Evidence map›Paper›PMID 30611429›Full record

ArticleMethods in enzymology2019

CS-ROSETTA.

Santrupti Nerli, Nikolaos G Sgourakis

Abstract read
In one paragraph

Article in Methods in enzymology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. [Bioinformatics analysis and validation of the interaction between PML protein and TAB1 protein].Nan fang yi ke da xue xue bao = Journal of Southern Medical University · 2024
    Article
  6. Probing excited stateMethods (San Diego, Calif.) · 2023
    Article
  7. Article
  8. Article
  9. Recent Advances in NMR Protein Structure Prediction with ROSETTA.International journal of molecular sciences · 2023
    Review
  10. Article
  11. Article
  12. Article
  13. Canine Adenovirus 1 Isolation Bioinformatics Analysis of the Fiber.Frontiers in cellular and infection microbiology · 2022
    Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Review
  19. Review
  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

2 authors.

Santrupti NerliDepartment of Chemistry and Biochemistry, University of California Santa Cruz, Santa Cruz, CA, United States; Department of Computer Science, University of California Santa Cruz, Santa Cruz, CA, United States.
Nikolaos G SgourakisDepartment of Chemistry and Biochemistry, University of California Santa Cruz, Santa Cruz, CA, United States. Electronic address: nsgourak@ucsc.edu.

Funding

An integrative structural biology approach to understanding metabolite recognition by cellular receptorsR35GM125034 · NIGMS · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI SGOURAKIS, NIKOLAOS · 2017 to 2025
$4.7M
Molecular mechanism of antigen editing by Class-I MHC ChaperonesR01AI143997 · NIAID · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI SGOURAKIS, NIKOLAOS · 2019 to 2023
$4.0M
NIAID NIH HHS R01 AI143997NIGMS NIH HHS R35 GM125034
6 · The paper itself

Abstract

Chemical Shift-Rosetta (CS-Rosetta) is an automated method that employs NMR chemical shifts to model protein structures de novo. In this chapter, we introduce the terminology and central concepts of CS-Rosetta. We describe the architecture and functionality of automatic NOESY assignment (AutoNOE) and structure determination protocols (Abrelax and RASREC) within the CS-Rosetta framework. We further demonstrate how CS-Rosetta can discriminate near-native structures against a large conformational search space using restraints obtained from NMR data, and/or sequence and structure homology. We highlight how CS-Rosetta can be combined with alternative automated approaches to (i) model oligomeric systems and (ii) create NMR-based structure determination pipeline. To show its practical applicability, we emphasize on the computational requirements and performance of CS-Rosetta for protein targets of varying molecular weight and complexity. Finally, we discuss the current Python interface, which enables easy execution of protocols for rapid and accurate high-resolution structure determination.

Indexed as

AlgorithmsSoftwareBinding SitesHumansMagnetic Resonance ImagingModels, MolecularMolecular WeightProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein FoldingProtein Interaction Domains and MotifsProteinsStructural Homology, ProteinThermodynamicsProteinsAbrelaxCS-RosettaNMR structure determinationNOE assignmentRASREC

Identifiers

PMID30611429
PMCPMC7416455

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.