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  1. Article: Antifungal proteins.

    Selitrennikoff, C P

    Applied and environmental microbiology

    2001  Volume 67, Issue 7, Page(s) 2883–2894

    MeSH term(s) Amino Acid Sequence ; Animals ; Antifungal Agents/chemistry ; Antifungal Agents/metabolism ; Antifungal Agents/pharmacology ; Fungi/drug effects ; Humans ; Molecular Sequence Data ; Mycoses/microbiology ; Proteins/chemistry ; Proteins/genetics ; Proteins/metabolism ; Proteins/pharmacology
    Chemical Substances Antifungal Agents ; Proteins
    Language English
    Publishing date 2001-07
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 223011-2
    ISSN 1098-5336 ; 0099-2240
    ISSN (online) 1098-5336
    ISSN 0099-2240
    DOI 10.1128/AEM.67.7.2883-2894.2001
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  2. Article: Antifungal proteins

    Selitrennikoff, C.P

    Applied and environmental microbiology. July 2001. v. 67 (7)

    2001  

    Keywords plants ; plant proteins ; defense mechanisms ; disease resistance ; antifungal properties ; plant pathogenic fungi ; pathogenesis-related proteins
    Language English
    Dates of publication 2001-07
    Size p. 2883-2894.
    Document type Article
    ZDB-ID 223011-2
    ISSN 1098-5336 ; 0099-2240
    ISSN (online) 1098-5336
    ISSN 0099-2240
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  3. Article: Screening for antifungal drugs.

    Selitrennikoff, C P

    Biotechnology (Reading, Mass.)

    1992  Volume 21, Page(s) 189–217

    MeSH term(s) Animals ; Antifungal Agents/isolation & purification ; Drug Evaluation, Preclinical ; Fungi/drug effects ; Humans ; Plants/microbiology
    Chemical Substances Antifungal Agents
    Language English
    Publishing date 1992
    Publishing country United States
    Document type Journal Article ; Research Support, U.S. Gov't, Non-P.H.S. ; Review
    ISSN 0740-7378
    ISSN 0740-7378
    DOI 10.1016/b978-0-7506-9115-4.50014-0
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  4. Article: Cryptococcus neoformans resistance to echinocandins: (1,3)beta-glucan synthase activity is sensitive to echinocandins.

    Maligie, Marybeth A / Selitrennikoff, Claude P

    Antimicrobial agents and chemotherapy

    2005  Volume 49, Issue 7, Page(s) 2851–2856

    Abstract: ... activity in vitro. We tested in vitro C. neoformans (1,3)beta-glucan synthase activity against the (1,3 ... respectively) to these echinocandins. Taken together with high MICs for C. neoformans (caspofungin MIC, 16 ... microg/ml; cilofungin MIC, 64 microg/ml), our results indicate that C. neoformans is resistant ...

