J
James H. Naismith
Researcher at Franklin Institute
Publications - 315
Citations - 18866
James H. Naismith is an academic researcher from Franklin Institute. The author has contributed to research in topics: Bacterial outer membrane & Periplasmic space. The author has an hindex of 70, co-authored 304 publications receiving 16124 citations. Previous affiliations of James H. Naismith include University of Edinburgh & Rutherford Appleton Laboratory.
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Journal ArticleDOI
An efficient one-step site-directed deletion, insertion, single and multiple-site plasmid mutagenesis protocol.
Huanting Liu,James H. Naismith +1 more
TL;DR: This modified protocol used a new primer design that promoted primer-template annealing by eliminating primer dimerization and also permitted the newly synthesized DNA to be used as the template in subsequent amplification cycles, significantly increased the efficiency of single mutation and also allowed facile large single insertions, deletions/truncations and multiple mutations in a single experiment.
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TNF alpha and the TNF receptor superfamily: structure-function relationship(s).
TL;DR: The structure/function relationships of the TNFα and the T NF receptor superfamily are reviewed and insights as to how structural features play a role in the pleiotropic effects of TNF α are discussed.
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Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9
Michael H. Tatham,Ellis Jaffray,Owen A. Vaughan,Joana M. P. Desterro,Catherine H. Botting,James H. Naismith,Ronald T. Hay +6 more
TL;DR: The ability to form polymeric chains is not shared by SUMO-1, and although all SUMO species use the same conjugation machinery, modification by SUMo-1 andsumO-2/-3 may have distinct functional consequences.
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Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis
TL;DR: The crystal structure of the dimeric RING domain of rat RNF4 in complex with E2 (UbcH5A) linked by an isopeptide bond to ubiquitin is reported, primed for catalysis as it can deprotonate the incoming substrate lysine residue and stabilize the consequent tetrahedral transition-state intermediate.
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Neutralizing nanobodies bind SARS-CoV-2 spike RBD and block interaction with ACE2.
J. Huo,J. Huo,A. Le Bas,A. Le Bas,Reinis R. Ruza,Duyvesteyn Hme.,H. Mikolajek,Tomas Malinauskas,Tiong Kit Tan,Pramila Rijal,Pramila Rijal,Maud Dumoux,Philip N. Ward,Philip N. Ward,Jingshan Ren,D. Zhou,Peter J. Harrison,Peter J. Harrison,Miriam Weckener,Daniel K. Clare,V K Vogirala,Julika Radecke,Lucile Moynié,Yuguang Zhao,Javier Gilbert-Jaramillo,Michael L. Knight,Julia A. Tree,Karen R. Buttigieg,Naomi Coombes,Michael J. Elmore,Miles W. Carroll,Loic Carrique,Shah Pnm.,William James,Alain Townsend,Alain Townsend,David I. Stuart,Raymond J. Owens,Raymond J. Owens,James H. Naismith,James H. Naismith +40 more
TL;DR: Two nanobodies that bind SARS-CoV-2 spike RBD are shown to block interaction with receptor ACE2 and thus neutralize the virus, and have an additive effect with antibody CR3022.