Cryo-EM structure of PepT2 reveals structural basis for proton-coupled peptide and prodrug transport in mammals
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Joanne L. Parker; Justin C. Deme; Zhiyi Wu; Gabriel Kuteyi; Jiandong Huo; Raymond J. Owens; Philip C. Biggin; +2 Authors
Joanne L. Parker; Justin C. Deme; Zhiyi Wu; Gabriel Kuteyi; Jiandong Huo; Raymond J. Owens; Philip C. Biggin; Susan M. Lea; Simon Newstead;
Cryo-EM structure of PepT2 reveals structural basis for proton-coupled peptide and prodrug transport in mammals
Structure of PepT2 reveals binding model for peptide recognition and enables a more rationalized approach to prodrug design.
- National Cancer Institute United States
- Franklin Institute United States
- Research Complex at Harwell United Kingdom
- University of Oxford United Kingdom
- Center for Cancer Research United States
Mammals, Symporters, Cryoelectron Microscopy, Membrane Transport Proteins, Peptide Transporter 1, Rats, Animals, Prodrugs, Protons, Peptides, Research Articles
Mammals, Symporters, Cryoelectron Microscopy, Membrane Transport Proteins, Peptide Transporter 1, Rats, Animals, Prodrugs, Protons, Peptides, Research Articles
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Citations provided by BIP!
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
Citations provided by BIP!popularityPopularity provided by BIP!
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
Popularity provided by BIP! 47
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