Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Kim L Gonzalez"'
Autor:
Hao-Ching Hsiao, Kim L Gonzalez, Daniel J Catanese, Kristopher E Jordy, Kathleen S Matthews, Sarah E Bondos
Publikováno v:
PLoS ONE, Vol 9, Iss 10, p e108217 (2014)
Interactions between structured proteins require a complementary topology and surface chemistry to form sufficient contacts for stable binding. However, approximately one third of protein interactions are estimated to involve intrinsically disordered
Externí odkaz:
https://doaj.org/article/45f0fe4a2e5548fcb7176e914bf591e4
Publikováno v:
Plant Physiology. 176:162-177
Recent advances highlight understanding of the diversity of peroxisome contributions to plant biology and the mechanisms through which these essential organelles are generated.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::55a8887adadacd540ef00c2720fd9874
https://doi.org/10.1104/pp.17.01050
https://doi.org/10.1104/pp.17.01050
Autor:
Wendell A. Fleming, Kim L. Gonzalez, Jaeseok Park, Meredith J. Ventura, Mauro A. Rinaldi, Ashish B. Patel, Bonnie Bartel
Publikováno v:
Plant Physiology. 174:2231-2247
A variety of metabolic pathways are sequestered in peroxisomes, conserved organelles that are essential for human and plant survival. Peroxin (PEX) proteins generate and maintain peroxisomes. The PEX1 ATPase facilitates recycling of the peroxisome ma
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::59f99c9fe266c8ed86ce16c309b7c27c
https://doi.org/10.1104/pp.17.00548
https://doi.org/10.1104/pp.17.00548
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
https://pubmed.ncbi.nlm.nih.gov/29555730
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
https://doi.org/10.1073/pnas.1721279115
Autor:
Daniel J. Catanese, Kristopher E. Jordy, Hao-Ching Hsiao, Kathleen S. Matthews, Sarah E. Bondos, Kim L. Gonzalez
Publikováno v:
PLoS ONE, Vol 9, Iss 10, p e108217 (2014)
PLoS ONE
PLoS ONE
Interactions between structured proteins require a complementary topology and surface chemistry to form sufficient contacts for stable binding. However, approximately one third of protein interactions are estimated to involve intrinsically disordered
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0c819dbc4cefe5fa7483d5c8501a3a5f
https://doaj.org/article/45f0fe4a2e5548fcb7176e914bf591e4
https://doaj.org/article/45f0fe4a2e5548fcb7176e914bf591e4
Autor:
Sarah E. Bondos, Zabeena Merchant, Hao-Ching Hsiao, Kim L. Gonzalez, Ying Liu, Kathleen S. Matthews
Publikováno v:
Biological Procedures
Biological Procedures Online, Vol 13, Iss 1, p 6 (2011)
Biological Procedures Online, Vol 13, Iss 1, p 6 (2011)
Although yeast two-hybrid experiments are commonly used to identify protein interactions, the frequent occurrence of false negatives and false positives hampers data interpretation. Using both yeast one-hybrid and two-hybrid experiments, we have iden
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::529a1806798f5b4cdd02aed15f3dc106