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1Printed BooksStaff View Availability
Person(s): Schwab, Joseph J.Type of Medium: UnknownPages: 394 S.ISBN: 0226741869Language: English -
2Printed BooksStaff View Availability
Person(s): Schwab, Joseph J.Type of Medium: BookPages: 152 S.Language: German -
3Latest Papers from Table of Contents or Articles in PressDavid R. Spigel, John D. Hainsworth, Mathew J. Joseph, Dianna L. Shipley, M. Kelly Hagan, Dana S. Thompson, Howard A. Burris, F. Anthony Greco
Wiley-Blackwell
Published 2018Staff ViewPublication Date: 2018-02-17Publisher: Wiley-BlackwellPrint ISSN: 0008-543XElectronic ISSN: 1097-0142Topics: BiologyMedicinePublished by: -
4Latest Papers from Table of Contents or Articles in PressStaff View
Publication Date: 2018-08-30Publisher: Institute of Physics (IOP)Print ISSN: 1757-8981Electronic ISSN: 1757-899XTopics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision MechanicsPublished by: -
5Latest Papers from Table of Contents or Articles in PressSaugata Majumder; Shreya Das; Vikas Somani; Shivakiran S. Makam; Kingston J. Joseph; Rakesh Bhatnagar
Nature Publishing Group (NPG)
Published 2018Staff ViewPublication Date: 2018-05-09Publisher: Nature Publishing Group (NPG)Electronic ISSN: 2045-2322Topics: Natural Sciences in GeneralPublished by: -
6Latest Papers from Table of Contents or Articles in PressStaff View
Publication Date: 2018-05-18Publisher: Institute of Physics Publishing (IOP)Electronic ISSN: 1748-0221Topics: PhysicsPublished by: -
7Latest Papers from Table of Contents or Articles in PressC. R. Webster ; P. R. Mahaffy ; G. J. Flesch ; P. B. Niles ; J. H. Jones ; L. A. Leshin ; S. K. Atreya ; J. C. Stern ; L. E. Christensen ; T. Owen ; H. Franz ; R. O. Pepin ; A. Steele ; C. Achilles ; C. Agard ; J. A. Alves Verdasca ; R. Anderson ; D. Archer ; C. Armiens-Aparicio ; R. Arvidson ; E. Atlaskin ; A. Aubrey ; B. Baker ; M. Baker ; T. Balic-Zunic ; D. Baratoux ; J. Baroukh ; B. Barraclough ; K. Bean ; L. Beegle ; A. Behar ; J. Bell ; S. Bender ; M. Benna ; J. Bentz ; G. Berger ; J. Berger ; D. Berman ; D. Bish ; D. F. Blake ; J. J. Blanco Avalos ; D. Blaney ; J. Blank ; H. Blau ; L. Bleacher ; E. Boehm ; O. Botta ; S. Bottcher ; T. Boucher ; H. Bower ; N. Boyd ; B. Boynton ; E. Breves ; J. Bridges ; N. Bridges ; W. Brinckerhoff ; D. Brinza ; T. Bristow ; C. Brunet ; A. Brunner ; W. Brunner ; A. Buch ; M. Bullock ; S. Burmeister ; M. Cabane ; F. Calef ; J. Cameron ; J. Campbell ; B. Cantor ; M. Caplinger ; J. Caride Rodriguez ; M. Carmosino ; I. Carrasco Blazquez ; A. Charpentier ; S. Chipera ; D. Choi ; B. Clark ; S. Clegg ; T. Cleghorn ; E. Cloutis ; G. Cody ; P. Coll ; P. Conrad ; D. Coscia ; A. Cousin ; D. Cremers ; J. Crisp ; A. Cros ; F. Cucinotta ; C. d'Uston ; S. Davis ; M. Day ; M. de la Torre Juarez ; L. DeFlores ; D. DeLapp ; J. DeMarines ; D. DesMarais ; W. Dietrich ; R. Dingler ; C. Donny ; B. Downs ; D. Drake ; G. Dromart ; A. Dupont ; B. Duston ; J. Dworkin ; M. D. Dyar ; L. Edgar ; K. Edgett ; C. Edwards ; L. Edwards ; B. Ehlmann ; B. Ehresmann ; J. Eigenbrode ; B. Elliott ; H. Elliott ; R. Ewing ; C. Fabre ; A. Fairen ; K. Farley ; J. Farmer ; C. Fassett ; L. Favot ; D. Fay ; F. Fedosov ; J. Feldman ; S. Feldman ; M. Fisk ; M. Fitzgibbon ; M. Floyd ; L. Fluckiger ; O. Forni ; A. Fraeman ; R. Francis ; P. Francois ; C. Freissinet ; K. L. French ; J. Frydenvang ; A. Gaboriaud ; M. Gailhanou ; J. Garvin ; O. Gasnault ; C. Geffroy ; R. Gellert ; M. Genzer ; D. Glavin ; A. Godber ; F. Goesmann ; W. Goetz ; D. Golovin ; F. Gomez Gomez ; J. Gomez-Elvira ; B. Gondet ; S. Gordon ; S. Gorevan ; J. Grant ; J. Griffes ; D. Grinspoon ; J. Grotzinger ; P. Guillemot ; J. Guo ; S. Gupta ; S. Guzewich ; R. Haberle ; D. Halleaux ; B. Hallet ; V. Hamilton ; C. Hardgrove ; D. Harker ; D. Harpold ; A. M. Harri ; K. Harshman ; D. Hassler ; H. Haukka ; A. Hayes ; K. Herkenhoff ; P. Herrera ; S. Hettrich ; E. Heydari ; V. Hipkin ; T. Hoehler ; J. Hollingsworth ; J. Hudgins ; W. Huntress ; J. Hurowitz ; S. Hviid ; K. Iagnemma ; S. Indyk ; G. Israel ; R. Jackson ; S. Jacob ; B. Jakosky ; E. Jensen ; J. K. Jensen ; J. Johnson ; M. Johnson ; S. Johnstone ; A. Jones ; J. Joseph ; I. Jun ; L. Kah ; H. Kahanpaa ; M. Kahre ; N. Karpushkina ; W. Kasprzak ; J. Kauhanen ; L. Keely ; O. Kemppinen ; D. Keymeulen ; M. H. Kim ; K. Kinch ; P. King ; L. Kirkland ; G. Kocurek ; A. Koefoed ; J. Kohler ; O. Kortmann ; A. Kozyrev ; J. Krezoski ; D. Krysak ; R. Kuzmin ; J. L. Lacour ; V. Lafaille ; Y. Langevin ; N. Lanza ; J. Lasue ; S. Le Mouelic ; E. M. Lee ; Q. M. Lee ; D. Lees ; M. Lefavor ; M. Lemmon ; A. Lepinette Malvitte ; R. Leveille ; E. Lewin-Carpintier ; K. Lewis ; S. Li ; L. Lipkaman ; C. Little ; M. Litvak ; E. Lorigny ; G. Lugmair ; A. Lundberg ; E. Lyness ; M. Madsen ; J. Maki ; A. Malakhov ; C. Malespin ; M. Malin ; N. Mangold ; G. Manhes ; H. Manning ; G. Marchand ; M. Marin Jimenez ; C. Martin Garcia ; D. Martin ; M. Martin ; J. Martinez-Frias ; J. Martin-Soler ; F. J. Martin-Torres ; P. Mauchien ; S. Maurice ; A. McAdam ; E. McCartney ; T. McConnochie ; E. McCullough ; I. McEwan ; C. McKay ; S. McLennan ; S. McNair ; N. Melikechi ; P. Y. Meslin ; M. Meyer ; A. Mezzacappa ; H. Miller ; K. Miller ; R. Milliken ; D. Ming ; M. Minitti ; M. Mischna ; I. Mitrofanov ; J. Moersch ; M. Mokrousov ; A. Molina Jurado ; J. Moores ; L. Mora-Sotomayor ; J. M. Morookian ; R. Morris ; S. Morrison ; R. Mueller-Mellin ; J. P. Muller ; G. Munoz Caro ; M. Nachon ; S. Navarro Lopez ; R. Navarro-Gonzalez ; K. Nealson ; A. Nefian ; T. Nelson ; M. Newcombe ; C. Newman ; H. Newsom ; S. Nikiforov ; B. Nixon ; E. Noe Dobrea ; T. Nolan ; D. Oehler ; A. Ollila ; T. Olson ; M. A. de Pablo Hernandez ; A. Paillet ; E. Pallier ; M. Palucis ; T. Parker ; Y. Parot ; K. Patel ; M. Paton ; G. Paulsen ; A. Pavlov ; B. Pavri ; V. Peinado-Gonzalez ; L. Peret ; R. Perez ; G. Perrett ; J. Peterson ; C. Pilorget ; P. Pinet ; J. Pla-Garcia ; I. Plante ; F. Poitrasson ; J. Polkko ; R. Popa ; L. Posiolova ; A. Posner ; I. Pradler ; B. Prats ; V. Prokhorov ; S. W. Purdy ; E. Raaen ; L. Radziemski ; S. Rafkin ; M. Ramos ; E. Rampe ; F. Raulin ; M. Ravine ; G. Reitz ; N. Renno ; M. Rice ; M. Richardson ; F. Robert ; K. Robertson ; J. A. Rodriguez Manfredi ; J. J. Romeral-Planello ; S. Rowland ; D. Rubin ; M. Saccoccio ; A. Salamon ; J. Sandoval ; A. Sanin ; S. A. Sans Fuentes ; L. Saper ; P. Sarrazin ; V. Sautter ; H. Savijarvi ; J. Schieber ; M. Schmidt ; W. Schmidt ; D. Scholes ; M. Schoppers ; S. Schroder ; S. Schwenzer ; E. Sebastian Martinez ; A. Sengstacken ; R. Shterts ; K. Siebach ; T. Siili ; J. Simmonds ; J. B. Sirven ; S. Slavney ; R. Sletten ; M. Smith ; P. Sobron Sanchez ; N. Spanovich ; J. Spray ; S. Squyres ; K. Stack ; F. Stalport ; T. Stein ; N. Stewart ; S. L. Stipp ; K. Stoiber ; E. Stolper ; B. Sucharski ; R. Sullivan ; R. Summons ; D. Sumner ; V. Sun ; K. Supulver ; B. Sutter ; C. Szopa ; F. Tan ; C. Tate ; S. Teinturier ; I. ten Kate ; P. Thomas ; L. Thompson ; R. Tokar ; M. Toplis ; J. Torres Redondo ; M. Trainer ; A. Treiman ; V. Tretyakov ; R. Urqui-O'Callaghan ; J. Van Beek ; T. Van Beek ; S. VanBommel ; D. Vaniman ; A. Varenikov ; A. Vasavada ; P. Vasconcelos ; E. Vicenzi ; A. Vostrukhin ; M. Voytek ; M. Wadhwa ; J. Ward ; E. Weigle ; D. Wellington ; F. Westall ; R. C. Wiens ; M. B. Wilhelm ; A. Williams ; J. Williams ; R. Williams ; R. B. Williams ; M. Wilson ; R. Wimmer-Schweingruber ; M. Wolff ; M. Wong ; J. Wray ; M. Wu ; C. Yana ; A. Yen ; A. Yingst ; C. Zeitlin ; R. Zimdar ; M. P. Zorzano Mier
