Relevant bibliographies by topics / Aspergillopepsin i

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  1. Journal articles
  2. Dissertations / Theses
  3. Book chapters

Academic literature on the topic 'Aspergillopepsin i'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 February 2022

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Journal articles on the topic "Aspergillopepsin i"

1

Moralejo, Francisco J., Rosa Elena Cardoza, Santiago Gutierrez, Marta Lombraña, Francisco Fierro, and Juan F. Martín. "Silencing of the Aspergillopepsin B (pepB) Gene of Aspergillus awamori by Antisense RNA Expression or Protease Removal by Gene Disruption Results in a Large Increase in Thaumatin Production." Applied and Environmental Microbiology 68, no. 7 (2002): 3550–59. http://dx.doi.org/10.1128/aem.68.7.3550-3559.2002.

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ABSTRACT Aspergillopepsin B was identified in culture broths of Aspergillus awamori by in situ detection of its proteolytic activity and by immunodetection with anti-aspergillopepsin B antibodies. Severe thaumatin degradation was observed after in vitro treatment of thaumatin with purified aspergillopepsin B. The pepB gene encoding aspergillopepsin B of A. awamori was cloned and characterized. It is located in chromosome IV of A. awamori, as shown by pulsed-field gel electrophoresis, and encodes a protein of 282 amino acids with high similarity to the aspergillopepsin B of Aspergillus niger va
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2

Sriranganadane, Dev, Utz Reichard, Karine Salamin, et al. "Secreted glutamic protease rescues aspartic protease Pep deficiency in Aspergillus fumigatus during growth in acidic protein medium." Microbiology 157, no. 5 (2011): 1541–50. http://dx.doi.org/10.1099/mic.0.048603-0.

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In an acidic protein medium Aspergillus fumigatus secretes an aspartic endoprotease (Pep) as well as tripeptidyl-peptidases, a prolyl-peptidase and carboxypeptidases. In addition, LC-MS/MS revealed a novel glutamic protease, AfuGprA, homologous to Aspergillus niger aspergillopepsin II. The importance of AfuGprA in protein digestion was evaluated by deletion of its encoding gene in A. fumigatus wild-type D141 and in a pepΔ mutant. Either A. fumigatus Pep or AfuGprA was shown to be necessary for fungal growth in protein medium at low pH. Exoproteolytic activity is therefore not sufficient for co
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Berka, Randy M., Cynthia L. Carmona, Kirk J. Hayenga, Sheryl A. Thompson, and Michael Ward. "Isolation and characterization of the Aspergillus oryzae gene encoding aspergillopepsin O." Gene 125, no. 2 (1993): 195–98. http://dx.doi.org/10.1016/0378-1119(93)90328-z.

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Maeda, Masahiro, Kayoko Takeuchi, Masaki Kojima, et al. "Kinetic studies of unfolding process of aspergillopepsin II by pH-jump methods." Biochemical and Biophysical Research Communications 301, no. 3 (2003): 745–50. http://dx.doi.org/10.1016/s0006-291x(03)00031-7.

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Kojima, Masaki, Masaru Tanokura, Masahiro Maeda, et al. "pH-Dependent Unfolding of Aspergillopepsin II Studied by Small-Angle X-ray Scattering†." Biochemistry 39, no. 6 (2000): 1364–72. http://dx.doi.org/10.1021/bi991584o.

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Shitani, T., M. Kobayashi, and E. Ichishima. "Characterization of the S1 Subsite Specificity of Aspergillopepsin I by Site-Directed Mutagenesis." Journal of Biochemistry 120, no. 5 (1996): 974–81. http://dx.doi.org/10.1093/oxfordjournals.jbchem.a021515.

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7

Berka, Randy M., Michael Ward, Lori J. Wilson, et al. "Molecular cloning and deletion of the gene encoding aspergillopepsin A from Aspergillus awamori." Gene 86, no. 2 (1990): 153–62. http://dx.doi.org/10.1016/0378-1119(90)90274-u.

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8

Marangon, Matteo, Steven C. Van Sluyter, Ella M. C. Robinson, et al. "Degradation of white wine haze proteins by Aspergillopepsin I and II during juice flash pasteurization." Food Chemistry 135, no. 3 (2012): 1157–65. http://dx.doi.org/10.1016/j.foodchem.2012.05.042.

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9

Cho, Sang Woo, Nam-june Kim, Myung-Un Choi, and Whanchul Shin. "Structure of aspergillopepsin I fromAspergillus phoenicis: variations of the S1′–S2 subsite in aspartic proteinases." Acta Crystallographica Section D Biological Crystallography 57, no. 7 (2001): 948–56. http://dx.doi.org/10.1107/s0907444901005972.

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10

Reichard, U., M. Monod, F. Odds, and R. Rüchel. "Virulence of an aspergillopepsin-deficient mutant ofAspergillus fumigatusand evidence for another aspartic proteinase linked to the fungal cell wall." Medical Mycology 35, no. 3 (1997): 189–96. http://dx.doi.org/10.1080/02681219780001131.

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Dissertations / Theses on the topic "Aspergillopepsin i"

1

Chomarat, Nadine. "Attaque enzymatique d'un tissu conjonctif, la peauTexte imprimé." Toulouse, INSA, 1993. http://www.theses.fr/1993ISAT0022.

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La peau, tissu conjonctif tres hydrate, se compose d'un reseau collagenique impliquant des interactions avec des proteoglycannes et des glycoproteines de structure, selon un modele d'organisation supramoleculaire (scott). Dans le but de liberer le collagene de la peau, notre attention s'est focalisee sur l'approche enzymatique, soit par les proteases acides, soit par les osidases. Nous avons demontre la quasi-insolubilite du collagene dans les bases et l'uree et confirme son caractere nettement acido soluble. Dans les conditions experimentales, les exoglycosidases testees n'ont qu'un role negl
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Book chapters on the topic "Aspergillopepsin i"

1

Schomburg, Dietmar, and Dörte Stephan. "Aspergillopepsin I." In Enzyme Handbook 16. Springer Berlin Heidelberg, 1998. http://dx.doi.org/10.1007/978-3-642-58903-4_17.

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Schomburg, Dietmar, and Dörte Stephan. "Aspergillopepsin II." In Enzyme Handbook 16. Springer Berlin Heidelberg, 1998. http://dx.doi.org/10.1007/978-3-642-58903-4_18.

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Ichishima, Eiji. "Aspergillopepsin I." In Handbook of Proteolytic Enzymes. Elsevier, 2004. http://dx.doi.org/10.1016/b978-0-12-079611-3.50030-6.

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4

Takahashi, Kenji. "Aspergillopepsin II." In Handbook of Proteolytic Enzymes. Elsevier, 2004. http://dx.doi.org/10.1016/b978-0-12-079611-3.50072-0.

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5

Ichishima, Eiji. "Aspergillopepsin I." In Handbook of Proteolytic Enzymes. Elsevier, 2013. http://dx.doi.org/10.1016/b978-0-12-382219-2.00027-2.

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Journal articles
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