    Abstract (1,3)Beta-D-glucan synthase (EC 2.4.1.34. UDP-glucose: 1,3-beta-D-glucan 3-beta-glucosyltransferase) uses UDP-glucose as substrate and catalyzes the polymerization of glucose ([1,3]-beta-linkages) to form the major carbohydrate component of the fungal cell wall. We have optimized in vitro assay conditions for (1,3)beta-glucan synthase activity from Cryptococcus neoformans. Cells lysed in 50 mM Tris, pH 7.75, containing 20% glycerol, 2 mM NaF, 1 mM dithiothreitol, 0.1 mM phenylmethylsulfonyl fluoride, 5 mM MgCl(2), 0.1% protease and phosphatase inhibitor cocktails, and 60 microM GTPgammaS produced maximum specific activity in vitro. We tested in vitro C. neoformans (1,3)beta-glucan synthase activity against the (1,3)beta-glucan synthase inhibitors, caspofungin and cilofungin, and have determined that (1,3)beta-glucan synthase activity is very sensitive (apparent K(i) of 0.17 +/- 0.02 microM and 22 +/- 5.7 microM, respectively) to these echinocandins. Taken together with high MICs for C. neoformans (caspofungin MIC, 16 microg/ml; cilofungin MIC, 64 microg/ml), our results indicate that C. neoformans is resistant to caspofungin and cilofungin by a mechanism(s) unrelated to (1,3)beta-glucan synthase resistance.
    MeSH term(s) Antifungal Agents/pharmacology ; Cryptococcus neoformans/drug effects ; Cryptococcus neoformans/enzymology ; Drug Resistance, Fungal ; Echinocandins ; Fungal Proteins/genetics ; Fungal Proteins/metabolism ; Glucosyltransferases/antagonists & inhibitors ; Glucosyltransferases/metabolism ; Humans ; Lipopeptides ; Microbial Sensitivity Tests ; Peptides, Cyclic/pharmacology
    Chemical Substances Antifungal Agents ; Echinocandins ; Fungal Proteins ; Lipopeptides ; Peptides, Cyclic ; cilofungin (8ZJC54A39X) ; Glucosyltransferases (EC 2.4.1.-) ; glucan synthase (EC 2.4.1.-) ; caspofungin (F0XDI6ZL63)
    Language English
    Publishing date 2005-07
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 217602-6
    ISSN 1098-6596 ; 0066-4804
    ISSN (online) 1098-6596
    ISSN 0066-4804
    DOI 10.1128/AAC.49.7.2851-2856.2005
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  5. Article: Construction of a Saccharomyces cerevisiae strain expressing the Leishmania major nucleoside hydrolase gene.

    Miller, Tamara K / Patel, Champa / Selitrennikoff, Claude P

    International journal of antimicrobial agents

    2007  Volume 29, Issue 1, Page(s) 103–107

    Abstract: Nucleoside hydrolase (NH) (EC 3.2.2.3) is an essential enzyme in the purine-pyrimidine salvage pathway utilised by many protozoan parasites and may be a useful drug target. However, the search for NH inhibitors has been hampered by the lack of suitable ... ...

    Abstract Nucleoside hydrolase (NH) (EC 3.2.2.3) is an essential enzyme in the purine-pyrimidine salvage pathway utilised by many protozoan parasites and may be a useful drug target. However, the search for NH inhibitors has been hampered by the lack of suitable in vitro screens. We have constructed a Saccharomyces cerevisiae strain that requires expression of the Leishmania major nucleoside hydrolase (LmNH) enzyme for growth and that may be suitable as a screen for NH inhibitors. The gene encoding LmNH was amplified using polymerase chain reaction with L. major genomic DNA as the template, cloned into an expression vector and used to transform a yeast mutant unable to grow on uridine as the sole source of uracil. Expression of LmNH yielded an ca. 35.6kDa protein, which was shown to be functional as the mutant strain was able to grow on medium containing uridine as the sole source of uracil. Importantly, this work has resulted in a strain that can be used to screen compounds as potential inhibitors of this essential Leishmania enzyme.
    MeSH term(s) Animals ; Blotting, Western ; Copper/pharmacology ; Gene Expression Regulation, Enzymologic/drug effects ; Genes, Transgenic, Suicide ; Genetic Vectors/genetics ; Leishmania major/enzymology ; Leishmania major/genetics ; Molecular Sequence Data ; N-Glycosyl Hydrolases/genetics ; N-Glycosyl Hydrolases/metabolism ; Promoter Regions, Genetic/genetics ; Proto-Oncogene Proteins c-myc/genetics ; Protozoan Proteins/genetics ; Protozoan Proteins/metabolism ; Recombinant Fusion Proteins/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Transformation, Genetic ; Transgenes/genetics ; Uracil/metabolism ; Uridine/metabolism
    Chemical Substances Proto-Oncogene Proteins c-myc ; Protozoan Proteins ; Recombinant Fusion Proteins ; Uracil (56HH86ZVCT) ; Copper (789U1901C5) ; N-Glycosyl Hydrolases (EC 3.2.2.-) ; Uridine (WHI7HQ7H85)
    Language English
    Publishing date 2007-01
    Publishing country Netherlands
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 1093977-5
    ISSN 1872-7913 ; 0924-8579
    ISSN (online) 1872-7913
    ISSN 0924-8579
    DOI 10.1016/j.ijantimicag.2006.08.029
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  6. Article: Use of a temperature-sensitive, protoplast-forming Neurospora crassa strain for the detection of antifungal antibiotics.