American Association for the Advancement of Science (AAAS)
Published 2013Staff ViewPublication Date: 2013-07-23Publisher: American Association for the Advancement of Science (AAAS)Print ISSN: 0036-8075Electronic ISSN: 1095-9203Topics: BiologyChemistry and PharmacologyComputer ScienceMedicineNatural Sciences in GeneralPhysicsPublished by: -
8Latest Papers from Table of Contents or Articles in PressElizabeth K. Duperret, Aspen Trautz, Regina Stoltz, Ami Patel, Megan C. Wise, Alfredo Perales-Puchalt, Trevor Smith, Kate E. Broderick, Emma Masteller, J. Joseph Kim, Laurent Humeau, Kar Muthumani, David B. Weiner
The American Association for Cancer Research (AACR)
Published 2018Staff ViewPublication Date: 2018-11-16Publisher: The American Association for Cancer Research (AACR)Print ISSN: 0008-5472Electronic ISSN: 1538-7445Topics: MedicinePublished by: -
9Latest Papers from Table of Contents or Articles in PressC. Cao ; E. Elliott ; J. Joseph ; H. Wu ; J. Petricka ; T. Schafer ; J. E. Thomas
American Association for the Advancement of Science (AAAS)
Published 2010Staff ViewPublication Date: 2010-12-15Publisher: American Association for the Advancement of Science (AAAS)Print ISSN: 0036-8075Electronic ISSN: 1095-9203Topics: BiologyChemistry and PharmacologyComputer ScienceMedicineNatural Sciences in GeneralPhysicsPublished by: -
10Articles: DFG German National LicensesStaff View
ISSN: 1550-7408Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: BiologyNotes: Leishmania major promastigotes were washed and resuspended in an iso-osmotic buffer. The rate of oxidation of 14C-labeled substrates was then measured as a function of osmolality. An acute decrease in osmolality (achieved by adding H2O to the cell suspension) caused an increase in the rates of 14CO2 production from [6-14C]glucose and, to a lesser extent, from [1, (3)-14C]glycerol. An acute increase in osmolality (achieved by adding NaCl, KCl, or mannitol) strongly inhibited the rates of 14CO2 production from [1-: 14C]alanine, [1-14C]glutamate, and [1, (3)-14C]glycerol. The rates of 14CO2 formation from [1-14C]laurate, [1-14C]acetate, and [2-14C]glucose (all of which form [1-14C]acetyl CoA prior to oxidation) were also inhibited, but less strongly, by increasing osmolality. These data suggest that with increasing osmolality there is an inhibition of mitochondrial oxidative capacity, which could facilitate the increase in alanine pool size that occurs in response to hyper-osmotic stress. Similarly, an increase in oxidative capacity would help prevent a rebuild up of the alanine pool after its rapid loss to the medium in response to hypo-osmotic stress.Type of Medium: Electronic ResourceURL: -
11Articles: DFG German National LicensesStaff View
