Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Anne A. Ollis"'
Publikováno v:
Frontiers in Microbiology, Vol 2 (2011)
A complex of ExbB, ExbD, and TonB transduces cytoplasmic membrane (CM) proton motive force (pmf) to outer membrane (OM) transporters so that large, scarce, and important nutrients can be released into the periplasmic space for subsequent transport ac
Externí odkaz:
https://doaj.org/article/099e4d3b7c47487ea7ff7d0346eedf2f
Autor:
Gheorghe-Doru Roiban, Douglas E. Fuerst, Katherine Joyce Honicker, Anne A. Ollis, Christopher M. MacDermaid, Jonathan Latham
Publikováno v:
Applied Biocatalysis
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cd7ab63607ca7713fa5a3e9e5defc68f
https://doi.org/10.1002/9781119487043.ch1
https://doi.org/10.1002/9781119487043.ch1
Autor:
Sandy S. Chang, Joseph Hosford, Mahesh J. Sanganee, Anne A. Ollis, Christopher M. MacDermaid, Leigh Anne F. Ihnken, Murray J. B. Brown, Douglas E. Fuerst, Jonathan Latham, Diluar Khan, Markus Schober, Gheorghe-Doru Roiban
Publikováno v:
Nature Catalysis. 2:909-915
Imine reductases catalyse the reductive amination of aldehydes or ketones with amines to produce chiral amines—a key transformation in the preparation of fine chemicals and active pharmaceutical ingredients. Although significant progress has been r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b1c5679819baaf967e2370855b4545f2
https://doi.org/10.1038/s41929-019-0341-4
https://doi.org/10.1038/s41929-019-0341-4
Autor:
Anne A. Ollis, Eda Çelik, David F. Smith, Yi Lasanajak, Adam C. Fisher, Matthew P. DeLisa, Göksu Gür
Publikováno v:
Biotechnology Journal. 10:199-209
Glycosylation is a widespread post-translational modification that plays important roles in health and disease. As glycan sequence and structure are not directly coded into the genome, our understanding of glycans and their functions in biological sy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fba7108f50bedb7326b0681003a47d0e
https://doi.org/10.1002/biot.201400354
https://doi.org/10.1002/biot.201400354
The ExbD Periplasmic Domain Contains Distinct Functional Regions for Two Stages in TonB Energization
Publikováno v:
Journal of Bacteriology. 194:3069-3077
The TonB system of Gram-negative bacteria energizes the active transport of diverse nutrients through high-affinity TonB-gated outer membrane transporters using energy derived from the cytoplasmic membrane proton motive force. Cytoplasmic membrane pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b3ee02f5c57ca85c4ca21480d12fcf38
https://doi.org/10.1128/jb.00015-12
https://doi.org/10.1128/jb.00015-12
Autor:
Anne A. Ollis, Kathleen Postle
Publikováno v:
Journal of Molecular Biology. 415:237-247
Cytoplasmic membrane proteins ExbB and ExbD of the Escherichia coli TonB system couple cytoplasmic membrane protonmotive force (pmf) to TonB. TonB transmits this energy to high-affinity outer membrane active transporters. ExbD is proposed to catalyze
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ee831947ada613f451fa57dd73e8ae05
https://doi.org/10.1016/j.jmb.2011.11.005
https://doi.org/10.1016/j.jmb.2011.11.005
Autor:
Thapakorn Jaroentomeechai, Emily C. Perregaux, Sheng Zhang, Anne A. Ollis, Matthew P. DeLisa, Yi Chai, Aravind Natarajan, Cassandra Guarino, Jessica C. Scillieri Smith
Publikováno v:
Scientific Reports
The central enzyme in the Campylobacter jejuni asparagine-linked glycosylation pathway is the oligosaccharyltransferase (OST), PglB, which transfers preassembled glycans to specific asparagine residues in target proteins. While C. jejuni PglB (CjPglB
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c6e2ccd61fcc811fd27166480a291836
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 1321
The Campylobacter jejuni protein glycosylation locus (pgl) encodes enzymes for asparagine-linked (N-linked) glycosylation and serves as the prototype for N-glycosylation in bacteria. This pathway has been functionally transferred into Escherichia col
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::7eda4ef3aeb18200ef6386203a3611e3
https://pubmed.ncbi.nlm.nih.gov/26082213
https://pubmed.ncbi.nlm.nih.gov/26082213
Publikováno v:
Glyco-Engineering ISBN: 9781493927593
The Campylobacter jejuni protein glycosylation locus (pgl) encodes enzymes for asparagine-linked (N-linked) glycosylation and serves as the prototype for N-glycosylation in bacteria. This pathway has been functionally transferred into Escherichia col
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::527524874c96ed97db82edb241057ce2
https://doi.org/10.1007/978-1-4939-2760-9_3
https://doi.org/10.1007/978-1-4939-2760-9_3
Publikováno v:
Nature chemical biology. 10(10)
The Campylobacter jejuni protein glycosylation locus (pgl) encodes machinery for asparagine-linked (N-linked) glycosylation and serves as the archetype for bacterial N-glycosylation. This machinery has been functionally transferred into Escherichia c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::de03a36936bf25a2591dba8c84275f93
https://pubmed.ncbi.nlm.nih.gov/25129029
https://pubmed.ncbi.nlm.nih.gov/25129029