    Selitrennikoff, C P

    Antimicrobial agents and chemotherapy

    1983  Volume 23, Issue 5, Page(s) 757–765

    Abstract: ... divided as cell wall-less cells when incubated under certain conditions at 37 degrees C. Each protoplast ... regenerated cell wall and formed a mycelium when the temperature was shifted to 22 degrees C. Cell wall ...

    Abstract Protoplasts of the temperature-sensitive osmotic-1 mutant of Neurospora crassa grew and divided as cell wall-less cells when incubated under certain conditions at 37 degrees C. Each protoplast regenerated cell wall and formed a mycelium when the temperature was shifted to 22 degrees C. Cell wall regeneration, but not cell growth, was prevented by the inhibition of cell wall assembly functions. Thus, the inhibition of cell wall regeneration could serve as an indicator of the mode of action of antibiotic drugs. A method for detecting cell wall-inhibiting antifungal compounds with osmotic-1 protoplasts is described.
    MeSH term(s) Anti-Bacterial Agents/pharmacology ; Antifungal Agents/pharmacology ; Chemical Phenomena ; Chemistry ; Neurospora/drug effects ; Neurospora crassa/drug effects ; Neurospora crassa/growth & development ; Protoplasts/drug effects ; Temperature
    Chemical Substances Anti-Bacterial Agents ; Antifungal Agents
    Language English
    Publishing date 1983-05
    Publishing country United States
    Document type Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 217602-6
    ISSN 1098-6596 ; 0066-4804
    ISSN (online) 1098-6596
    ISSN 0066-4804
    DOI 10.1128/AAC.23.5.757
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    In stock of ZB MED Cologne/Königswinter

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  7. Article: Screening for antifungal drugs

    Selitrennikoff, C.P

    Biotechnology of filamentous fungi : technology and products /

    1992  

    Keywords antifungal agents
    Language English
    Size p. 189-217.
    Publisher Butterworth-Heinemann, c1992.
    Publishing place Boston
    Document type Article
    ISBN 0750691158 ; 9780750691154
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  8. Article: Cell wall assembly of Neurospora crassa: lack of evidence for preexisting cell wall acting as primer or template.

    Selitrennikoff, C P

    Developmental biology

    1983  Volume 97, Issue 1, Page(s) 245–249

    Abstract: Cell wall formation of Neurospora crassa and other filamentous fungi involves the apical extension of preexisting cell wall in a complex assembly sequence; however, it is not known if preexisting wall participates in the formation of new cell wall. It ... ...

    Abstract Cell wall formation of Neurospora crassa and other filamentous fungi involves the apical extension of preexisting cell wall in a complex assembly sequence; however, it is not known if preexisting wall participates in the formation of new cell wall. It was found that temperature-sensitive protoplasts which lack detectable preexisting wall form cell wall upon a shift to a permissive temperature. Similarly, temperature-sensitive colonial mutants form morphologically normal cell wall directly from preexisting abnormal hyphae after a shift to a permissive temperature. These results are consistent with the idea that cell wall assembly occurs without the participation of preexisting cell wall as either primer or template for new cell wall assembly.
    MeSH term(s) Cell Wall/physiology ; Hot Temperature ; Mutation ; Neurospora/physiology ; Neurospora crassa/genetics ; Neurospora crassa/physiology ; Protoplasts/physiology ; Templates, Genetic
    Language English
    Publishing date 1983-05
    Publishing country United States
    Document type Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 1114-9
    ISSN 1095-564X ; 0012-1606
    ISSN (online) 1095-564X
    ISSN 0012-1606
    DOI 10.1016/0012-1606(83)90082-9
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  9. Article: Regulation of the hexosamine biosynthetic pathway in the water mold Blastocladiella emersonii: Sensitivity to endproduct inhibition is dependent upon the life cycle phase.

