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Showing 1 to 9 of 9 entries
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Coordinated and Iterative Enzyme Catalysis in Fungal Polyketide Biosynthesis.

ACS catalysis

Hang L, Liu N, Tang Y.
PMID: 28529817
ACS Catal. 2016 Sep 02;6(9):5935-5945. doi: 10.1021/acscatal.6b01559. Epub 2016 Jul 27.

Fungal polyketides are natural products with great chemical diversity that exhibit a wide range of biological activity. This chemical diversity stems from specialized enzymes encoded in the biosynthetic gene cluster responsible for the natural product biosynthesis. Fungal polyketide synthases...

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Hang L, Liu N, Tang Y. Coordinated and Iterative Enzyme Catalysis in Fungal Polyketide Biosynthesis. ACS Catal. 2016;6(9):5935-5945doi: 10.1021/acscatal.6b01559.
Hang, L., Liu, N., & Tang, Y. (2016). Coordinated and Iterative Enzyme Catalysis in Fungal Polyketide Biosynthesis. ACS catalysis, 6(9), 5935-5945. https://doi.org/10.1021/acscatal.6b01559
Hang, Leibniz, et al. "Coordinated and Iterative Enzyme Catalysis in Fungal Polyketide Biosynthesis." ACS catalysis vol. 6,9 (2016): 5935-5945. doi: https://doi.org/10.1021/acscatal.6b01559
Hang L, Liu N, Tang Y. Coordinated and Iterative Enzyme Catalysis in Fungal Polyketide Biosynthesis. ACS Catal. 2016 Sep 02;6(9):5935-5945. doi: 10.1021/acscatal.6b01559. Epub 2016 Jul 27. PMID: 28529817; PMCID: PMC5436725.
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Mycotoxins of Aspergillus clavatus: Toxicity of Cytochalasin E, Patulin, and Extracts of Contaminated Barley Malt.

Journal of food protection

Lopez-Diaz TM, Flannigan B.
PMID: 31207790
J Food Prot. 1997 Nov;60(11):1381-1385. doi: 10.4315/0362-028X-60.11.1381.

Brine shrimp and conductimetric Saccharomyces cerevisiae bioassays were used to investigate the toxicity of green barley malt prepared at 16 and 25°C from grain inoculated with a strain of Aspergillus clavatus known to produce the mycotoxins cytochalasin E and...

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Lopez-Diaz TM, Flannigan B. Mycotoxins of Aspergillus clavatus: Toxicity of Cytochalasin E, Patulin, and Extracts of Contaminated Barley Malt. J Food Prot. 1997;60(11):1381-1385doi: 10.4315/0362-028X-60.11.1381.
Lopez-Diaz, T. M., & Flannigan, B. (1997). Mycotoxins of Aspergillus clavatus: Toxicity of Cytochalasin E, Patulin, and Extracts of Contaminated Barley Malt. Journal of food protection, 60(11), 1381-1385. https://doi.org/10.4315/0362-028X-60.11.1381
Lopez-Diaz, Teresa-Maria, and Flannigan, Brian. "Mycotoxins of Aspergillus clavatus: Toxicity of Cytochalasin E, Patulin, and Extracts of Contaminated Barley Malt." Journal of food protection vol. 60,11 (1997): 1381-1385. doi: https://doi.org/10.4315/0362-028X-60.11.1381
Lopez-Diaz TM, Flannigan B. Mycotoxins of Aspergillus clavatus: Toxicity of Cytochalasin E, Patulin, and Extracts of Contaminated Barley Malt. J Food Prot. 1997 Nov;60(11):1381-1385. doi: 10.4315/0362-028X-60.11.1381. PMID: 31207790.
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Cytochalasin-E-Resistant Mutants of Coprinus cinereus: Isolation and Genetic, Biochemical, and Cytological Analyses.

Fungal genetics and biology : FG & B

Tsukamoto M, Yamamoto M, Tanabe S, Kamada T.
PMID: 8812286
Fungal Genet Biol. 1996 Mar;20(1):52-8. doi: 10.1006/fgbi.1996.0009.

