Evidence map›Paper›PMID 19917234›Full record

ArticleBiophysical journal2009

Configuration of PKCalpha-C2 domain bound to mixed SOPC/SOPS lipid monolayers.

Chiu-Hao Chen, Sárka Málková, Sai Venkatesh Pingali, Fei Long, Shekhar Garde, Wonhwa Cho, Mark L Schlossman

Abstract read
In one paragraph

Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. CaThe journal of physical chemistry. B · 2025
    Article
  2. Review
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  5. Article
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  7. Molecular mechanism for differential recognition of membrane phosphatidylserine by the immune regulatory receptor Tim4.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
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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

7 authors.

Chiu-Hao ChenDepartment of Physics, University of Illinois at Chicago, Chicago, Illinois, USA.
Sárka Málková
Sai Venkatesh Pingali
Fei Long
Shekhar Garde
Wonhwa Cho
Mark L Schlossman

Funding

Membrane Targeting by Phosphoinositide-Binding ProteinsR01GM068849 · NIGMS · UNIVERSITY OF ILLINOIS AT CHICAGO · PI CHO, WONHWA · 2003 to 2015
$3.9M
Studies of Diacylglycerol-Binding ProteinsR01GM076581 · NIGMS · UNIVERSITY OF ILLINOIS AT CHICAGO · PI CHO, WONHWA · 2006 to 2009
$1.1M
NIGMS NIH HHS GM68849NIGMS NIH HHS GM76581NIGMS NIH HHS R01 GM068849NIGMS NIH HHS R01 GM076581
6 · The paper itself

Abstract

X-ray reflectivity measurements are used to determine the configuration of the C2 domain of protein kinase Calpha (PKCalpha-C2) bound to a lipid monolayer of a 7:3 mixture of 1-stearoyl-2-oleoyl-sn-glycero-3-phosphocholine and 1-stearoyl-2-oleoyl-sn-glycero-3-phosphoserine supported on a buffered aqueous solution. The reflectivity is analyzed in terms of the known crystallographic structure of PKCalpha-C2 and a slab model representation of the lipid layer. The configuration of lipid-bound PKCalpha-C2 is described by two angles that define its orientation, theta = 35 degrees +/- 10 degrees and phi =210 degrees +/- 30 degrees, and a penetration depth (=7.5 +/- 2 A) into the lipid layer. In this structure, the beta-sheets of PKCalpha-C2 are nearly perpendicular to the lipid layer and the domain penetrates into the headgroup region of the lipid layer, but not into the tailgroup region. This configuration of PKCalpha-C2 determined by our x-ray reflectivity is consistent with many previous findings, particularly mutational studies, and also provides what we believe is new molecular insight into the mechanism of PKCalpha enzyme activation. Our analysis method, which allows us to test all possible protein orientations, shows that our data cannot be explained by a protein that is orientated parallel to the membrane, as suggested by earlier work.

Indexed as

Models, ChemicalModels, MolecularPhosphatidylcholinesPhosphatidylserinesPressureProtein BindingProtein ConformationProtein Kinase C-alphaProtein Structure, SecondaryUnilamellar LiposomesWaterX-Rays1-stearoyl-2-oleoyl-sn-glycero-3-phosphocholinePhosphatidylcholinesPhosphatidylserinesProtein Kinase C-alphastearoyl-oleoyl-phosphatidylserineUnilamellar LiposomesWater

Identifiers

PMID19917234
PMCPMC2776280

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.