Evidence map›Paper›PMID 17367712›Full record

ArticleMethods (San Diego, Calif.)2007

NMR of membrane proteins in micelles and bilayers: the FXYD family proteins.

Carla M Franzin, Xiao-Min Gong, Khang Thai, Jinghua Yu, Francesca M Marassi

Abstract read
In one paragraph

Article in Methods (San Diego, Calif.), 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
4.0field-weighted citation impact, top 6% of its field
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

17 citing papers in PubMed, 41 citations in OpenAlex.

  1. Review
  2. Review
  3. Na+/Ca2+ exchange and Na+/K+-ATPase in the heart.The Journal of physiology · 2015
    Review
  4. Article
  5. Article
  6. Phospholemman: a novel cardiac stress protein.Clinical and translational science · 2010
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Structural similarity of a membrane protein in micelles and membranes.Journal of the American Chemical Society · 2007
    Article
  17. 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

5 authors at 1 institution in 1 country.

Carla M FranzinThe Burnham Institute, 10901 North Torrey Pines Road, La Jolla, CA 92037, USA.
Xiao-Min Gong
Khang Thai
Jinghua Yu
Francesca M Marassi
Sanford Burnham Prebys Medical Discovery Institute · US

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
Structure of Mammary Tumor Mat8 and the FXYD proteinsR01CA082864 · NCI · BURNHAM INSTITUTE FOR MEDICAL RESEARCH · PI MARASSI, FRANCESCA M · 2001 to 2005
$1.5M
Structures of membrane-bound Bcl-2 apoptotic proteinsR01GM065374 · NIGMS · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI MARASSI, FRANCESCA M · 2005 to 2009
$1.3M
NCI NIH HHS CA082864NCI NIH HHS P30 CA030199NCI NIH HHS R01 CA082864NIBIB NIH HHS P41 EB002031NIGMS NIH HHS GM065374NIGMS NIH HHS R01 GM065374
6 · The paper itself

Abstract

Determining the atomic resolution structures of membrane proteins is of particular interest in contemporary structural biology. Helical membrane proteins constitute one-third of the expressed proteins encoded in a genome, many drugs have membrane-bound proteins as their receptors, and mutations in membrane proteins result in human diseases. Although integral membrane proteins provide daunting technical challenges for all methods of protein structure determination, nuclear magnetic resonance (NMR) spectroscopy can be an extremely versatile and powerful method for determining their structures and characterizing their dynamics, in lipid environments that closely mimic the cell membranes. Once milligram amounts of isotopically labeled protein are expressed and purified, micelle samples can be prepared for solution NMR analysis, and lipid bilayer samples can be prepared for solid-state NMR analysis. The two approaches are complementary and can provide detailed structural and dynamic information. This paper describes the steps for membrane protein structure determination using solution and solid-state NMR. The methods for protein expression and purification, sample preparation and NMR experiments are described and illustrated with examples from the FXYD proteins, a family of regulatory subunits of the Na,K-ATPase.

Indexed as

MicellesAmino Acid SequenceCell Line, TransformedDetergentsGene ExpressionIntracellular Signaling Peptides and ProteinsLipid BilayersMembrane ProteinsMolecular Sequence DataNeoplasm ProteinsNitrogen IsotopesNuclear Magnetic Resonance, BiomolecularPhosphoproteinsPhosphorus IsotopesPlasmidsPotassium ChannelsDetergentsFXYD2 protein, humanFxyd3 protein, mouseFxyd4 protein, ratIntracellular Signaling Peptides and ProteinsLipid BilayersMembrane ProteinsMicellesNeoplasm ProteinsNitrogen IsotopesphospholemmanPhosphoproteinsPhosphorus IsotopesPotassium ChannelsSodium-Potassium-Exchanging ATPase

Identifiers

PMID17367712
PMCPMC2920895
OpenAlexW1974633473

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.