We first obtained a cytochalasin-E supersensitive strain (CES14) of the basidiomycete Coprinus cinereus and then isolated 1000 revertants of CES14, expecting that at least some of the revertants have defects in the functions of actin filaments. Microscopic examination revealed...

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Tsukamoto M, Yamamoto M, Tanabe S, et al. Cytochalasin-E-Resistant Mutants of Coprinus cinereus: Isolation and Genetic, Biochemical, and Cytological Analyses. Fungal Genet Biol. 1996;20(1):52-8doi: 10.1006/fgbi.1996.0009.
Tsukamoto, M., Yamamoto, M., Tanabe, S., & Kamada, T. (1996). Cytochalasin-E-Resistant Mutants of Coprinus cinereus: Isolation and Genetic, Biochemical, and Cytological Analyses. Fungal genetics and biology : FG & B, 20(1), 52-8. https://doi.org/10.1006/fgbi.1996.0009
Tsukamoto, et al. "Cytochalasin-E-Resistant Mutants of Coprinus cinereus: Isolation and Genetic, Biochemical, and Cytological Analyses." Fungal genetics and biology : FG & B vol. 20,1 (1996): 52-8. doi: https://doi.org/10.1006/fgbi.1996.0009
Tsukamoto M, Yamamoto M, Tanabe S, Kamada T. Cytochalasin-E-Resistant Mutants of Coprinus cinereus: Isolation and Genetic, Biochemical, and Cytological Analyses. Fungal Genet Biol. 1996 Mar;20(1):52-8. doi: 10.1006/fgbi.1996.0009. PMID: 8812286.
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Callose deposition during the interaction between cowpea (Vigna unguiculata) and the monokaryotic stage of the cowpea rust fungus (Uromyces vignae).

The New phytologist

Škalamera D, Jibodhand S, Heath MC.
PMID: 33863006
New Phytol. 1997 Jul;136(3):511-524. doi: 10.1046/j.1469-8137.1997.00760.x.

The interaction between the race 1 of the cowpea rust fungus (Uromyces vignae Barclay) and the resistant cowpea (Vigna unguiculata (L.) Walp.) ev. Queen Anne is characterized by the deposition of callose around intracellular fungal structures. Ultrastructural examination of...

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Škalamera D, Jibodhand S, Heath MC. Callose deposition during the interaction between cowpea (Vigna unguiculata) and the monokaryotic stage of the cowpea rust fungus (Uromyces vignae). New Phytol. 1997;136(3):511-524doi: 10.1046/j.1469-8137.1997.00760.x.
Škalamera, D., Jibodhand, S., & Heath, M. C. (1997). Callose deposition during the interaction between cowpea (Vigna unguiculata) and the monokaryotic stage of the cowpea rust fungus (Uromyces vignae). The New phytologist, 136(3), 511-524. https://doi.org/10.1046/j.1469-8137.1997.00760.x
Škalamera, Dubravka, et al. "Callose deposition during the interaction between cowpea (Vigna unguiculata) and the monokaryotic stage of the cowpea rust fungus (Uromyces vignae)." The New phytologist vol. 136,3 (1997): 511-524. doi: https://doi.org/10.1046/j.1469-8137.1997.00760.x
Škalamera D, Jibodhand S, Heath MC. Callose deposition during the interaction between cowpea (Vigna unguiculata) and the monokaryotic stage of the cowpea rust fungus (Uromyces vignae). New Phytol. 1997 Jul;136(3):511-524. doi: 10.1046/j.1469-8137.1997.00760.x. PMID: 33863006.
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Localization of GPIb/IX and GPIIb/IIIa on Discoid Platelets.

Platelets

White JG, Krumwiede MD, Johnson DK, Escolar G.
PMID: 21043734
Platelets. 1995;6(4):233-41. doi: 10.3109/09537109509078460.

