIH HHS/ -- R01 MH083840-03/MH/NIMH NIH HHS/ -- R21 GM075936/GM/NIGMS NIH HHS/ -- R21 GM075936-02/GM/NIGMS NIH HHS/ -- U54 GM075026/GM/NIGMS NIH HHS/ -- U54 GM075026-050010/GM/NIGMS NIH HHS/ -- England -- Nature. 2010 May 13;465(7295):171-2. doi: 10.1038/465171a.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20463728" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/*chemistry/*metabolism ; Crystallography, X-Ray ; Fluorescence Resonance Energy Transfer ; Molecular Dynamics Simulation ; Plasma Membrane Neurotransmitter Transport Proteins/*chemistry/*metabolism ; Protein Conformation ; Sodium/metabolism
    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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  • 2
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    LeuT-desipramine structure reveals how antidepressants block neurotransmitter reuptake (2007)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2007-08-11
    Description: Tricyclic antidepressants exert their pharmacological effect-inhibiting the reuptake of serotonin, norepinephrine, and dopamine-by directly blocking neurotransmitter transporters (SERT, NET, and DAT, respectively) in the presynaptic membrane. The drug-binding site and the mechanism of this inhibition are poorly understood. We determined the crystal structure at 2.9 angstroms of the bacterial leucine transporter (LeuT), a homolog of SERT, NET, and DAT, in complex with leucine and the antidepressant desipramine. Desipramine binds at the inner end of the extracellular cavity of the transporter and is held in place by a hairpin loop and by a salt bridge. This binding site is separated from the leucine-binding site by the extracellular gate of the transporter. By directly locking the gate, desipramine prevents conformational changes and blocks substrate transport. Mutagenesis experiments on human SERT and DAT indicate that both the desipramine-binding site and its inhibition mechanism are probably conserved in the human neurotransmitter transporters.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3711652/" 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/PMC3711652/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhou, Zheng -- Zhen, Juan -- Karpowich, Nathan K -- Goetz, Regina M -- Law, Christopher J -- Reith, Maarten E A -- Wang, Da-Neng -- DA013261/DA/NIDA NIH HHS/ -- DA019676/DA/NIDA NIH HHS/ -- GM075026/GM/NIGMS NIH HHS/ -- GM075936/GM/NIGMS NIH HHS/ -- R01 DA013261/DA/NIDA NIH HHS/ -- R01 DA019676/DA/NIDA NIH HHS/ -- R01 DK053973/DK/NIDDK NIH HHS/ -- R21 DK060841/DK/NIDDK NIH HHS/ -- R21 GM075936/GM/NIGMS NIH HHS/ -- U54 GM075026/GM/NIGMS NIH HHS/ -- U54 GM095315/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 Sep 7;317(5843):1390-3. Epub 2007 Aug 9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Kimmel Center for Biology and Medicine at the Skirball Institute of Biomolecular Medicine and Department of Cell Biology, New York University School of Medicine, 540 First Avenue, New York, NY 10016, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17690258" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antidepressive Agents, Tricyclic/chemistry/*metabolism ; Bacterial Proteins/chemistry/*metabolism ; Binding Sites ; Caenorhabditis elegans Proteins/chemistry/metabolism ; Cell Line ; Conserved Sequence ; Crystallography, X-Ray ; Desipramine/chemistry/*metabolism ; Dopamine/chemistry/metabolism ; Dopamine Uptake Inhibitors/chemistry/metabolism ; Drosophila Proteins/chemistry/metabolism ; Humans ; Leucine/chemistry/metabolism ; Models, Molecular ; Molecular Sequence Data ; Neurotransmitter Uptake Inhibitors/chemistry/*metabolism ; Norepinephrine/chemistry/metabolism ; Norepinephrine Plasma Membrane Transport Proteins/antagonists & ; inhibitors/chemistry/metabolism ; Plasma Membrane Neurotransmitter Transport Proteins/chemistry/*metabolism ; Protein Binding ; Protein Conformation ; Sequence Homology, Amino Acid ; Serotonin/chemistry/metabolism ; Serotonin Uptake Inhibitors/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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    Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-08-02
