Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Scott Betts"'
Autor:
Huirong Gao, Jasdeep Mutti, Joshua K. Young, Meizhu Yang, Megan Schroder, Brian Lenderts, Lijuan Wang, Dave Peterson, Grace St. Clair, Spencer Jones, Lanie Feigenbutz, Wally Marsh, Min Zeng, Susan Wagner, Jeffry Farrell, Kay Snopek, Chris Scelonge, Xiaoyi Sopko, Jeffry D. Sander, Scott Betts, A. Mark Cigan, N. Doane Chilcoat
Publikováno v:
Frontiers in Plant Science, Vol 11 (2020)
Modern maize hybrids often contain biotech and native traits. To-date all biotech traits have been randomly inserted in the genome. Consequently, developing hybrids with multiple traits is expensive, time-consuming, and complex. Here we report using
Externí odkaz:
https://doaj.org/article/1e57717eb81b4cd696863de608e3ba39
Autor:
Bill Gordon-Kamm, Nagesh Sardesai, Maren Arling, Keith Lowe, George Hoerster, Scott Betts, Todd Jones
Publikováno v:
Plants, Vol 8, Iss 2, p 38 (2019)
Efficient transformation of numerous important crops remains a challenge, due predominantly to our inability to stimulate growth of transgenic cells capable of producing plants. For years, this difficulty has been partially addressed by tissue cultur
Externí odkaz:
https://doaj.org/article/d65ba3f1c68d4d28aabaac1d16ec2706
Autor:
Keith S. Lowe, Scott Betts, And Todd Jones, Maren Arling, George J. Hoerster, Bill Gordon-Kamm, Nagesh Sardesai
Publikováno v:
Plants
Plants, Vol 8, Iss 2, p 38 (2019)
Plants, Vol 8, Iss 2, p 38 (2019)
Efficient transformation of numerous important crops remains a challenge, due predominantly to our inability to stimulate growth of transgenic cells capable of producing plants. For years, this difficulty has been partially addressed by tissue cultur
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b6db2b37e2d8e28f54a760c222173b92
https://pubmed.ncbi.nlm.nih.gov/30754699
https://pubmed.ncbi.nlm.nih.gov/30754699
The processive beta-strands and turns of a polypeptide parallel beta-helix represent one of the topologically simplest beta-sheet folds. The three subunits of the tailspike adhesin of phage P22 each contain 13 rungs of a parallel beta-helix followed
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::53db1f3b5bbb223b6d81208f843efa8f
https://europepmc.org/articles/PMC2280027/
https://europepmc.org/articles/PMC2280027/
Publikováno v:
Additives in Water-borne Coatings ISBN: 9780854046133
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b0cba7f8bd4aec6379d879e54fc465f6
https://doi.org/10.1039/9781847550057-00007
https://doi.org/10.1039/9781847550057-00007
Publikováno v:
Protein science : a publication of the Protein Society. 11(4)
The P22 tailspike adhesin is an elongated thermostable trimer resistant to protease digestion and to denaturation in sodium dodecyl sulfate. Monomeric, dimeric, and protrimeric folding and assembly intermediates lack this stability and are thermolabi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9fa32e2d13517186aaf8f9c3eae82765
https://pubmed.ncbi.nlm.nih.gov/11910025
https://pubmed.ncbi.nlm.nih.gov/11910025
Autor:
Lisa Stuart, Stephen W. Raso, Cameron Haase-Pettingell, Scott Betts, Jonathan King, Anne S. Robinson
Publikováno v:
Protein science : a publication of the Protein Society. 10(2)
The predominantly beta-sheet phage P22 tailspike adhesin contains eight reduced cysteines per 666 residue chain, which are buried and unreactive in the native trimer. In the pathway to the native trimer, both in vivo and in vitro transient interchain
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::272f3be34be7b0e82287e54ca5d91910
https://pubmed.ncbi.nlm.nih.gov/11266625
https://pubmed.ncbi.nlm.nih.gov/11266625
A right-handed parallel beta-helix of 400 residues in 13 tightly packed coils is a major motif of the chains forming the trimeric P22 tailspike adhesin. The beta-helix domains of three identical subunits are side-by-side in the trimer and make predom
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8165d03277162e420028829484ac0b9e
https://europepmc.org/articles/PMC2144511/
https://europepmc.org/articles/PMC2144511/
Publisher Summary Protein misfolding and aggregation have been implicated in the molecular basis of several human diseases. The failure of correct folding and assembly processes also limits yields of recombinant proteins in research laboratories and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::32bbabc7f02dc143b63c5edcf091e28e
https://doi.org/10.1016/s0076-6879(99)09024-2
https://doi.org/10.1016/s0076-6879(99)09024-2
Autor:
Scott Betts, Jonathan King
Off-pathway intermolecular interactions between partially folded polypeptide chains often compete with correct intramolecular interactions, resulting in self-association of folding intermediates into the inclusion body state. Intermediates for both p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ddf164c8548d8b937ed0dd8e811af371
https://europepmc.org/articles/PMC2144048/
https://europepmc.org/articles/PMC2144048/