ArticleThe Journal of biological chemistry2023
Identification and classification of papain-like cysteine proteinases.
Article in The Journal of biological chemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 33 citations in OpenAlex.
- Reprogramming of bacterial virulence by lysine acetylation.Nature communications · 2026Article
- Identifying microbial protease allergens through protein language model-guided homology.Cell systems · 2026Article
- Systematic identification of Salmonella T6SS effectors uncovers diverse new families and lipid-targeting activities.PLoS biology · 2026Article
- Decoding the Pine Wood Nematode's survival mystery: Gene family expansion drives adaptation revealed by dual-omics.PLoS pathogens · 2026Article
- Structural and functional analysis reveals the catalytic mechanism and substrate binding mode of the broad-spectrum endolysin Ply2741.Virulence · 2025Article
- Microbial Proteases: Integration into Food Products and Industrial Processes.Current microbiology · 2025Review
- Structural and functional characterization of IdeC, a novel IgG-specific protease ofInfection and immunity · 2025Article
- Genome-wide molecular characterization and expression profiling of the cysteine protease gene family in maize.BMC genomics · 2025Article
- Identification of a Papain-like Cysteine Protease Functioning as an Avirulence Factor in Striga-Cowpea Interactions.Plants (Basel, Switzerland) · 2025Article
- An interbacterial cysteine protease toxin inhibits cell growth by targeting type II DNA topoisomerases GyrB and ParE.PLoS biology · 2025Article
- The multiple roles of the NlpC_P60 peptidase family in mycobacteria - an underexplored target for antimicrobial drug discovery.FEBS letters · 2025Review
- α/β Hydrolases: Toward Unraveling Entangled Classification.Proteins · 2025Article
- The pan-genome of Spodoptera frugiperda provides new insights into genome evolution and horizontal gene transfer.Communications biology · 2025Article
- Comparative transcriptomes reveal differential effects on host metabolism reprogramming in two different pelagiphage-SAR11 infection systems.ISME communications · 2025Article
- Elucidating the molecular properties and anti-mycobacterial activity of cysteine peptidase domain of D29 mycobacteriophage endolysin.Journal of virology · 2024Article
- Pangenome graph analysis reveals extensive effector copy-number variation in spinach downy mildew.PLoS genetics · 2024Article
- Article
- Females translate male mRNA transferred during mating.iScience · 2024Article
- Identification of novel toxins associated with the extracellular contractile injection system using machine learning.Molecular systems biology · 2024Article
- Genetic evidence for a regulated cysteine protease catalytic triad in LegA7, abioRxiv : the preprint server for biology · 2024Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Papain-like cysteine peptidases form a big and highly diverse superfamily of proteins involved in many important biological functions, such as protein turnover, deubiquitination, tissue remodeling, blood clotting, virulence, defense, and cell wall remodeling. High sequence and structure diversity observed within these proteins hinders their comprehensive classification as well as the identification of new representatives. Moreover, in general protein databases, many families already classified as papain like lack details regarding their mechanism of action or biological function. Here, we use transitive remote homology searches and 3D modeling to newly classify 21 families to the papain-like cysteine peptidase superfamily. We attempt to predict their biological function and provide structural characterization of 89 protein clusters defined based on sequence similarity altogether spanning 106 papain-like families. Moreover, we systematically discuss observed diversity in sequences, structures, and catalytic sites. Eventually, we expand the list of human papain-related proteins by seven representatives, including dopamine receptor-interacting protein 1 as potential deubiquitinase, and centriole duplication regulating CEP76 as retaining catalytically active peptidase-like domain. The presented results not only provide structure-based rationales to already existing peptidase databases but also may inspire further experimental research focused on peptidase-related biological processes.
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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 Socratic graph.