    Description: The major facilitator superfamily represents the largest group of secondary membrane transporters in the cell. Here we report the 3.3 angstrom resolution structure of a member of this superfamily, GlpT, which transports glycerol-3-phosphate into the cytoplasm and inorganic phosphate into the periplasm. The amino- and carboxyl-terminal halves of the protein exhibit a pseudo two-fold symmetry. Closed off to the periplasm, a centrally located substrate-translocation pore contains two arginines at its closed end, which comprise the substrate-binding site. Upon substrate binding, the protein adopts a more compact conformation. We propose that GlpT operates by a single-binding site, alternating-access mechanism through a rocker-switch type of movement.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huang, Yafei -- Lemieux, M Joanne -- Song, Jinmei -- Auer, Manfred -- Wang, Da-Neng -- New York, N.Y. -- Science. 2003 Aug 1;301(5633):616-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Skirball Institute of Biomolecular Medicine and Department of Cell Biology, New York University School of Medicine, 540 First Avenue, New York, NY 10016, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12893936" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Biological Transport ; Cell Membrane/chemistry ; Crystallization ; Crystallography, X-Ray ; Escherichia coli/*chemistry/enzymology ; Escherichia coli Proteins/chemistry/metabolism ; Glycerophosphates/*metabolism ; Helix-Turn-Helix Motifs ; Mass Spectrometry ; Membrane Transport Proteins/*chemistry/*metabolism ; Models, Molecular ; Molecular Sequence Data ; Periplasm/metabolism ; Phosphates/metabolism ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary
    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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    Identification and characterization of a bacterial hydrosulphide ion channel (2012)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2012-03-13
    Description: The hydrosulphide ion (HS(-)) and its undissociated form, hydrogen sulphide (H(2)S), which are believed to have been critical to the origin of life on Earth, remain important in physiology and cellular signalling. As a major metabolite in anaerobic bacterial growth, hydrogen sulphide is a product of both assimilatory and dissimilatory sulphate reduction. These pathways can reduce various oxidized sulphur compounds including sulphate, sulphite and thiosulphate. The dissimilatory sulphate reduction pathway uses this molecule as the terminal electron acceptor for anaerobic respiration, in which process it produces excess amounts of H(2)S (ref. 4). The reduction of sulphite is a key intermediate step in all sulphate reduction pathways. In Clostridium and Salmonella, an inducible sulphite reductase is directly linked to the regeneration of NAD(+), which has been suggested to have a role in energy production and growth, as well as in the detoxification of sulphite. Above a certain concentration threshold, both H(2)S and HS(-) inhibit cell growth by binding the metal centres of enzymes and cytochrome oxidase, necessitating a release mechanism for the export of this toxic metabolite from the cell. Here we report the identification of a hydrosulphide ion channel in the pathogen Clostridium difficile through a combination of genetic, biochemical and functional approaches. The HS(-) channel is a member of the formate/nitrite transport family, in which about 50 hydrosulphide ion channels form a third subfamily alongside those for formate (FocA) and for nitrite (NirC). The hydrosulphide ion channel is permeable to formate and nitrite as well as to HS(-) ions. Such polyspecificity can be explained by the conserved ion selectivity filter observed in the channel's crystal structure. The channel has a low open probability and is tightly regulated, to avoid decoupling of the membrane proton gradient.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3711795/" 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/PMC3711795/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Czyzewski, Bryan K -- Wang, Da-Neng -- F31 AI086072/AI/NIAID NIH HHS/ -- F31-AI086072/AI/NIAID NIH HHS/ -- R01 DK053973/DK/NIDDK NIH HHS/ -- R01 GM093825/GM/NIGMS NIH HHS/ -- R01 MH083840/MH/NIMH NIH HHS/ -- R01-DK053973-08A1S1/DK/NIDDK NIH HHS/ -- R01-DK073973/DK/NIDDK NIH HHS/ -- R01-GM093825/GM/NIGMS NIH HHS/ -- R01-MH083840/MH/NIMH NIH HHS/ -- U54 GM075026/GM/NIGMS NIH HHS/ -- U54-GM075026/GM/NIGMS NIH HHS/ -- England -- Nature. 2012 Mar 11;483(7390):494-7. doi: 10.1038/nature10881.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Helen L. and Martin S. Kimmel Center for Biology and Medicine at the Skirball Institute of Biomolecular Medicine, New York University School of Medicine, 540 First Avenue, New York, New York 10016, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22407320" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/chemistry/genetics/isolation & purification/metabolism ; *Clostridium difficile/chemistry/drug effects/genetics ; Crystallography, X-Ray ; Formates/metabolism ; Ion Channel Gating ; Ion Channels/chemistry/genetics/*isolation & purification/*metabolism ; Ion Transport ; Models, Biological ; Models, Molecular ; Nitrites/metabolism ; Operon/genetics ; Proteolipids/metabolism ; Proton-Motive Force ; Structure-Activity Relationship ; Substrate Specificity ; Sulfides/*metabolism/toxicity
