Evidence map›Paper›PMID 27086078›Full record

ReviewCurrent opinion in structural biology2016

Algorithms for protein design.

Pablo Gainza, Hunter M Nisonoff, Bruce R Donald

Abstract readReview
In one paragraph

Review in Current opinion in structural biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed, 1 pooled it
–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

35 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Exploring the Protein Sequence Space with Global Generative Models.Cold Spring Harbor perspectives in biology · 2023
    Review
  8. Article
  9. From sequence to function through structure: Deep learning for protein design.Computational and structural biotechnology journal · 2023
    Review
  10. Article
  11. Protein design via deep learning.Briefings in bioinformatics · 2022
    Review
  12. Article
  13. Knowledge-Based Unfolded State Model for Protein Design.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
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

3 authors.

Pablo GainzaDepartment of Computer Science, Duke University, Durham, NC, United States.
Hunter M NisonoffDepartment of Computer Science, Duke University, Durham, NC, United States.
Bruce R DonaldDepartment of Computer Science, Duke University, Durham, NC, United States; Department of Biochemistry, Duke University Medical Center, Durham, NC, United States; Department of Chemistry, Duke University, Durham, NC, United States. Electronic address: brd+cosb15@cs.duke.edu.

Funding

Computational Structure-Based Protein DesignR01GM078031 · NIGMS · DUKE UNIVERSITY · PI DONALD, BRUCE R. · 2008 to 2021
$4.3M
NIGMS NIH HHS R01 GM078031
6 · The paper itself

Abstract

Computational structure-based protein design programs are becoming an increasingly important tool in molecular biology. These programs compute protein sequences that are predicted to fold to a target structure and perform a desired function. The success of a program's predictions largely relies on two components: first, the input biophysical model, and second, the algorithm that computes the best sequence(s) and structure(s) according to the biophysical model. Improving both the model and the algorithm in tandem is essential to improving the success rate of current programs, and here we review recent developments in algorithms for protein design, emphasizing how novel algorithms enable the use of more accurate biophysical models. We conclude with a list of algorithmic challenges in computational protein design that we believe will be especially important for the design of therapeutic proteins and protein assemblies.

Indexed as

AlgorithmsComputational BiologyHeuristicsProtein EngineeringProteinsThermodynamicsProteins

Identifiers

PMID27086078
PMCPMC5065368

What OpenQuestion holds

Textmetadata
LicenceTDM
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.