ISSN: 1550-7408Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: BiologyNotes: . An enzyme that oxidizes ethanol to acetaldehyde in the presence of NADP (but not NAD) and reduces acetaldehyde to ethanol in the presence of NADPH (but not NADH) is present in Leishmania donovani promastigotes. The activity is present only in the supernatant fraction obtained from sonication of the cells and high speed centrifugation. The Km and Vm values were evaluated for propanol and propionaldehyde as well as for ethanol and acetaldehyde in cells obtained from late log and 3-day stationary phase cultures. There was no significant change in Km or Vm values for any of these four substrates with culture age. Since the Km values for ethanol and propanol are much higher than for the corresponding aldehydes and higher than any physiological range of alcohol concentration likely to be encountered, this enzyme is considered to function as an aldehyde reductase.Type of Medium: Electronic ResourceURL: -
12Articles: DFG German National LicensesStaff View
ISSN: 1550-7408Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: BiologyNotes: . Leishmania donovani promastigotes were collected, washed, resuspended in buffer, and assayed for sucrase activity. No activity was observed in the intact washed cells, but activity was measurable when the cells were permeabilized with Triton X-100. Intracellular sucrase activity was highest in promastigotes grown at pH 7.4, somewhat lower in promastigotes grown at pH 5.5, and significantly lower in “amastigotes” grown at pH 5.5. No trehalase, lactase, or maltase activities were observed. Assay of the medium in which the cells had grown showed that most the sucrase activity was extracellular, i.e. was secreted into the medium during growth.Type of Medium: Electronic ResourceURL: -
13Articles: DFG German National LicensesStaff View
ISSN: 1550-7408Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: BiologyNotes: Leishmania donovani promastigotes were grown to late log phase, washed and resuspended in iso-osmotic buffer containing L-arginine, and the rate of urea formation was then measured under various conditions. Addition of glucose or mannose activated urea formation, whereas 2-deoxyglucose inhibited and 6-deoxyglucose had no effect. Addition of alanine or of α-aminoisobutyrate inhibited urea formation, alanine causing a greater inhibition than α-aminoisobutyrate. Addition of leucine, proline, glycine, or lysine had no effect on urea formation. The presence of glutamate also increased the rate of urea formation from arginine, but to a lesser extent than did glucose. The presence of both glucose and alanine caused no net change in urea formation, whereas the inhibitory effect of alanine exceeded the activating effect of glutamate, so that a small inhibition in the rate of urea formation occurred in the presence of both alanine and glutamate. Cells grown to 3-day stationary phase had a markedly reduced rate of arginine catabolism to urea, but the activating effect of glucose and the inhibitory effect of alanine were qualitatively similar to their effects on late log phase cells. Addition of water to cells suspended in buffer also inhibited urea formation, but this appeared to be due primarily to the release of alanine caused by the hypo-osmotic stress. Addition of mannitol to cells suspended in buffer caused a small inhibition of arginine catabolism. Addition of dibutyrylcyclic AMP, 3′,5′-cyclic GMP, phorbol myristic acid, or A23187 had no effect on the rate of urea formation from arginine. It is suggested that the effects of glucose and 2-deoxyglucose on arginine catabolism depend largely upon the nature of their metabolites, whereas the effects of the various amino acids examined depend largely on the extent to which they interfere with or enhance arginine transport into the cells.Type of Medium: Electronic ResourceURL: -