    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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    Structure and mechanism of a bacterial sodium-dependent dicarboxylate transporter (2012)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2012-10-23
    Description: In human cells, cytosolic citrate is a chief precursor for the synthesis of fatty acids, triacylglycerols, cholesterol and low-density lipoprotein. Cytosolic citrate further regulates the energy balance of the cell by activating the fatty-acid-synthesis pathway while downregulating both the glycolysis and fatty-acid beta-oxidation pathways. The rate of fatty-acid synthesis in liver and adipose cells, the two main tissue types for such synthesis, correlates directly with the concentration of citrate in the cytosol, with the cytosolic citrate concentration partially depending on direct import across the plasma membrane through the Na(+)-dependent citrate transporter (NaCT). Mutations of the homologous fly gene (Indy; I'm not dead yet) result in reduced fat storage through calorie restriction. More recently, Nact (also known as Slc13a5)-knockout mice have been found to have increased hepatic mitochondrial biogenesis, higher lipid oxidation and energy expenditure, and reduced lipogenesis, which taken together protect the mice from obesity and insulin resistance. To understand the transport mechanism of NaCT and INDY proteins, here we report the 3.2 A crystal structure of a bacterial INDY homologue. One citrate molecule and one sodium ion are bound per protein, and their binding sites are defined by conserved amino acid motifs, forming the structural basis for understanding the specificity of the transporter. Comparison of the structures of the two symmetrical halves of the transporter suggests conformational changes that propel substrate translocation.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3617922/" 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/PMC3617922/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mancusso, Romina -- Gregorio, G Glenn -- Liu, Qun -- Wang, Da-Neng -- P30 EB009998/EB/NIBIB NIH HHS/ -- R01 DK053973/DK/NIDDK NIH HHS/ -- R01 GM093825/GM/NIGMS NIH HHS/ -- R01 MH083840/MH/NIMH NIH HHS/ -- R01-DK073973/DK/NIDDK NIH HHS/ -- R01-GM093825/GM/NIGMS NIH HHS/ -- R01-MH083840/MH/NIMH NIH HHS/ -- U54 GM075026/GM/NIGMS NIH HHS/ -- U54-GM075026/GM/NIGMS NIH HHS/ -- England -- Nature. 2012 Nov 22;491(7425):622-6. doi: 10.1038/nature11542. Epub 2012 Oct 21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Helen L. and Martin S. Kimmel Center for Biology and Medicine at the Skirball Institute of Biomolecular Medicine, New York University School of Medicine, 540 First Avenue, New York, New York 10016, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23086149" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Binding Sites ; Citric Acid/chemistry/metabolism ; Crystallography, X-Ray ; Dicarboxylic Acid Transporters/*chemistry/*metabolism ; Ion Transport ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Sodium/chemistry/metabolism ; Structural Homology, Protein ; Structure-Activity Relationship ; Vibrio cholerae/*chemistry
    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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  • 6
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    Structural biology. Symmetric transporters for asymmetric transport (2008)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2008-08-09
    Description: 〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2630483/" 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/PMC2630483/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Karpowich, Nathan K -- Wang, Da-Neng -- DK053973/DK/NIDDK NIH HHS/ -- GM075026/GM/NIGMS NIH HHS/ -- GM075936/GM/NIGMS NIH HHS/ -- MH083840/MH/NIMH NIH HHS/ -- R01 DK053973/DK/NIDDK NIH HHS/ -- R01 DK053973-09/DK/NIDDK NIH HHS/ -- R01 MH083840/MH/NIMH NIH HHS/ -- R01 MH083840-01/MH/NIMH NIH HHS/ -- R21 GM075936/GM/NIGMS NIH HHS/ -- R21 GM075936-02S1/GM/NIGMS NIH HHS/ -- U54 GM075026/GM/NIGMS NIH HHS/ -- U54 GM075026-040010/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2008 Aug 8;321(5890):781-2. doi: 10.1126/science.1161495.