The organization and reorganization of mobile receptors, GPIIb/IIIa and GPIb/IX, on surface- and suspension-activated platelets have been studied in detail, but their distribution on resting, discoid platelets is uncertain. The present study has treated platelets in suspension with cytochalasin...

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White JG, Krumwiede MD, Johnson DK, et al. Localization of GPIb/IX and GPIIb/IIIa on Discoid Platelets. Platelets. 1995;6(4):233-41doi: 10.3109/09537109509078460.
White, J. G., Krumwiede, M. D., Johnson, D. K., & Escolar, G. (1995). Localization of GPIb/IX and GPIIb/IIIa on Discoid Platelets. Platelets, 6(4), 233-41. https://doi.org/10.3109/09537109509078460
White, J G, et al. "Localization of GPIb/IX and GPIIb/IIIa on Discoid Platelets." Platelets vol. 6,4 (1995): 233-41. doi: https://doi.org/10.3109/09537109509078460
White JG, Krumwiede MD, Johnson DK, Escolar G. Localization of GPIb/IX and GPIIb/IIIa on Discoid Platelets. Platelets. 1995;6(4):233-41. doi: 10.3109/09537109509078460. PMID: 21043734.
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Binding of polymerizing fibrin to integrin alpha(IIb)beta(3) on chymotrypsin-treated rabbit platelets decreases phosphatidylinositol 4,5-bisphosphate and increases cytoskeletal actin.

Platelets

Vickers JD.
PMID: 16801097
Platelets. 1999 Jul;10(4):228-37. doi: 10.1080/09537109976077.

Incubation of polymerizing fibrin with washed, chymotrypsin-treated (CT) rabbit platelets resulted in the formation of platelet-fibrin clots, a decrease of 27.4% (P < 0.001, n = 20) in the amount of phosphatidylinositol 4,5-bisphosphate (PIP) and an increase of 37.2%...

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Vickers JD. Binding of polymerizing fibrin to integrin alpha(IIb)beta(3) on chymotrypsin-treated rabbit platelets decreases phosphatidylinositol 4,5-bisphosphate and increases cytoskeletal actin. Platelets. 1999;10(4):228-37doi: 10.1080/09537109976077.
Vickers, J. D. (1999). Binding of polymerizing fibrin to integrin alpha(IIb)beta(3) on chymotrypsin-treated rabbit platelets decreases phosphatidylinositol 4,5-bisphosphate and increases cytoskeletal actin. Platelets, 10(4), 228-37. https://doi.org/10.1080/09537109976077
Vickers, J D. "Binding of polymerizing fibrin to integrin alpha(IIb)beta(3) on chymotrypsin-treated rabbit platelets decreases phosphatidylinositol 4,5-bisphosphate and increases cytoskeletal actin." Platelets vol. 10,4 (1999): 228-37. doi: https://doi.org/10.1080/09537109976077
Vickers JD. Binding of polymerizing fibrin to integrin alpha(IIb)beta(3) on chymotrypsin-treated rabbit platelets decreases phosphatidylinositol 4,5-bisphosphate and increases cytoskeletal actin. Platelets. 1999 Jul;10(4):228-37. doi: 10.1080/09537109976077. PMID: 16801097.
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Changes in the cytoskeleton accompanying infection-induced nuclear movements and the hypersensitive response in plant cells invaded by rust fungi.

The Plant journal : for cell and molecular biology

Skalamera D, Heath MC.
PMID: 22507136
Plant J. 1998 Oct;16(2):191-200. doi: 10.1046/j.1365-313x.1998.00285.x.

During the infection of cowpea (Vigna unguiculata) by the cowpea rust fungus (Uromyces vignae, race 1 ) the plant nucleus moves towards and away from the invading hypha and eventually moves close to the fungus in the susceptible cultivar...

