Evidence map›Paper›PMID 19809597›Full record

ArticleBiointerphases2008

Molecular simulation of protein-surface interactions: benefits, problems, solutions, and future directions.

Robert A Latour

Abstract read
In one paragraph

Article in Biointerphases, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing 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

34 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Developments and Ongoing Challenges for Analysis of Surface-Bound Proteins.Annual review of analytical chemistry (Palo Alto, Calif.) · 2021
    Article
  6. Enzyme Models-From Catalysis to Prodrugs.Molecules (Basel, Switzerland) · 2021
    Review
  7. Article
  8. Article
  9. Surface Analysis: From Single Crystals to Biomaterials.Surface and interface analysis : SIA · 2018
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. α-helix to β-hairpin transition of human amylin monomer.The Journal of chemical physics · 2013
    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

1 author.

Robert A LatourDepartment of Bioengineering, Clemson University, Clemson, South Carolina 29634, USA. latourr@clemson.edu

Funding

RESBIO - the Technology Resource for Polymeric BiomaterialsP41EB001046 · NIBIB · RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK · PI KOHN, JOACHIM B. · 2003 to 2017
$17.0M
Nanoscale Investigation of Protein-Surface InteractionsR01GM074511 · NIGMS · UNIVERSITY OF WASHINGTON · PI CASTNER, DAVID G · 2006 to 2009
$2.3M
Force Field Development for Protein Absorption ModelingR01EB006163 · NIBIB · CLEMSON UNIVERSITY · PI LATOUR, ROBERT A · 2006 to 2009
$1.4M
NIBIB NIH HHS P41 EB001046NIBIB NIH HHS R01 EB006163NIGMS NIH HHS R01 GM074511
6 · The paper itself

Abstract

While the importance of protein adsorption to materials surfaces is widely recognized, little is understood at this time regarding how to design surfaces to control protein adsorption behavior. All-atom empirical force field molecular simulation methods have enormous potential to address this problem by providing an approach to directly investigate the adsorption behavior of peptides and proteins at the atomic level. As with any type of technology, however, these methods must be appropriately developed and applied if they are to provide realistic and useful results. Three issues that are particularly important for the accurate simulation of protein adsorption behavior are the selection of a valid force field to represent the atomic-level interactions involved, the accurate representation of solvation effects, and system sampling. In this article, each of these areas is addressed and future directions for continued development are presented.

Identifiers

PMID19809597
PMCPMC2756768

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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.