Výsledky vyhledávání - "Eric C. Bretsnyder"

Comparison of in vitro and in vivo binding site competition of Bacillus thuringiensis Cry1 proteins in two important maize pests

Autor: Patricia, Hernández-Martínez, Eric C, Bretsnyder, James A, Baum, Jeff A, Haas, Graham P, Head, Agoston, Jerga, Juan, Ferré

Publikováno v: Pest management scienceREFERENCES. 78(4)

Binding site models, derived from in vitro competition binding studies, have been widely used for predicting potential cross-resistance among insecticidal proteins from Bacillus thuringiensis. However, because discrepancies have been found between bi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::4c279ce340cb8d61eec4ad66c5d0d3b0
https://pubmed.ncbi.nlm.nih.gov/34951106

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Structural and functional characterization of Mpp75Aa1.1, a putative beta-pore forming protein from Brevibacillus laterosporus active against the western corn rootworm

Autor: Milligan Jason S, Jeffrey R. Nageotte, Danqi Chen, Yoonseong Park, Stephen Duff, Jean-Louis Kouadio, Yong Yin, Agoston Jerga, Artem G Evdokimov, Timothy J. Rydel, Chunsheng Xia, Jeffrey A. Haas, William Moar, Jun Zhang, Michael J. Aikins, Kara Giddings, Meiying Zheng, Eric C. Bretsnyder

Publikováno v: PLoS ONE
PLoS ONE, Vol 16, Iss 10, p e0258052 (2021)

The western corn rootworm (WCR), Diabrotica virgifera virgifera LeConte, is a major corn pest of significant economic importance in the United States. The continuous need to control this corn maize pest and the development of field-evolved resistance

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4fe943a117d19a63dbe738c5cea75080
https://pubmed.ncbi.nlm.nih.gov/34634061

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Bacillus thuringiensis Cry1Da_7 and Cry1B.868 Protein Interactions with Novel Receptors Allow Control of Resistant Fall Armyworms, Spodoptera frugiperda (J.E. Smith)

Publikováno v: Applied and Environmental Microbiology

There is increased concern with the development of resistance to insecticidal proteins currently expressed in crop plants, especially against high-resistance-risk pests such as fall armyworm (FAW), Spodoptera frugiperda, a maize pest that already has

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6a96f3d2d82c4dea23104e75a72cb46c
https://pubmed.ncbi.nlm.nih.gov/31175187

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Mechanisms of Mitochondrial Holocytochrome c Synthase and the Key Roles Played by Cysteines and Histidine of the Heme Attachment Site, Cys-XX-Cys-His

Autor: Brian San Francisco, Gudrun S. Lukat-Rodgers, Eric C. Bretsnyder, Kenton R. Rodgers, Shalon E. Babbitt, Robert G. Kranz, Deanna L. Mendez

Publikováno v: Journal of Biological Chemistry. 289:28795-28807

Mitochondrial cytochrome c assembly requires the covalent attachment of heme by thioether bonds between heme vinyl groups and a conserved CXXCH motif of cytochrome c/c1. The enzyme holocytochrome c synthase (HCCS) binds heme and apocytochrome c subst

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5d65e37a9330703437c890b86ca27fb6
https://doi.org/10.1074/jbc.m114.593509

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Conserved Residues of the Human Mitochondrial Holocytochrome c Synthase Mediate Interactions with Heme

Autor: Eric C. Bretsnyder, Robert G. Kranz, Shalon E. Babbitt, Brian San Francisco

Publikováno v: Biochemistry

C-type cytochromes are distinguished by the covalent attachment of a heme cofactor, a modification that is typically required for its subsequent folding, stability, and function. Heme attachment takes place in the mitochondrial intermembrane space an

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4cb4db58920d235547878837689c4a33
https://doi.org/10.1021/bi500704p

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Heme Ligand Identification and Redox Properties of the Cytochrome c Synthetase, CcmF

Autor: Robert G. Kranz, Brian San Francisco, Kenton R. Rodgers, Eric C. Bretsnyder

Publikováno v: Biochemistry. 50:10974-10985

Cytochrome c maturation in many bacteria, archaea, and plant mitochondria involves the integral membrane protein CcmF, which is thought to function as a cytochrome c synthetase by facilitating the final covalent attachment of heme to the apocytochrom

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c926612186f32be1a0422143575bdc4f
https://doi.org/10.1021/bi201508t

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Human mitochondrial holocytochrome c synthase's heme binding, maturation determinants, and complex formation with cytochrome c

Autor: Eric C. Bretsnyder, Robert G. Kranz, Brian San Francisco

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America. 110(9)

Proper functioning of the mitochondrion requires the orchestrated assembly of respiratory complexes with their cofactors. Cytochrome c , an essential electron carrier in mitochondria and a critical component of the apoptotic pathway, contains a heme

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a584fc5abddcb0bfa9ba4bba3dd9e86a
https://pubmed.ncbi.nlm.nih.gov/23150584

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