14Articles: DFG German National LicensesStaff View
ISSN: 1550-7408Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: BiologyNotes: Earlier studies showed that Leishmania major promastigotes are sensitive to osmotic conditions. A reduction in osmolality caused the cells to shorten and to rapidly release most of their large internal pool of alanine. In this study some effects of hyper-osmotic stress were examined. an increase in osmolality of the culture medium from 308 to 625 mOsm/kg caused only a small decrease in growth rate. When cells grown in the usual culture medium (308 mOsm/kg) were washed, resuspended in iso-osmotic buffer, and subjected to acute hyper-osmotic stress by addition of mannitol, the alanine content increased even in the absence of exogenous substrate. Promastigotes, depleted of alanine by a 5-min exposure to hypo-osmotic conditions, also synthesized alanine when resuspended in iso-osmotic buffer. Washed cells resuspended in iso-osmotic buffer consume their internal pool of alanine under aerobic conditions, Rates of consumption decreased on addition of mannitol, becoming zero at about 440 mOsm/kg. At higher osmolalities, alanine synthesis occurred. to estimate whether proteolysis could account for alanine synthesis in the absence of exogenous substrate, cells that had been grown with [1-14C]leucine were washed and resuspended under hypo-, iso-, and hyper-osmotic conditions and the amounts of 14CO2 and 14C-labelled peptides released in 1 h were measured. Little proteolysis occurred under these conditions, but the possibility that proteolysis was the source of the alanine increase, observed in response to hyper-osmotic stress, cannot be ruled out.Type of Medium: Electronic ResourceURL: -
15Articles: DFG German National LicensesDARLING, THOMAS N. ; BURROWS, CHRISTINE M. ; BLUM, J. JOSEPH
Oxford, UK : Blackwell Publishing Ltd
Published 1990Staff ViewISSN: 1550-7408Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: BiologyNotes: . Leishmania major promastigotes were grown to late-log phase and washed and resuspended in an isosmotic buffer. When osmolality was suddenly decreased by 50%, the cells rapidly became shorter and increased in width. Cell volume, calculated assuming a prolate-ellipsoidal shape, increased 1.4 times after 1 min. Over the next several minutes, the average length and width returned to control values while the volume returned to baseline, indicating the ability to regulate volume. Concomitantly with the swelling, large amounts of alanine and other ninhydrin-positive substances were released. All of the alanine pool was released within 1 min after reduction of the osmolality by 66%. Cells pre-loaded with [14C]-aminoisobutyric acid also released it very rapidly upon hypo-osmotic stress. Release of ninhydrin-positive substances resulted from decreased osmolality rather than changes in ionic composition. The same results were obtained if osmolality was decreased by reducing only the NaCl content of the buffer instead of diluting it with water, and mannitol could substitute for the NaCl. Promastigotes were able to grow well over several days in media as low as 154 mOsm/kg. The nature of the signalling mechanism(s) that initiates the rapid shape change and efflux of ninhydrin-positive substances in response to hypo-osmotic stress is at present unknown.Type of Medium: Electronic ResourceURL: -
16Articles: DFG German National LicensesStaff View
