Evidence map›Paper›PMID 17001006›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2006

Prediction of protein orientation upon immobilization on biological and nonbiological surfaces.

AmirAli H Talasaz, Mohsen Nemat-Gorgani, Yang Liu, Patrik Ståhl, Robert W Dutton, Mostafa Ronaghi, Ronald W Davis

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. 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
4.9field-weighted citation impact, top 5% 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, 68 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Differences in Charge Distribution inInternational journal of molecular sciences · 2022
    Article
  5. Article
  6. Review
  7. From Protein Features to Sensing Surfaces.Sensors (Basel, Switzerland) · 2018
    Review
  8. Article
  9. Article
  10. Tunable control of antibody immobilization using electric field.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Microfluidic systems for pathogen sensing: a review.Sensors (Basel, Switzerland) · 2009
    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

7 authors at 2 institutions in 1 country.

AmirAli H TalasazDepartment of Electrical Engineering, Stanford University, Palo Alto, CA 94305, USA.
Mohsen Nemat-Gorgani
Yang Liu
Patrik Ståhl
Robert W Dutton
Mostafa Ronaghi
Ronald W Davis
New York Genome Center · USStanford University · US

Funding

WHOLE YEAST GENOME TRANSCRIPTIONAL AND FUNCTIONAL GENE MAPS--A FEASIBILITY STUDYP01HG000205 · NHGRI · STANFORD UNIVERSITY · PI DAVIS, RONALD WAYNE, HOWE, ROGER THOMAS · 1990 to 2016
$120.9M
NHGRI NIH HHS P01 HG 000205NHGRI NIH HHS P01 HG000205
6 · The paper itself

Abstract

We report on a rapid simulation method for predicting protein orientation on a surface based on electrostatic interactions. New methods for predicting protein immobilization are needed because of the increasing use of biosensors and protein microarrays, two technologies that use protein immobilization onto a solid support, and because the orientation of an immobilized protein is important for its function. The proposed simulation model is based on the premise that the protein interacts with the electric field generated by the surface, and this interaction defines the orientation of attachment. Results of this model are in agreement with experimental observations of immobilization of mitochondrial creatine kinase and type I hexokinase on biological membranes. The advantages of our method are that it can be applied to any protein with a known structure; it does not require modeling of the surface at atomic resolution and can be run relatively quickly on readily available computing resources. Finally, we also propose an orientation of membrane-bound cytochrome c, a protein for which the membrane orientation has not been unequivocally determined.

Indexed as

AnimalsComputer SimulationCreatine Kinase, Mitochondrial FormCytochromes cEnzymes, ImmobilizedHexokinaseMitochondrial MembranesModels, BiologicalModels, MolecularSarcomeresStatic ElectricityCreatine Kinase, Mitochondrial FormCytochromes cEnzymes, ImmobilizedHexokinase

Identifiers

PMID17001006
PMCPMC1576295
OpenAlexW2117199397

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.