ArticleProceedings of the National Academy of Sciences of the United States of America2020
Structural cavities are critical to balancing stability and activity of a membrane-integral enzyme.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
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Who cites it
17 citing papers in PubMed.
- Conformational Flexibility of Transmembrane Helices: How it Works and Where it Matters.Chemical reviews · 2026Review
- The lipid bilayer strengthens the cooperative network of membrane proteins.Science advances · 2025Article
- Article
- Article
- Steric trapping strategy for studying the folding of helical membrane proteins.Methods (San Diego, Calif.) · 2024Review
- Statistical Analysis of the Role of Cavity Flexibility in Thermostability of Proteins.Polymers · 2024Article
- Stretch-activated ion channel TMEM63B associates with developmental and epileptic encephalopathies and progressive neurodegeneration.American journal of human genetics · 2023Article
- Redesign of γ-glutamyl transpeptidase from Bacillus subtilis for high-level production of L-theanine by cavity topology engineering.Applied microbiology and biotechnology · 2023Article
- CaviDB: a database of cavities and their features in the structural and conformational space of proteins.Database : the journal of biological databases and curation · 2023Article
- Inside Out Computational Redesign of Cavities for Improving Thermostability and Catalytic Activity ofApplied and environmental microbiology · 2023Article
- Mutation in the D1 domain of CD4 receptor modulates the binding affinity to HIV-1 gp120.RSC advances · 2023Article
- In silico comparative structural and compositional analysis of glycoproteins of RSV to study the nature of stability and transmissibility of RSV A.Systems microbiology and biomanufacturing · 2023Article
- How physical forces drive the process of helical membrane protein folding.EMBO reports · 2022Review
- Dawn of a New Era for Membrane Protein Design.Biodesign research · 2022Review
- Article
- Insights into the Role of Membrane Lipids in the Structure, Function and Regulation of Integral Membrane Proteins.International journal of molecular sciences · 2021Review
- Eugene P. Kennedy's Legacy: Defining Bacterial Phospholipid Pathways and Function.Frontiers in molecular biosciences · 2021Review
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
Packing interaction is a critical driving force in the folding of helical membrane proteins. Despite the importance, packing defects (i.e., cavities including voids, pockets, and pores) are prevalent in membrane-integral enzymes, channels, transporters, and receptors, playing essential roles in function. Then, a question arises regarding how the two competing requirements, packing for stability vs. cavities for function, are reconciled in membrane protein structures. Here, using the intramembrane protease GlpG of
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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 Socratic graph.