ArticleMagnetic resonance in chemistry : MRC2004
Structural studies of apoptosis and ion transport regulatory proteins in membranes.
Article in Magnetic resonance in chemistry : MRC, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 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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Who cites it
21 citing papers in PubMed, 40 citations in OpenAlex.
- Conformational States of the Cytoprotective Protein Bcl-xL.Biophysical journal · 2020Article
- Reconstitution and Characterization of BCL-2 Family Proteins in Lipid Bilayer Nanodiscs.Methods in molecular biology (Clifton, N.J.) · 2019Article
- Characterization of the membrane-inserted C-terminus of cytoprotective BCL-XL.Protein expression and purification · 2016Article
- Conformation of BCL-XL upon Membrane Integration.Journal of molecular biology · 2015Article
- The rheostat in the membrane: BCL-2 family proteins and apoptosis.Cell death and differentiation · 2014Review
- Comparison of membrane insertion pathways of the apoptotic regulator Bcl-xL and the diphtheria toxin translocation domain.Biochemistry · 2013Article
- Acidic pH promotes oligomerization and membrane insertion of the BclXL apoptotic repressor.Archives of biochemistry and biophysics · 2012Article
- Ligand binding and membrane insertion compete with oligomerization of the BclXL apoptotic repressor.Journal of molecular biology · 2012Article
- Active fragments from pro- and antiapoptotic BCL-2 proteins have distinct membrane behavior reflecting their functional divergence.PloS one · 2010Article
- Mapping the interaction of pro-apoptotic tBID with pro-survival BCL-XL.Biochemistry · 2009Article
- Activation of Bax by joint action of tBid and mitochondrial outer membrane: Monte Carlo simulations.European biophysics journal : EBJ · 2009Article
- Monte Carlo simulations of tBid association with the mitochondrial outer membrane.European biophysics journal : EBJ · 2007Article
- Helix orientations in membrane-associated Bcl-X(L) determined by 15N-solid-state NMR spectroscopy.European biophysics journal : EBJ · 2007Article
- NMR structural studies of the bacterial outer membrane protein OmpX in oriented lipid bilayer membranes.Biochimica et biophysica acta · 2007Article
- NMR structural investigation of the mitochondrial outer membrane protein VDAC and its interaction with antiapoptotic Bcl-xL.Biochemistry · 2007Article
- The N-terminal domain of Bcl-xL reversibly binds membranes in a pH-dependent manner.Biochemistry · 2006Article
- Evidence that membrane insertion of the cytosolic domain of Bcl-xL is governed by an electrostatic mechanism.Journal of molecular biology · 2006Article
- Secondary structure, orientation, and oligomerization of phospholemman, a cardiac transmembrane protein.Protein science : a publication of the Protein Society · 2006Article
- Association of renal Na,K-ATPase alpha-subunit with the beta- and gamma-subunits based on cryoelectron microscopy.The Journal of membrane biology · 2006Article
- Structure determination of membrane proteins by NMR spectroscopy.Chemical reviews · 2004Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Solid-state NMR spectroscopy is being used to determine the structures of membrane proteins involved in the regulation of apoptosis and ion transport. The Bcl-2 family includes pro- and anti-apoptotic proteins that play a major regulatory role in mitochondrion-dependent apoptosis or programmed cell death. The NMR data obtained for (15)N-labeled anti-apoptotic Bcl-xL in lipid bilayers are consistent with membrane association through insertion of the two central hydrophobic alpha-helices that are also required for channel formation and cytoprotective activity. The FXYD family proteins regulate ion flux across membranes, through interaction with the Na(+), K(+)-ATPase, in tissues that perform fluid and solute transport or that are electrically excitable. We have expressed and purified three FXYD family members, Mat8 (mammary tumor protein), CHIF (channel-inducing factor) and PLM (phospholemman), for structure determination by NMR in lipids. The solid-state NMR spectra of Bcl-2 and FXYD proteins, in uniaxially oriented lipid bilayers, give the first view of their membrane-associated architectures.
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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.