Search Results - (Author, Cooperation:H. Zhan)
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1Latest Papers from Table of Contents or Articles in PressGuo, A., Wang, Y., Chen, B., Wang, Y., Yuan, J., Zhang, L., Hall, D., Wu, J., Shi, Y., Zhu, Q., Chen, C., Thiel, W. H., Zhan, X., Weiss, R. M., Zhan, F., Musselman, C. A., Pufall, M., Zhu, W., Au, K. F., Hong, J., Anderson, M. E., Grueter, C. E., Song, L.-S.
American Association for the Advancement of Science (AAAS)
Published 2018Staff ViewPublication Date: 2018-12-21Publisher: American Association for the Advancement of Science (AAAS)Print ISSN: 0036-8075Electronic ISSN: 1095-9203Topics: BiologyChemistry and PharmacologyGeosciencesComputer ScienceMedicineNatural Sciences in GeneralPhysicsKeywords: Cell Biology, Molecular Biology, Online OnlyPublished by: -
2Latest Papers from Table of Contents or Articles in PressB. Pinan-Lucarre ; H. Tu ; M. Pierron ; P. I. Cruceyra ; H. Zhan ; C. Stigloher ; J. E. Richmond ; J. L. Bessereau
Nature Publishing Group (NPG)
Published 2014Staff ViewPublication Date: 2014-06-05Publisher: Nature Publishing Group (NPG)Print ISSN: 0028-0836Electronic ISSN: 1476-4687Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsKeywords: ADAM Proteins/metabolism ; Acetylcholine/metabolism ; Animals ; Caenorhabditis elegans/*metabolism ; Caenorhabditis elegans Proteins/chemistry/*metabolism ; Cholinergic Neurons/*metabolism ; Extracellular Matrix Proteins/metabolism ; GABAergic Neurons/*metabolism ; Motor Neurons/metabolism ; Nerve Tissue Proteins/chemistry/deficiency/*metabolism ; Neuromuscular Junction ; Post-Synaptic Density/*metabolism ; Protein Isoforms/chemistry/deficiency/metabolism ; Receptors, Cholinergic/metabolism ; Receptors, GABA-A/metabolismPublished by: -
3Latest Papers from Table of Contents or Articles in PressI. Mayrose ; S. H. Zhan ; C. J. Rothfels ; K. Magnuson-Ford ; M. S. Barker ; L. H. Rieseberg ; S. P. Otto
American Association for the Advancement of Science (AAAS)
Published 2011Staff ViewPublication Date: 2011-08-20Publisher: American Association for the Advancement of Science (AAAS)Print ISSN: 0036-8075Electronic ISSN: 1095-9203Topics: BiologyChemistry and PharmacologyComputer ScienceMedicineNatural Sciences in GeneralPhysicsKeywords: Angiosperms/*genetics ; *Biological Evolution ; Diploidy ; *Extinction, Biological ; Ferns/*genetics ; *Genetic Speciation ; Genome, Plant ; *PolyploidyPublished by: -
4Articles: DFG German National LicensesZhan, H. H. ; Kang, J. Y. ; Wu, Z. Y. ; Huang, Q. S.
[S.l.] : American Institute of Physics (AIP)
Published 1998Staff ViewISSN: 1089-7550Source: AIP Digital ArchiveTopics: PhysicsNotes: High resolution Laplace defect spectroscopy was used to study the fine structure of the electron emission process of DX(Sn) centers in AlxGa1−xAs (x=0.26,0.53). Two groups of peaks in the spectra of electron emission rates were found to correspond to two DX-like centers observed by deep level transient spectroscopy. The line splitting in both groups derives from the alloy disorder effect attributed to the different local configurations of Al and Ga atoms around two DX-like centers. Experimental evidence for the microscopic nature of two DX-like centers in Sn-doped AlGaAs is provided. © 1998 American Institute of Physics.Type of Medium: Electronic ResourceURL: -
5Articles: DFG German National LicensesStaff View
ISSN: 0020-1693Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002Topics: Chemistry and PharmacologyType of Medium: Electronic ResourceURL: -
6Articles: DFG German National LicensesStaff View
ISSN: 0008-6215Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002Topics: Chemistry and PharmacologyType of Medium: Electronic ResourceURL: -
7Articles: DFG German National LicensesStaff View
ISSN: 0047-6374Keywords: Aging ; Free radical ; Liver ; Rat ; Sex glandSource: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002Topics: MedicineType of Medium: Electronic ResourceURL: -
8Articles: DFG German National LicensesSilverman, J. A. ; Mindell, J. A. ; Zhan, H. ; Finkelstein, A. ; Collier, R. J.