    Selitrennikoff, C P / Dalley, N E / Sonneborn, D R

    Proceedings of the National Academy of Sciences of the United States of America

    2002  Volume 77, Issue 10, Page(s) 5998–6002

    Abstract: Chitin, a homopolymer of N-acetylglucosamine (GlcNAc), is the major macromolecular constituent of Blastocladiella emersonii cell walls. Zoospores do not possess a wall nor do they contain sufficient total hexosamine to account for the chitin content of ... ...

    Abstract Chitin, a homopolymer of N-acetylglucosamine (GlcNAc), is the major macromolecular constituent of Blastocladiella emersonii cell walls. Zoospores do not possess a wall nor do they contain sufficient total hexosamine to account for the chitin content of the wall abruptly formed during germination. UDPGlcNAc, both the endproduct of hexosamine biosynthesis and the substrate for chitin synthesis, is present in zoospores in sufficient concentration to inhibit the first hexosamine pathway-specific enzyme activity. Net chitin accumulates in register with dry weight during exponential growth, but does not accumulate appreciably during the succeeding sporulation phase. Predicted relationships among net rates of chitin synthesis, UDPGlcNAc concentrations, and UDP plus UTP concentrations throughout the life cycle are explored, as are the assumptions upon which the predictions were based. We find that the sensitivity of the first hexosamine pathway-specific enzyme to endproduct inhibition is not constant throughout the life cycle; sensitivity is very high in the zoospore phase, decreases dramatically during germination, remains very low through the growth phase, and increases gradually to the zoospore level during sporulation. The organism appears to have evolved endproduct regulation in this case as an adaptation to "hard-times" phases of the life cycle-i.e., as a safeguard against overproduction of end product (UDPGlcNAc) when its utilization in cell wall (specifically chitin) synthesis is curtailed. Conversely, the organism effectively discards this mode of regulation during "good times," when the demands for end product are evidently greater than endproduct inhibition would otherwise permit.
    Language English
    Publishing date 2002-09-13
    Publishing country United States
    Document type Journal Article
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.77.10.5998
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    Zs.A 1148: Show issues Location:
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  10. Article: Cloning and characterization of a Neurospora crassa gene required for (1,3) beta-glucan synthase activity and cell wall formation.

    Enderlin, C S / Selitrennikoff, C P

    Proceedings of the National Academy of Sciences of the United States of America

    1994  Volume 91, Issue 20, Page(s) 9500–9504

    Abstract: The glucan synthase 1 gene (gs-1) is required for (1,3) beta-glucan synthase activity [E.C. 2.4.1 ...

    Abstract The glucan synthase 1 gene (gs-1) is required for (1,3) beta-glucan synthase activity [E.C. 2.4.1.34; UDP glucose:1,3-beta-D-glucan 3-beta-D-glucosyltransferase] and for cell wall formation. The gs-1 gene was cloned by functional complementation of the cell-wall-less defect of the (1,3) beta-glucan synthase-deficient mutant, TM1, by using a genomic Neurospora crassa cosmid library. A 2568-nucleotide gs-1 cDNA sequence revealed a 532-amino acid open reading frame encoding a polypeptide of 59 kDa. The predicted gs-1 gene product has no obvious signal peptide cleavage sites or transmembrane domains. A gs-1 null mutant is defective for cell wall formation and (1,3) beta-glucan synthase activity. The predicted GS-1 protein is weakly homologous to a putative Saccharomyces cerevisiae transcriptional regulatory protein.
    MeSH term(s) Amino Acid Sequence ; Base Sequence ; Cell Wall/genetics ; Cloning, Molecular ; DNA, Fungal/chemistry ; Genes, Fungal ; Glucosyltransferases/biosynthesis ; Membrane Proteins ; Molecular Sequence Data ; Neurospora crassa/enzymology ; Neurospora crassa/genetics ; Restriction Mapping ; Saccharomyces cerevisiae/genetics ; Schizosaccharomyces pombe Proteins ; Sequence Homology, Amino Acid
    Chemical Substances DNA, Fungal ; Membrane Proteins ; Schizosaccharomyces pombe Proteins ; Glucosyltransferases (EC 2.4.1.-) ; 1,3-beta-glucan synthase (EC 2.4.1.34)
    Language English
    Publishing date 1994-09-27
    Publishing country United States
    Document type Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.91.20.9500
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