Zobrazeno 1 - 10
of 52
pro vyhledávání: '"Susan K, Boehlein"'
Autor:
Christina Finegan, Susan K. Boehlein, Kristen A. Leach, Gabriela Madrid, L. Curtis Hannah, Karen E. Koch, William F. Tracy, Marcio F. R. Resende
Publikováno v:
Frontiers in Plant Science, Vol 12 (2022)
In maize, starch mutants have facilitated characterization of key genes involved in endosperm starch biosynthesis such as large subunit of AGPase Shrunken2 (Sh2) and isoamylase type DBE Sugary1 (Su1). While many starch biosynthesis enzymes have been
Externí odkaz:
https://doaj.org/article/d4992f7ff85f4ba0b3899671b966708d
Publikováno v:
Frontiers in Plant Science, Vol 9 (2018)
ADP-glucose pyrophosphorylase (AGPase) is an important enzyme in starch synthesis and previous studies showed that the heat lability of this enzyme is a determinant to starch synthesis in the maize endosperm and, in turn, seed yield. Here, amino acid
Externí odkaz:
https://doaj.org/article/39e0cf361bbc4f4fabea85868a465e5c
Publikováno v:
Molecules, Vol 25, Iss 3, p 637 (2020)
Owing to its unique structure and properties, the glucose dendrimer phytoglycogen is gaining interest for medical and biotechnology applications. Although many maize variants are available from commercial and academic breeding programs, most applicat
Externí odkaz:
https://doaj.org/article/d42e5c077b964e7e82dc1651e5828a71
Autor:
Christina Finegan, Susan K. Boehlein, Kristen A. Leach, Gabriela Madrid, L. Curtis Hannah, Karen E. Koch, William F. Tracy, Marcio F. R. Resende
Publikováno v:
Frontiers in Plant Science, Vol 12 (2022)
In maize, starch mutants have facilitated characterization of key genes involved in endosperm starch biosynthesis such as large subunit of AGPase Shrunken2 (Sh2) and isoamylase type DBE Sugary1 (Su1). While many starch biosynthesis enzymes have been
Autor:
Gaoyuan Song, Alan M. Myers, Junya Zhang, A. Mark Settles, Justin W. Walley, Shan Wu, Donald R. McCarty, Susan K. Boehlein
Publikováno v:
Journal of Cell Biology. 218:2638-2658
Chloroplasts are of prokaryotic origin with a double-membrane envelope separating plastid metabolism from the cytosol. Envelope membrane proteins integrate chloroplasts with the cell, but envelope biogenesis mechanisms remain elusive. We show that ma
Autor:
Shan Wu, Peng Liu, Masaharu Suzuki, L. C. Hannah, Camila Ribeiro, Ashley Webster, Karen E. Koch, A. Mark Settles, William F. Tracy, Donald R. McCarty, Tracie A. Hennen-Bierwagen, Jon D. Stewart, Susan K. Boehlein, Jiahn-Chou Guan, Alan M. Myers
Publikováno v:
The Plant Journal. 99:23-40
Cereal yields decrease when grain fill proceeds under conditions of prolonged, moderately elevated temperatures. Endosperm-endogenous processes alter both rate and duration of dry weight gain, but underlying mechanisms remain unclear. Heat effects co
Publikováno v:
Molecules, Vol 25, Iss 3, p 637 (2020)
Molecules
Volume 25
Issue 3
Molecules
Volume 25
Issue 3
Owing to its unique structure and properties, the glucose dendrimer phytoglycogen is gaining interest for medical and biotechnology applications. Although many maize variants are available from commercial and academic breeding programs, most applicat
Publikováno v:
Crop Science. 57:3068-3074
Autor:
Junya, Zhang, Shan, Wu, Susan K, Boehlein, Donald R, McCarty, Gaoyuan, Song, Justin W, Walley, Alan, Myers, A Mark, Settles
Publikováno v:
The Journal of Cell Biology
Zhang et al. show that the maize dek5 locus is required for chloroplast envelope biogenesis and encodes a TamB-like protein. Bacterial TamB proteins facilitate insertion of β-barrel outer membrane proteins, indicating plastids have a conserved mecha
Autor:
Shan Wu, Alan M. Myers, Gaoyuan Song, Susan K. Boehlein, Junya Zhang, Donald R. McCarty, A. Mark Settles, Justin W. Walley
Chloroplasts are of prokaryotic origin with a double membrane envelope that separates plastid metabolism from the cytosol. Envelope membrane proteins integrate the chloroplast with the cell, but the biogenesis of the envelope membrane remains elusive
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::67e65b8a966d88e927f910267cf6ebc1