Springer
Published 1994Staff ViewISSN: 1432-1424Keywords: Diphtheria toxin ; Site-directed mutagenesis ; Planar lipid bilayers ; Ion channels ; T-domain ; Channel-forming peptidesSource: Springer Online Journal Archives 1860-2000Topics: BiologyChemistry and PharmacologyNotes: Abstract Diphtheria Toxin (DT) is a 535 amino acid exotoxin, whose active form consists of two polypeptide chains linked by an interchain disulphide bond. DT's N-terminal A fragment kills cells by enzymatically inactivating their protein synthetic machinery; its C terminal B chain is required for the binding of toxin to sensitive cells and for the translocation of the A fragment into the cytosol. This B fragment, consisting of its N-terminal T domain (amino acids 191–386) and its C-terminal R domain (amino acids 387–535) is responsible for the ion-conducting channels formed by DT in lipid bilayers and cellular plasma membranes. To further delineate the channel-forming region of DT, we studied channels formed by deletion mutants of DT in lipid bilayer membranes under several pH conditions. Channels formed by mutants containing only the T domain (i.e., lacking the A fragment and/or the R domain), as well as those formed by mutants replacing the R domain with Interleukin-2 (Il–2), have single channel conductances and selectivities essentially identical to those of channels formed by wild-type DT. Furthermore, deleting the N-terminal 118 amino acids of the T domain also has minimal effect on the single channel conductance and selectivity of the mutant channels. Together, these data identify a 61 amino acid stretch of the T domain, corresponding to the region which includes α-helices TH8 and TH9 in the crystal structure of DT, as the channel-forming region of the toxin.Type of Medium: Electronic ResourceURL: -
9Articles: DFG German National LicensesZhan, H. ; Elliott, J.L. ; Shen, W.H. ; Huynh, P.D. ; Finkelstein, A. ; Collier, R.J.
Springer
Published 1999Staff ViewISSN: 1432-1424Keywords: Key words: Diphtheria toxin — Proline — Mutagenesis — Membrane insertion — Transmembrane domain — Site-specific labelingSource: Springer Online Journal Archives 1860-2000Topics: BiologyChemistry and PharmacologyNotes: Abstract. Translocation of the catalytic domain of diphtheria toxin (DT) across the endosomal membrane to the cytoplasm of mammalian cells requires the low-pH-dependent insertion of a hydrophobic helical hairpin (TH8-TH9) that is buried within the T domain of the native protein. Mutations of Pro345, which terminates helix TH8, have been reported to block toxicity for Vero cells. We found that mutant toxins in which Pro345 had been replaced by Cys, Glu, or Gly were profoundly defective at low pH in forming channels in planar phospholipid bilayers and in permeabilizing phospholipid vesicles to entrapped fluorophores. Experiments with isolated T domain containing a polarity-sensitive fluorophore attached to Cys at position 332 suggest that the P345E mutation blocks membrane insertion. None of the Pro345 mutations shifted the pH-dependence of binding in solution of the hydrophobic fluorophore, 2-p-toluidinyl-naphthalene 7-sulfonate. The results indicate that proline at position 345 is required for the T domain to insert into phospholipid bilayers or to adopt a functional conformation within the bilayer.Type of Medium: Electronic ResourceURL: