Výsledky vyhledávání - "Sarah E. Ratzel"

Autor: Kim L, Gonzalez, Sarah E, Ratzel, Kendall H, Burks, Charles H, Danan, Jeanne M, Wages, Bethany K, Zolman, Bonnie, Bartel

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America. 115(14)

ATPases have diverse cellular roles, including extracting proteins from membranes to maintain organellar function. The PEX1–PEX6 heterohexameric ATPases are thought to retrotranslocate PEX5 from the peroxisome membrane, and PEX1–PEX6 dysfunction

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::50708131ba1e3e1fd5ff70dec93c5567
https://pubmed.ncbi.nlm.nih.gov/29555730

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A pex1 missense mutation improves peroxisome function in a subset of Arabidopsis pex6 mutants without restoring PEX5 recycling

Autor: Bonnie Bartel, Bethany K. Zolman, Charles H. Danan, Jeanne M. Wages, Kendall H. Burks, Kim L. Gonzalez, Sarah E. Ratzel

Publikováno v: Proceedings of the National Academy of Sciences. 115

Peroxisomes are eukaryotic organelles critical for plant and human development because they house essential metabolic functions, such as fatty acid β-oxidation. The interacting ATPases PEX1 and PEX6 contribute to peroxisome function by recycling PEX

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::0034786eaf4813e02461dad35034bfd6
https://doi.org/10.1073/pnas.1721279115

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A viable Arabidopsis pex13 missense allele confers severe peroxisomal defects and decreases PEX5 association with peroxisomes

Autor: Sarah E. Burkhart, Andrew Woodward, Bonnie Bartel, Wendell A. Fleming, Marta Bjornson, Sarah E. Ratzel

Publikováno v: Plant Molecular Biology. 86:201-214

Peroxisomes are organelles that catabolize fatty acids and compartmentalize other oxidative metabolic processes in eukaryotes. Using a forward-genetic screen designed to recover severe peroxisome-defective mutants, we isolated a viable allele of the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::847650d1cbca625e68997c881099dfe4
https://doi.org/10.1007/s11103-014-0223-8

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Reducing PEX13 expression ameliorates physiological defects of late-acting peroxin mutants

Autor: Sarah E. Ratzel, Bonnie Bartel, Matthew J. Lingard, Andrew Woodward

Publikováno v: Traffic (Copenhagen, Denmark). 12(1)

Proteins are targeted to the peroxisome matrix via processes that are mechanistically distinct from those used by other organelles. Protein entry into peroxisomes requires peroxin (PEX) proteins, including early-acting receptor (e.g., PEX5) and docki

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::50855eaf09998d71f4cd651914d00161
https://pubmed.ncbi.nlm.nih.gov/20969679

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Matrix proteins are inefficiently imported into Arabidopsis peroxisomes lacking the receptor-docking peroxin PEX14

Autor: Sarah E. Ratzel, Naxhiely Martínez Ramón, Sarah E. Christensen, Matthew J. Lingard, Bonnie Bartel, Melanie Monroe-Augustus, Chaya Murali

Publikováno v: Plant molecular biology. 77(1-2)

Mutations in peroxisome biogenesis proteins (peroxins) can lead to developmental deficiencies in various eukaryotes. PEX14 and PEX13 are peroxins involved in docking cargo-receptor complexes at the peroxisomal membrane, thus aiding in the transport o

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ec0d309c1a1196c43b55accafb9c6705
https://pubmed.ncbi.nlm.nih.gov/21553312

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Mutation of E1-CONJUGATING ENZYME-RELATED1 decreases RELATED TO UBIQUITIN conjugation and alters auxin response and development

Autor: Yousif Shamoo, Erin E. Woodward, Bonnie Bartel, Andrew Woodward, Sarah E. Ratzel

Publikováno v: Plant physiology. 144(2)

The ubiquitin-like protein RELATED TO UBIQUITIN (RUB) is conjugated to CULLIN (CUL) proteins to modulate the activity of Skp1-Cullin-F-box (SCF) ubiquitylation complexes. RUB conjugation to specific target proteins is necessary for the development of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d5f853dd4e84f74f8c99ef83bb91a34f
https://pubmed.ncbi.nlm.nih.gov/17449645

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