Evidence map›Paper›PMID 35696087›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2022

Deep Learning-Based Advances In Protein Posttranslational Modification Site and Protein Cleavage Prediction.

Subash C Pakhrin, Suresh Pokharel, Hiroto Saigo, Dukka B Kc

Abstract read
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In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
12.1field-weighted citation impact, top 1% 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

9 citing papers in PubMed, 19 citations in OpenAlex.

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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

4 authors at 3 institutions in 2 countries.

Subash C Pakhrin *School of Computing, College of Engineering, Wichita State University, Wichita, KS, USA.
Suresh Pokharel *Department of Computer Science, College of Computing, Michigan Technological University, Houghton, MI, USA.
Hiroto SaigoFaculty of Information Science and Electrical Engineering, Kyushu University, Fukuoka, Japan.
Dukka B KcDepartment of Computer Science, College of Computing, Michigan Technological University, Houghton, MI, USA. dbkc@mtu.edu.
Michigan Technological University · USKyushu University · JPWichita State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Posttranslational modification (PTM ) is a ubiquitous phenomenon in both eukaryotes and prokaryotes which gives rise to enormous proteomic diversity. PTM mostly comes in two flavors: covalent modification to polypeptide chain and proteolytic cleavage. Understanding and characterization of PTM is a fundamental step toward understanding the underpinning of biology. Recent advances in experimental approaches, mainly mass-spectrometry-based approaches, have immensely helped in obtaining and characterizing PTMs. However, experimental approaches are not enough to understand and characterize more than 450 different types of PTMs and complementary computational approaches are becoming popular. Recently, due to the various advancements in the field of Deep Learning (DL), along with the explosion of applications of DL to various fields, the field of computational prediction of PTM has also witnessed the development of a plethora of deep learning (DL)-based approaches. In this book chapter, we first review some recent DL-based approaches in the field of PTM site prediction. In addition, we also review the recent advances in the not-so-studied PTM , that is, proteolytic cleavage predictions. We describe advances in PTM prediction by highlighting the Deep learning architecture, feature encoding, novelty of the approaches, and availability of the tools/approaches. Finally, we provide an outlook and possible future research directions for DL-based approaches for PTM prediction.

Indexed as

Deep LearningProteomicsMass SpectrometryProtein Processing, Post-TranslationalProteinsProteinsDeep learningMachine learningPhosphorylationPosttranslational modification siteProteolytic cleavage

Identifiers

PMID35696087
OpenAlexW4285159613

What OpenQuestion holds

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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.