PreprintCited by 8Bioinformatics and Genomic NetworksGenomics and Phylogenetic StudiesAdvanced Proteomics Techniques and Applications

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

SHEPHARD: a modular and extensible software architecture for analyzing and annotating large protein datasets

Open access

Preprint — published as 10.1093/bioinformatics/btad488

Abstract

The emergence of high-throughput experiments and high-resolution computational predictions has led to an explosion in the quality and volume of protein sequence annotations at proteomic scales. Unfortunately, integrating and analyzing complex sequence annotations remains logistically challenging. Here we present SHEPHARD, a software package that makes large-scale integrative protein bioinformatics trivial. SHEPHARD is provided as a stand-alone package and with a pre-compiled set of human annotations in a Google Colab notebook.

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1101/2022.09.18.508433

Cites

1 of 1 references verified0 citation errors · 0 not checkable

Statistics

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Flagged first, then by citations

Research works printed but not linked: 36

  1. 10.1146/annurev-anchem-071213-020216 · DOI
  2. 2019, Massively Parallel Assays and Quantitative Sequence–Function Relationships, Annu. Rev. Genomics Hum. Genet, 20, 99, 10.1146/annurev-genom-083118-014845 · DOI
  3. 10.1021/acs.analchem.5b04123 · DOI · Paper page
  4. 10.1021/cr500491u · DOI
  5. 2021, Highly accurate protein structure prediction for the human proteome, Nature, 596, 590, 10.1038/s41586-021-03828-1 · DOI · Paper page
  6. Lindorff-Larsen, K. & Kragelund, B. B. On the potential of machine learning to examine the relationship between sequence, structure, dynamics and function of intrinsically disordered proteins. J. Mol. Biol. 167196 (2021). · DOI · Paper page
  7. 2022, Current progress and open challenges for applying deep learning across the biosciences, Nat. Commun, 13, 1728, 10.1038/s41467-022-29268-7 · DOI
  8. 10.1093/nar/gku989 · DOI · Paper page
  9. CAID Predictors, DisProt Curators, 2021, Critical assessment of protein intrinsic disorder prediction, Nat. Methods, 18, 472, 10.1038/s41592-021-01117-3 · DOI · Paper page
  10. 10.1093/nar/gkh253 · DOI · Paper page
  11. 2022, The structural context of posttranslational modifications at a proteome-wide scale, PLoS Biol, 20, e3001636, 10.1371/journal.pbio.3001636 · DOI
  12. 10.1016/j.sbi.2015.03.008 · DOI
  13. Zarin, T. , Strome, B. , Peng, G. , Pritišanac, I. , Forman-Kay, J. D. & Moses, A. M. Identifying molecular features that are associated with biological function of intrinsically disordered protein regions. Elife 10,(2021). · DOI
  14. 10.1073/pnas.1821038116 · DOI
  15. Gutierrez, J. I. , Brittingham, G. P. , Karadeniz, Y. , Tran, K. D. , Dutta, A. , Holehouse, A. S. , Peterson, C. L. & Holt, L. J. SWI/SNF senses carbon starvation with a pH-sensitive low-complexity sequence. Elife 11, (2022). · DOI
  16. 2020, IDDomainSpotter: Compositional bias reveals domains in long disordered protein regions-Insights from transcription factors, Protein Sci, 29, 169, 10.1002/pro.3754 · DOI
  17. 2020, Intrinsically disordered protein regions and phase separation: sequence determinants of assembly or lack thereof, Emerg Top Life Sci, 4, 307, 10.1042/ETLS20190164 · DOI
  18. 2016, A Concentration-Dependent Liquid Phase Separation Can Cause Toxicity upon Increased Protein Expression, Cell Rep, 16, 222, 10.1016/j.celrep.2016.05.076 · DOI
  19. 10.1038/s41586-020-2649-2 · DOI · Paper page
  20. 2011, The NumPy Array: A Structure for Efficient Numerical Computation, Computing in Science Engineering, 13, 22, 10.1109/MCSE.2011.37 · DOI · Paper page
  21. 10.1093/nar/gku1154 · DOI
  22. 2022, PANTHER: Making genome-scale phylogenetics accessible to all, Protein Sci, 31, 8, 10.1002/pro.4218 · DOI · Paper page
  23. 10.1016/j.cell.2015.09.053 · DOI · Paper page
  24. 2020, Reshaping of the Arabidopsis thaliana Proteome Landscape and Co-regulation of Proteins in Development and Immunity, Mol. Plant, 13, 1709, 10.1016/j.molp.2020.09.024 · DOI
  25. 2019, Quantification of Proteins and Histone Marks in Drosophila Embryos Reveals Stoichiometric Relationships Impacting Chromatin Regulation, Dev. Cell, 51, 632, 10.1016/j.devcel.2019.09.011 · DOI
  26. 2014, Quantitative analysis of the Escherichia coli proteome, Data Brief, 1, 7, 10.1016/j.dib.2014.08.004 · DOI
  27. 10.1186/1471-2164-9-102 · DOI
  28. 10.1074/mcp.M113.035824 · DOI
  29. 10.1038/nature02046 · DOI · Paper page
  30. 10.1074/mcp.M115.054288 · DOI
  31. 2021, Metapredict: a fast, accurate, and easy-to-use predictor of consensus disorder and structure, Biophys. J, 120, 4312, 10.1016/j.bpj.2021.08.039 · DOI
  32. 10.1093/bioinformatics/btu310 · DOI
  33. 10.1016/j.bpj.2015.08.015 · DOI
  34. 10.1002/bip.360221211 · DOI · Paper page
  35. 10.1021/ci400541d · DOI
  36. 2019, SESCA: Predicting Circular Dichroism Spectra from Protein Molecular Structures, J. Chem. Theory Comput, 15, 5087, 10.1021/acs.jctc.9b00203 · DOI

Metadata

Authors
Ginell, G. M., Flynn, A. J., & Holehouse, A. S.
Affiliations
Washington University in St. Louis (US)
Corresponding author
Holehouse, Alex S.
Venue
Bioinformatics
Publisher
openRxiv
Published
2022-09-19
Volume
39
Issue
8
ISSN
1367-4803 (ISSN-L)
OpenAlex
W4385564401
Cited by
8
References
1
Citations by year
2025: 2 · 2024: 4 · 2023: 2
FWCI
0.71
Type
journal article
Language
en
Open access
Licence
cc-by
Locations
  • Bioinformatics (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • Digital Commons@Becker (Washington University School of Medicine) (submittedVersion, cc-by)
Funders
  • National Science Foundation (2213983, 2128068)
  • Longer Life Foundation
  • Division of Biological Infrastructure (2213983)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Bioinformatics and Genomic Networks
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Phylogenetic Studies
  • Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
Keywords
protein sequence annotation, proteomics, integrative bioinformatics, software architecture, Python framework, hierarchical data structures, annotation integration, proteome-wide analysis
MeSH terms
Software, Computational Biology, Proteome, Proteomics, Molecular Sequence Annotation

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review