ISSN: 1550-7408Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: BiologyType of Medium: Electronic ResourceURL: -
17Articles: DFG German National LicensesStaff View
ISSN: 1550-7408Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: BiologyNotes: Leishmania donovani promastigotes in late-stationary phase incorporated label from [2-14C]acetate and [1-14C]laurate into the mannose residues of mannan, thus confirming the presence of a functional glyoxylate bypass in these parasitic protozoa. Isolated, washed calls also incorporated label from [2-14C]acetate and [1-14C]laurate into mannan during a 1-hr incubation in buffer. Glucose had no effect on label incorporation into mannan, but glutamate caused over a four-fold increase in incorporation from [2-14C]acetate and a 2.4-fold increase from [1-14C]laurate. Staurosporine, a protein kinase inhibitor that inhibits glutamate and alanine oxidation, did not inhibit label incorporation from [2-14C]acetate into mannan. Hyperosmolality caused about a 33% inhibition of label incorporation into mannan. These results show the glyoxylate cycle and/or the subsequent biosynthetic pathway from fructose-6-phosphate to mannan are subject to regulation.Type of Medium: Electronic ResourceURL: -
18Articles: DFG German National LicensesStaff View
ISSN: 1550-7408Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: BiologyType of Medium: Electronic ResourceURL: -
19Articles: DFG German National LicensesStaff View
ISSN: 1550-7408Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: BiologyNotes: SYNOPSIS. The feasibility of using a macrophage-like murine tumor cell as a host for Leishmania donovani was investigated. This cell line, designated P388D1, rapidly phagocytized amastigotes and supported their intracellular replication. It can serve as a model “host” without the inherent limitations of primary macrophage cultures.Type of Medium: Electronic ResourceURL: -
20Articles: DFG German National LicensesStaff View
ISSN: 1550-7408Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: BiologyNotes: Leishmania donovani promastigotes were collected from cultures in log and stationary phases of growth and resuspended in Hank's Balanced Salt Solution containing 1 mM sodium acetate. Changes in the forward and side scattering of the cells were measured by flow cytometry in response to acute changes in osmolality and to the addition of several different substrates. Forward and side scattering of cells from log phase cultures decreased when the osmolality was decreased by the addition of H2O and increased when the osmolality was increased by the addition of NaCl. Cells from stationary phase cultures had about the same forward scatter as cells from log phase cultures, but almost a four-fold lower side scatter, and their side scatter values did not change significantly in response to a reduction in osmolality. Microscopic observation showed that both log and stationary cells got longer and thinner, on average, in response to hyperosmolality. The light scattering properties of log (but not of stationary) cells changed in a reproducible manner when substrates were added to the buffer. The ratio of forward to side scatter increased in the following order: controls in balanced salt solution 〉aspartate 〉glutamate, glucose or 2-deoxyglucose 〉alanine 〉proline. Thus the light scattering properties of L. donovani promastigotes change with culture age, in response to changes in osmolality, and, in log phase cells, in response to the presence of several substrates.Type of Medium: Electronic ResourceURL: