ReviewBiochimica et biophysica acta. Molecular and cell biology of lipids2017
Structural basis for catalysis at the membrane-water interface.
Review in Biochimica et biophysica acta. Molecular and cell biology of lipids, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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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.
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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.
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Who cites it
8 citing papers in PubMed, 12 citations in OpenAlex.
- Expression and Purification of Integral Membrane Enzymes for Functional and Structural Studies.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Highly flexible cell membranes are the key to efficient production of lipophilic compounds.Journal of lipid research · 2024Review
- The role of water in reactions catalysed by hydrolases under conditions of molecular crowding.Biophysical reviews · 2023Review
- Predicting protein-membrane interfaces of peripheral membrane proteins using ensemble machine learning.Briefings in bioinformatics · 2022Article
- Molecular ruler mechanism and interfacial catalysis of the integral membrane acyltransferase PatA.Science advances · 2021Article
- The phosphatidylglycerol phosphate synthase PgsA utilizes a trifurcated amphipathic cavity for catalysis at the membrane-cytosol interface.Current research in structural biology · 2021Article
- Structural and mechanistic themes in glycoconjugate biosynthesis at membrane interfaces.Current opinion in structural biology · 2019Review
- Membrane properties that shape the evolution of membrane enzymes.Current opinion in structural biology · 2018Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The membrane-water interface forms a uniquely heterogeneous and geometrically constrained environment for enzymatic catalysis. Integral membrane enzymes sample three environments - the uniformly hydrophobic interior of the membrane, the aqueous extramembrane region, and the fuzzy, amphipathic interfacial region formed by the tightly packed headgroups of the components of the lipid bilayer. Depending on the nature of the substrates and the location of the site of chemical modification, catalysis may occur in each of these environments. The availability of structural information for alpha-helical enzyme families from each of these classes, as well as several beta-barrel enzymes from the bacterial outer membrane, has allowed us to review here the different ways in which each enzyme fold has adapted to the nature of the substrates, products, and the unique environment of the membrane. Our focus here is on enzymes that process lipidic substrates. This article is part of a Special Issue entitled: Bacterial Lipids edited by Russell E. Bishop.
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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 OpenQuestion graph.