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Kimmel Center for Biology and Medicine, Skirball Institute of Biomolecular Medicine and Department of Cell Biology, New York University School of Medicine, 540 First Avenue, New York, NY 10016, USA. karpowic@saturn.med.nyu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18687947" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/*chemistry/metabolism ; Binding Sites ; Cell Membrane/*metabolism ; Galactose/*metabolism ; Glucose/metabolism ; Humans ; Hydrophobic and Hydrophilic Interactions ; Intestinal Absorption ; Intestinal Mucosa/metabolism ; Kidney/metabolism ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Sodium/metabolism ; Sodium-Glucose Transport Proteins/*chemistry/metabolism ; Sodium-Glucose Transporter 1/metabolism ; Sodium-Glucose Transporter 2/*metabolism ; Vibrio parahaemolyticus/*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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  • 7
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    Science communication: Quality at stake (2013)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2013-12-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Loew, Leslie M -- Wang, Da-Neng -- New York, N.Y. -- Science. 2013 Dec 6;342(6163):1169. doi: 10.1126/science.342.6163.1169-a.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Cell Analysis and Modeling, University of Connecticut Health Center, Farmington, CT 06030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24311662" target="_blank"〉PubMed〈/a〉
    Keywords: *Access to Information ; *Fraud ; *Peer Review ; *Scientific Misconduct
    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
    Electronic Resource
    Electronic Resource
    Optical instrumentation for eye length measurement using a short coherence length laser-based interferometer approach (1993)
    [S.l.] : American Institute of Physics (AIP)
    Review of Scientific Instruments 64 (1993), S. 3082-3087 
    Details
    ISSN: 1089-7623
    Source: AIP Digital Archive
    Topics: Physics , Electrical Engineering, Measurement and Control Technology
    Notes: An optical interferometric approach is described for the measurement of axial eye length. The technique uses the short coherence length characteristics of the light source to locate, interferometrically, the position of the front surface of the eye and the retina. Results are presented from studies on an idealized model eye and the precision of the measurement is discussed. The advantages of the technique and a comparison with previously used short coherence measurements are also reviewed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.1144363
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  • 9
    Electronic Resource
    Electronic Resource
    A low coherence "white light'' interferometric sensor for eye length measurement (1995)
    [S.l.] : American Institute of Physics (AIP)
    Review of Scientific Instruments 66 (1995), S. 5464-5468 
    Details
    ISSN: 1089-7623
    Source: AIP Digital Archive
    Topics: Physics , Electrical Engineering, Measurement and Control Technology
    Notes: This article discusses the use of low coherence interferometric techniques, employing the so-called "white light interferometer,'' for axial eye length measurement. This system utilizes two Michelson interferometers, each of which locates one of the surfaces of the eye, the cornea and the retina, respectively, and thus a simultaneous determination of the two surface positions of the eye gives the value of eye length. The experimental results carried out on a simulated eye are presented, showing that the proposed system is simple, easy to align, suitable for measuring different kinds of eyes, tolerant to transverse eye movement, and worth further exploration. © 1995 American Institute of Physics.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.1146070
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  • 10
    Electronic Resource
    Electronic Resource
    Multiple optical paths in a self-seeding scheme for multiwavelength short pulse generation (1997)
    Woodbury, NY : American Institute of Physics (AIP)
    Applied Physics Letters 71 (1997), S. 1305-1307 
    Details
    ISSN: 1077-3118
    Source: AIP Digital Archive
    Topics: Physics
    Notes: A simultaneous generation of multiwavelength short pulses is demonstrated by self-injection seeding of a laser diode. The wavelengths are selected by the use of multiple optical paths in an external cavity consisting of a grating, a beam splitter, and two mirrors. By adjusting the grating and either one of the mirrors, the wavelengths and their spacings can be readily tuned in a flexible manner. The system is simple, robust, and is of low cost. © 1997 American Institute of Physics.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.119879
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