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Skalamera D, Heath MC. Changes in the cytoskeleton accompanying infection-induced nuclear movements and the hypersensitive response in plant cells invaded by rust fungi. Plant J. 1998;16(2):191-200doi: 10.1046/j.1365-313x.1998.00285.x.
Skalamera, D., & Heath, M. C. (1998). Changes in the cytoskeleton accompanying infection-induced nuclear movements and the hypersensitive response in plant cells invaded by rust fungi. The Plant journal : for cell and molecular biology, 16(2), 191-200. https://doi.org/10.1046/j.1365-313x.1998.00285.x
Skalamera, D, and Heath, M C. "Changes in the cytoskeleton accompanying infection-induced nuclear movements and the hypersensitive response in plant cells invaded by rust fungi." The Plant journal : for cell and molecular biology vol. 16,2 (1998): 191-200. doi: https://doi.org/10.1046/j.1365-313x.1998.00285.x
Skalamera D, Heath MC. Changes in the cytoskeleton accompanying infection-induced nuclear movements and the hypersensitive response in plant cells invaded by rust fungi. Plant J. 1998 Oct;16(2):191-200. doi: 10.1046/j.1365-313x.1998.00285.x. PMID: 22507136.
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Electrophysiology of K+ transport by midgut epithelium of lepidopteran insect larvae. IV. A multicompartment model accounts for tetramethylammonium entry into goblet cavities.

The Journal of experimental biology

Koch A, Moffett D.
PMID: 9320027
J Exp Biol. 1995;198:2115-25.

A quantitative model was developed to explain the kinetics of tetramethylammonium (TMA+) movement into and out of the goblet cavities of posterior midgut cells of Manduca sexta based on the data of the accompanying paper, which indicated that TMA+...

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Koch A, Moffett D. Electrophysiology of K+ transport by midgut epithelium of lepidopteran insect larvae. IV. A multicompartment model accounts for tetramethylammonium entry into goblet cavities. J Exp Biol. 1995;198:2115-25
Koch, A., & Moffett, D. (1995). Electrophysiology of K+ transport by midgut epithelium of lepidopteran insect larvae. IV. A multicompartment model accounts for tetramethylammonium entry into goblet cavities. The Journal of experimental biology, 1982115-25.
Koch, and Moffett. "Electrophysiology of K+ transport by midgut epithelium of lepidopteran insect larvae. IV. A multicompartment model accounts for tetramethylammonium entry into goblet cavities." The Journal of experimental biology vol. 198 (1995): 2115-25.
Koch A, Moffett D. Electrophysiology of K+ transport by midgut epithelium of lepidopteran insect larvae. IV. A multicompartment model accounts for tetramethylammonium entry into goblet cavities. J Exp Biol. 1995;198:2115-25. PMID: 9320027.
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Electrophysiology of K+ transport by midgut epithelium of lepidopteran insect larvae. III. Goblet valve patency.

The Journal of experimental biology

Moffett D, Koch A, Woods R.
PMID: 9320016
J Exp Biol. 1995;198:2103-13.

The midgut epithelium of lepidopteran insect larvae contains characteristic goblet cells possessing an apical cavity surrounded by goblet cell apical membrane (GCAM) and guarded from the gut lumen by a valve-like structure. The currently accepted model of active K+...

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Moffett D, Koch A, Woods R. Electrophysiology of K+ transport by midgut epithelium of lepidopteran insect larvae. III. Goblet valve patency. J Exp Biol. 1995;198:2103-13
Moffett, D., Koch, A., & Woods, R. (1995). Electrophysiology of K+ transport by midgut epithelium of lepidopteran insect larvae. III. Goblet valve patency. The Journal of experimental biology, 1982103-13.
Moffett, et al. "Electrophysiology of K+ transport by midgut epithelium of lepidopteran insect larvae. III. Goblet valve patency." The Journal of experimental biology vol. 198 (1995): 2103-13.
Moffett D, Koch A, Woods R. Electrophysiology of K+ transport by midgut epithelium of lepidopteran insect larvae. III. Goblet valve patency. J Exp Biol. 1995;198:2103-13. PMID: 9320016.
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Showing 1 to 9 of 9 entries