ArticleBiochemistry2011
Lactose permease and the alternating access mechanism.
Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
72 citing papers in PubMed, 109 citations in OpenAlex.
- Article
- Allosteric effects of the coupling cation in melibiose transporter MelB.bioRxiv : the preprint server for biology · 2025Article
- Single-Molecule Imaging of Integral Membrane Protein Dynamics and Function.Annual review of biophysics · 2024Review
- The culmination of multidrug-resistant efflux pumps vs. meager antibiotic arsenal era: Urgent need for an improved new generation of EPIs.Frontiers in microbiology · 2023Review
- ID-Checker Technology for the Highly Selective Macroscale Delivery of Anticancer Agents to the Cancer Cells.Journal of medicinal chemistry · 2022Article
- Structure and mechanism of membrane transporters.Scientific reports · 2022Article
- Structural snapshots of human PepT1 and PepT2 reveal mechanistic insights into substrate and drug transport across epithelial membranes.Science advances · 2021Article
- Cooperative binding ensures the obligatory melibiose/Na+ cotransport in MelB.The Journal of general physiology · 2021Article
- Article
- A selective transmembrane recognition mechanism by a membrane-anchored ubiquitin ligase adaptor.The Journal of cell biology · 2021Article
- AspThe Journal of biological chemistry · 2020Article
- The proton electrochemical gradient induces a kinetic asymmetry in the symport cycle of LacY.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- It takes two to tango: The dance of the permease.The Journal of general physiology · 2019Review
- Conformational Studies of Glucose Transporter 1 (GLUT1) as an Anticancer Drug Target.Molecules (Basel, Switzerland) · 2019Article
- Mentors: Ron Kaback.The Journal of general physiology · 2019Article
- Engineered occluded apo-intermediate of LacY.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Structural elements required for coupling ion and substrate transport in the neurotransmitter transporter homolog LeuT.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Oversized galactosides as a probe for conformational dynamics in LacY.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- A partially-open inward-facing intermediate conformation of LeuT is associated with NaNature communications · 2018Article
- Ligand-induced conformational dynamics of theProceedings of the National Academy of Sciences of the United States of America · 2017Article
12 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Crystal structures of the lactose permease of Escherichia coli (LacY) reveal 12, mostly irregular transmembrane α-helices surrounding a large cavity open to the cytoplasm and a tightly sealed periplasmic side (inward-facing conformation) with the sugar-binding site at the apex of the cavity and inaccessible from the periplasm. However, LacY is highly dynamic, and binding of a galactopyranoside causes closing of the inward-facing cavity with opening of a complementary outward-facing cavity. Therefore, the coupled, electrogenic translocation of a sugar and a proton across the cytoplasmic membrane via LacY very likely involves a global conformational change that allows alternating access of sugar- and H(+)-binding sites to either side of the membrane. Here the various biochemical and biophysical approaches that provide strong support for the alternating access mechanism are reviewed. Evidence is also presented indicating that opening of the periplasmic cavity is probably the limiting step for binding and perhaps transport.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.