Search Results - (Author, Cooperation:S. Mok)
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1S. Mok ; E. A. Ashley ; P. E. Ferreira ; L. Zhu ; Z. Lin ; T. Yeo ; K. Chotivanich ; M. Imwong ; S. Pukrittayakamee ; M. Dhorda ; C. Nguon ; P. Lim ; C. Amaratunga ; S. Suon ; T. T. Hien ; Y. Htut ; M. A. Faiz ; M. A. Onyamboko ; M. Mayxay ; P. N. Newton ; R. Tripura ; C. J. Woodrow ; O. Miotto ; D. P. Kwiatkowski ; F. Nosten ; N. P. Day ; P. R. Preiser ; N. J. White ; A. M. Dondorp ; R. M. Fairhurst ; Z. Bozdech
American Association for the Advancement of Science (AAAS)
Published 2014Staff ViewPublication Date: 2014-12-17Publisher: American Association for the Advancement of Science (AAAS)Print ISSN: 0036-8075Electronic ISSN: 1095-9203Topics: BiologyChemistry and PharmacologyComputer ScienceMedicineNatural Sciences in GeneralPhysicsKeywords: Animals ; Antimalarials/*pharmacology ; Artemisinins/*pharmacology ; Chaperonin Containing TCP-1/genetics/metabolism ; Drug Resistance/*genetics ; Humans ; Malaria/*drug therapy/parasitology ; Malaria, Falciparum/*drug therapy/parasitology ; Plasmodium falciparum/*drug effects/*genetics ; Transcriptome ; Unfolded Protein Response/*geneticsPublished by: -
2Fodero, L. R. ; Mok, S. S. ; Losic, D. ; Martin, L. L. ; Aguilar, M. I. ; Barrow, C. J. ; Livett, B. G. ; Small, D. H.
Oxford, UK : Blackwell Science Ltd
Published 2004Staff ViewISSN: 1471-4159Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: MedicineNotes: The β-amyloid protein (Aβ) is the major protein component of amyloid plaques found in the Alzheimer brain. Although there is a loss of acetylcholinesterase (AChE) from both cholinergic and non-cholinergic neurones in the brain of Alzheimer patients, the level of AChE is increased around amyloid plaques. Previous studies using P19 cells in culture and transgenic mice which overexpress human Aβ have suggested that this increase may be due to a direct action of Aβ on AChE expression in cells adjacent to amyloid plaques. The aim of the present study was to examine the mechanism by which Aβ increases levels of AChE in primary cortical neurones. Aβ1−42 was more potent than Aβ1−40 in its ability to increase AChE in primary cortical neurones. The increase in AChE was unrelated to the toxic effects of the Aβ peptides. The effect of Aβ1−42 on AChE was blocked by inhibitors of α7 nicotinic acetylcholine receptors (α7 nAChRs) as well as by inhibitors of L- or N-type voltage-dependent calcium channels (VDCCs), whereas agonists of α7 nAChRs (choline, nicotine) increased the level of AChE. The results demonstrate that the effect of Aβ1−42 on AChE is due to an agonist effect of Aβ1−42 on the α7 nAChR.Type of Medium: Electronic ResourceURL: -
3Staff View
ISSN: 0378-1119Keywords: Bidirectional promoter ; DNA-protein complexes ; deletion mutants ; minimal promoter ; mobility shift assays ; novel cis elementsSource: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002Topics: BiologyType of Medium: Electronic ResourceURL: -
4Tsui, F.W.L. ; Tsui, H.-W. ; Mok, S. ; Mlinaric, I. ; Copeland, N.G. ; Gilbert, D.J. ; Jenkins, N.A. ; Siminovitch, K.A.
Amsterdam : ElsevierStaff ViewISSN: 0888-7543Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002Topics: BiologyMedicineType of Medium: Electronic ResourceURL: -
5Staff View
ISSN: 0009-9120Keywords: HPLC ; cholelithiasis ; cholestasis ; conjugated bile acids ; gall bladder ; human bileSource: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002Topics: MedicineType of Medium: Electronic ResourceURL: -
6Staff View
ISSN: 1572-9982Source: Springer Online Journal Archives 1860-2000Topics: EconomicsType of Medium: Electronic ResourceURL: -
7Staff View
ISSN: 1572-9982Source: Springer Online Journal Archives 1860-2000Topics: EconomicsType of Medium: Electronic ResourceURL: -
8Staff View
ISSN: 1572-9982Source: Springer Online Journal Archives 1860-2000Topics: EconomicsType of Medium: Electronic ResourceURL: -
9Mok, S. ; Worsfold, D. J. ; Fouda, A. ; Matsuura, T.
New York, NY [u.a.] : Wiley-Blackwell
Published 1994Staff ViewISSN: 0021-8995Keywords: Chemistry ; Polymer and Materials ScienceSource: Wiley InterScience Backfile Collection 1832-2000Topics: Chemistry and PharmacologyMechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision MechanicsPhysicsNotes: The fouling of ultrafiltration membrane is often caused by gel formation on the membrane surface. This gel layer arises due to concentration polarization or macromolecular adsorption on the membrane surface. The gel layer affects both the hydraulic permeability and the rejection properties of the membrane. In this report, the adsorption of porcine albumin and the concentration polarization effect on modified and unmodified polyethersulfone (PES) hollow-fiber membrane is studied. PES ultrafiltration hollow-fiber membranes were modified by the grafting of polyethylene glycol (PEG) polymer on the internal surface using γ-ray irradiation method. The modified hollow fibers were less susceptible to fouling than were the unmodified fiber. The performance of both modified and unmodified hollow fibers was tested as a function of feed flow rates and protein concentrations. © 1994 John Wiley & Sons, Inc.Additional Material: 5 Ill.Type of Medium: Electronic ResourceURL: