Evidence map›Paper›PMID 20576615›Full record

ArticleThe Journal of biological chemistry2010

Defining specific lipid binding sites for a peripheral membrane protein in situ using subtesla field-cycling NMR.

Mingming Pu, Andrew Orr, Alfred G Redfield, Mary F Roberts

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

25 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
  2. Cooperative Membrane Binding of HIV-1 Matrix Proteins.The journal of physical chemistry. B · 2024
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. High ResolutionFrontiers in molecular biosciences · 2022
    Review
  9. Article
  10. Article
  11. Article
  12. Structural features and lipid binding domain of tubulin on biomimetic mitochondrial membranes.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  13. A Structural Model for Vinculin Insertion into PIPStructure (London, England : 1993) · 2017
    Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. 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

4 authors at 2 institutions in 1 country.

Mingming PuDepartment of Chemistry, Boston College, Chestnut Hill, Massachusetts 02465.
Andrew OrrDepartment of Chemistry, Boston College, Chestnut Hill, Massachusetts 02465.
Alfred G RedfieldDepartment of Biochemistry, Brandeis University, Waltham, Massachusetts 024547.
Mary F RobertsDepartment of Chemistry, Boston College, Chestnut Hill, Massachusetts 02465. Electronic address: mary.roberts@bc.edu.
Boston College · USBrandeis University · US

Funding

ACTIVATION OF PI-SPECIFIC PHOSPHOLIPASE C ENZYMESR01GM060418 · NIGMS · BOSTON COLLEGE · PI ROBERTS, MARY FEDARKO · 2000 to 2013
$3.1M
Applications of Field-Cycling NMR to Studies of Biomolecules.R01GM077974 · NIGMS · BRANDEIS UNIVERSITY · PI REDFIELD, ALFRED GUILLOU · 2005 to 2008
$596k
NIGMS NIH HHS GM077974NIGMS NIH HHS GM60418NIGMS NIH HHS R01 GM060418NIGMS NIH HHS R01 GM077974
6 · The paper itself

Abstract

Despite the profound physiological consequences associated with peripheral membrane protein localization, only a rudimentary understanding of the interactions of proteins with membrane surfaces exists because these questions are inaccessible by commonly used structural techniques. Here, we combine high resolution field-cycling (31)P NMR relaxation methods with spin-labeled proteins to delineate specific interactions of a bacterial phospholipase C with phospholipid vesicles. Unexpectedly, discrete binding sites for both a substrate analogue and a different phospholipid (phosphatidylcholine) known to activate the enzyme are observed. The lifetimes for the occupation of these sites (when the protein is anchored transiently to the membrane) are >1-2 micros (but <1 ms), which represents the first estimate of an off-rate for a lipid dissociating from a specific site on the protein and returning to the bilayer. Furthermore, analyses of the spin-label induced NMR relaxation corroborates the presence of a discrete tyrosine-rich phosphatidylcholine binding site whose location is consistent with that suggested by modeling studies. The methodology illustrated here may be extended to a wide range of peripheral membrane proteins.

Indexed as

Models, MolecularBacillus thuringiensisBacterial ProteinsBinding SitesLipid BilayersNuclear Magnetic Resonance, BiomolecularType C PhospholipasesBacterial ProteinsLipid BilayersType C Phospholipases

Identifiers

PMID20576615
PMCPMC2930691
OpenAlexW2028653672

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.