Zobrazeno 1 - 10
of 98
pro vyhledávání: '"Donald Oliver"'
Publikováno v:
Angle Orthod
Autor:
Donald Oliver
Growing up in the only Black family in Wolfville, Nova Scotia, Donald Oliver felt duty-bound to honour his great-grandparents, who had fled slavery in the US. His childhood, surrounded by music, family, and respected, hard-working role models, was id
Publikováno v:
The FASEB Journal. 33
Autor:
Donald Oliver
Publikováno v:
Journal of Bacteriology. 201
Characterization of Sec-dependent bacterial protein transport has often relied on an in vitro protein translocation system comprised in part of Escherichia coli inverted inner membrane vesicles or, more recently, purified SecYEG translocons reconstit
The bacterial Sec-dependent system is the major protein-biogenic pathway for protein secretion across the cytoplasmic membrane or insertion of integral membrane proteins into the phospholipid bilayer. The mechanism of SecA-driven protein transport ac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d83206a34d7d975f217c7f08923e8d4b
https://europepmc.org/articles/PMC5712611/
https://europepmc.org/articles/PMC5712611/
A conserved hairpin-like structure comprised of a signal peptide and early mature region initiates protein transport across the SecY or Sec61α channel in Bacteria or Archaea and Eukarya, respectively. When and how this initiator substrate hairpin fo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::06fb274050521fc785840c0e4415337a
https://europepmc.org/articles/PMC5584415/
https://europepmc.org/articles/PMC5584415/
Publikováno v:
Molecular microbiology. 103(3)
SecA ATPase motor protein plays a central role in bacterial protein transport by binding substrate proteins and the SecY channel complex and utilizing its ATPase activity to drive protein translocation across the plasma membrane. SecA has been shown
Signal peptides are critical for the initiation of protein transport in bacteria by virtue of their recognition by the SecA ATPase motor protein followed by their transfer to the lateral gate region of the SecYEG protein-conducting channel complex. I
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bfc5cba3501d6921634a7b9f838a8d0b
https://europepmc.org/articles/PMC4883009/
https://europepmc.org/articles/PMC4883009/
Autor:
Ishita Mukerji, Sarah M. Auclair, Debra A. Kendall, Donald Oliver, Monika Musial-Siwek, Julia P. Moses
Publikováno v:
Biochemistry. 49:782-792
Identification of the signal peptide-binding domain within SecA ATPase is an important goal for understanding the molecular basis of SecA preprotein recognition as well as elucidating the chemo-mechanical cycle of this nanomotor during protein transl
Publikováno v:
Journal of Bacteriology. 190:7302-7307
The SecA nanomotor promotes protein translocation in eubacteria by binding both protein cargo and the protein-conducting channel and by undergoing ATP-driven conformation cycles that drive this process. There are conflicting reports about whether Sec