Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Meghan Whitney Franklin"'
Autor:
Ali Bootwala, Hyun Hwan An, Meghan Whitney Franklin, Benjamin J. Manning, Lucy Y. Xu, Shruti Panchal, Joseph D. Garlick, Reshica Baral, Michael E. Hudson, Gevorg Grigoryan, Mark A. Murakami, Kristen Hopson, Daniel S. Leventhal
Publikováno v:
Frontiers in Immunology, Vol 13 (2022)
The optimal use of many biotherapeutics is restricted by Anti-drug antibodies (ADAs) and hypersensitivity responses which can affect potency and ability to administer a treatment. Here we demonstrate that Re-surfacing can be utilized as a generalizab
Externí odkaz:
https://doaj.org/article/4a3b4c9302ed43f8bcb616f28001d45c
Autor:
Meghan Whitney Franklin, Sergey Nepomnyachyi, Ryan Feehan, Nir Ben-Tal, Rachel Kolodny, Joanna SG Slusky
Publikováno v:
eLife, Vol 7 (2018)
Outer membrane proteins (OMPs) are the proteins in the surface of Gram-negative bacteria. These proteins have diverse functions but a single topology: the β-barrel. Sequence analysis has suggested that this common fold is a β-hairpin repeat protein
Externí odkaz:
https://doaj.org/article/69259f8ebb4d4194a9db6262707ed056
Outer membrane proteins are all beta barrels and these barrels have a variety of well-documented loop conformations. Here we test the effect of three different loop types on outer membrane protein A (OmpA) folding. We designed twelve 5-residue loops
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a8a4da4d03474e0524dac9c09eb6ed38
https://doi.org/10.1101/2020.10.08.331546
https://doi.org/10.1101/2020.10.08.331546
Autor:
Sergey Nepomnyachyi, Joanna S.G. Slusky, Ryan Feehan, Nir Ben-Tal, Rachel Kolodny, Meghan Whitney Franklin
Publikováno v:
eLife, Vol 7 (2018)
eLife
eLife
Outer membrane proteins (OMPs) are the proteins in the surface of Gram-negative bacteria. These proteins have diverse functions but a single topology: the β-barrel. Sequence analysis has suggested that this common fold is a β-hairpin repeat protein
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f54778ee0c09856473f82213443ac4ec
https://elifesciences.org/articles/40308
https://elifesciences.org/articles/40308
Autor:
Nir Ben-Tal, Ryan Feehan, Joanna S.G. Slusky, Sergey Nepomnyaciy, Meghan Whitney Franklin, Rachel Kolodny
Outer membrane beta barrels (OMBBs) are the proteins on the surface of Gram negative bacteria. These proteins have diverse functions but only a single topology, the beta barrel. It has been suggested that this common fold is a repeat protein with the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ae36eca502e609fde69c1660226e2644
https://doi.org/10.1101/309393
https://doi.org/10.1101/309393
I.AbstractAs a structural class, tight turns can control molecular recognition, enzymatic activity, and nucleation of folding. They have been extensively characterized in soluble proteins but have not been characterized in outer membrane proteins (OM
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1ebae2a74efaa0e4292d23809b734a1b
Autor:
Nir Ben-Tal, Rachel Kolodny, Meghan Whitney Franklin, Joanna S.G. Slusky, Sergey Nepomnyachiy, Ryan Feehan
Publikováno v:
Structure (London, England : 1993). 26(9)
Summary There are around 100 varieties of outer membrane proteins in each Gram-negative bacteria. All of these proteins have the same fold—an up-down β-barrel. It has been suggested that all membrane β-barrels excluding lysins are homologous. Her
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7c29fd249ada1e6d8174cb2b476e1708
https://pubmed.ncbi.nlm.nih.gov/30057025
https://pubmed.ncbi.nlm.nih.gov/30057025
Autor:
Joanna S.G. Slusky, Ryan Feehan, Rachel Kolodny, Meghan Whitney Franklin, Nir Ben-Tal, Sergey Nepomnyachiy
SummaryThere are around 100 types of integral outer membrane proteins in each Gram negative bacteria. All of these proteins have the same fold—an up-down β-barrel. It has been suggested that all membrane β-barrels other than lysins are homologous
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::969493aa65dd06043eae184d31f034a4
https://doi.org/10.1101/268029
https://doi.org/10.1101/268029