Evidence map›Paper›PMID 30536010›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2019

Reconstitution and Characterization of BCL-2 Family Proteins in Lipid Bilayer Nanodiscs.

Yong Yao, Francesca M Marassi

Abstract read
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

6 citing papers in PubMed.

  1. Article
  2. Lipids modulate the BH3-independent membrane targeting and activation of BAX and Bcl-xL.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  3. Article
  4. Article
  5. Review
  6. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

Yong YaoSanford Burnham Prebys Medical Discovery Institute, La Jolla, CA, USA.
Francesca M MarassiSanford Burnham Prebys Medical Discovery Institute, La Jolla, CA, USA. fmarassi@sbp.edu.

Funding

Tumor Microenvironment and Cancer ImmunologyP30CA030199 · NCI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI Michael Jackson · 1985 to 2026
$107.2M
RESOURCE FOR SOLID STATE NMR OF PROTEINSP41EB002031 · NIBIB · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI OPELLA, STANLEY J · 2003 to 2018
$16.3M
Membrane Protein Effectors of Pathogen Interactions With HostR35GM118186 · NIGMS · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI Francesca M Marassi · 2016 to 2026
$8.5M
Molecular mechanism of BCL2-dependent apoptosisR01CA179087 · NCI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI HANEIN, DORIT, MARASSI, FRANCESCA M · 2014 to 2018
$3.6M
Host recognition by pathogenic yersiniaeR01GM100265 · NIGMS · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI MARASSI, FRANCESCA M · 2012 to 2015
$1.7M
NCI NIH HHS P30 CA030199NCI NIH HHS R01 CA179087NIBIB NIH HHS P41 EB002031NIGMS NIH HHS R01 GM100265NIGMS NIH HHS R35 GM118186
6 · The paper itself

Abstract

The BCL-2 family proteins are key regulators of programmed cell death or apoptosis, and represent important targets for the development of anticancer drugs. Because their functions are intimately connected with intracellular membranes, it is important to perform structural and activity studies in precisely characterized samples that include phospholipids and capture the features of the native physiological environment as closely as possible. NMR studies and activity assays based on lipid bilayer nanodiscs are ideally suited for this purpose: they enable the conformations and interactions of these proteins to be probed at atomic resolution in their membrane-associated states. Here we describe detailed protocols for generating the protein components and the reconstituted nanodisc samples suitable for NMR studies and functional assays. The protocols focus on the BCL-2 family protein BCL-XL, a dominant inhibitor of programmed cell death and a major anticancer drug target. The protocols are relatively straightforward. Provided care is taken to ensure protein integrity and sample homogeneity, BCL-XL can be readily reconstituted in nanodiscs, with its hydrophobic C-terminal tail anchored through the nanodisc lipid bilayer, and its folded N-terminal head and ligand binding pocket exposed to the aqueous solution. We anticipate that BCL-2 samples prepared with these protocols will advance structural and mechanistic studies for this important protein family.

Indexed as

Amino Acid SequenceAntineoplastic Agentsbcl-X ProteinCell DeathHumansHydrophobic and Hydrophilic InteractionsLipid BilayersMembrane ProteinsNanostructuresPhospholipidsProto-Oncogene Proteins c-bcl-2Antineoplastic AgentsBCL2 protein, humanbcl-X ProteinLipid BilayersMembrane ProteinsPhospholipidsProto-Oncogene Proteins c-bcl-2ApoptosisBCL-2MembraneNanodiscNMRStructure

Identifiers

PMID30536010
PMCPMC6599400

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Registered trials

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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.