Cited by 5Advanced Proteomics Techniques and ApplicationsBioinformatics and Genomic NetworksGenomics and Phylogenetic Studies

The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.

RAPDOR: Using Jensen-Shannon Distance for the computational analysis of complex proteomics datasets

Open access

Published version of a preprint

Abstract

The computational analysis of large proteomics datasets from gradient profiling or spatially resolved proteomics is often as crucial as experimental design. We present RAPDOR, a tool for intuitive analyzing and visualizing such datasets, based on the Jensen-Shannon distance and analysis of similarities between replicates, applied to the identification of RNA-binding proteins (RBPs) and spatial proteomics. First, we examine the in-gradient distribution profiles of protein complexes with or without RNase treatment (GradR) to identify RBPs in the cyanobacterium Synechocystis 6803. RBPs play pivotal regulatory and structural roles. Although numerous RBPs are well characterized, the complete set of RBPs remains unknown for any species. RAPDOR identifies 165 potential RBPs, including ribosomal proteins, RNA-modifying enzymes, and proteins not previously associated with RNA binding. High-ranking putative RBPs, such as ribosome hibernation factor LrtA/RaiA, phosphoglucomutase Sll0726, antitoxin Ssl2245, and preQ(1) synthase QueF predicted by RAPDOR but not the TriPepSVM algorithm, are experimentally validated, indicating the existence of uncharacterized RBP domains. These data are available online, providing a resource for RNase-sensitive protein complexes in cyanobacteria. We then show by reanalyzing existing datasets that RAPDOR effectively examines the intracellular redistribution of proteins upon growth factor stimulation. RAPDOR is a generic, non-parametric tool for analyzing highly complex datasets.

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 · 10.1038/s41467-025-64086-7

Cites

5 of 5 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: 107

  1. Liao, J.-Y. et al. EuRBPDB: a comprehensive resource for annotation, functional and oncological investigation of eukaryotic RNA binding proteins (RBPs). Nucleic Acids Res. 48, D307–D313 (2020). · DOI
  2. Hentze, M. W., Castello, A., Schwarzl, T. & Preiss, T. A brave new world of RNA-binding proteins. Nat. Rev. Mol. Cell Biol. 19, 327–341 (2018). · DOI · Paper page
  3. Akamatsu, W. et al. The RNA-binding protein HuD regulates neuronal cell identity and maturation. Proc. Natl. Acad. Sci. USA 102, 4625–4630 (2005). · DOI · Paper page
  4. Bhargava, S., Patil, V., Mahalingam, K. & Somasundaram, K. Elucidation of the genetic and epigenetic landscape alterations in RNA binding proteins in glioblastoma. Oncotarget 8, 16650–16668 (2016). · DOI
  5. Fusaro, A. F. et al. AtGRP2, a cold-induced nucleo-cytoplasmic RNA-binding protein, has a role in flower and seed development. Planta 225, 1339–1351 (2007). · DOI
  6. Moll, I., Leitsch, D., Steinhauser, T. & Bläsi, U. RNA chaperone activity of the Sm-like Hfq protein. EMBO Rep. 4, 284–289 (2003). · DOI
  7. Møller, T. et al. Hfq: a bacterial Sm-like protein that mediates RNA-RNA interaction. Mol. Cell 9, 23–30 (2002). · DOI
  8. Melamed, S., Adams, P. P., Zhang, A., Zhang, H. & Storz, G. RNA-RNA interactomes of ProQ and Hfq reveal overlapping and competing roles. Mol. Cell 77, 411–425 (2020). · DOI
  9. Smirnov, A., Wang, C., Drewry, L. L. & Vogel, J. Molecular mechanism of mRNA repression in trans by a ProQ-dependent small RNA. EMBO J. 36, 1029–1045 (2017). · DOI
  10. Westermann, A. J. et al. The major RNA-binding protein ProQ impacts virulence gene expression in Salmonella enterica Serovar Typhimurium. mBio 10, e02504-18 (2019). · DOI
  11. Liu, M. Y., Yang, H. & Romeo, T. The product of the pleiotropic Escherichia coli gene csrAi modulates glycogen biosynthesis via effects on mRNA stability. J. Bacteriol. 177, 2663–2672 (1995). · DOI
  12. Zhu, Y., Ponath, F., Cosi, V. & Vogel, J. A global survey of small RNA interactors identifies KhpA and KhpB as major RNA-binding proteins in Fusobacterium nucleatum. Nucleic Acids Res. 52, 3950–3970 (2024). · DOI
  13. Hör, J. et al. Grad-seq in a Gram-positive bacterium reveals exonucleolytic sRNA activation in competence control. EMBO J. 39, e103852 (2020). · DOI
  14. Lekontseva, N. et al. Crystal structures and RNA-binding properties of Lsm proteins from archaea Sulfolobus acidocaldarius and Methanococcus vannielii: Similarity and difference of the U-binding mode. Biochimie 175, 1–12 (2020). · DOI
  15. Zhang, X. & Liu, S. RBPPred: predicting RNA-binding proteins from sequence using SVM. Bioinformatics 33, 854–862 (2017). · DOI
  16. Zheng, J. et al. Deep-RBPPred: Predicting RNA binding proteins in the proteome scale based on deep learning. Sci. Rep. 8, 15264 (2018). · DOI
  17. Bressin, A. et al. TriPepSVM: de novo prediction of RNA-binding proteins based on short amino acid motifs. Nucleic Acids Res. 47, 4406–4417 (2019). · DOI
  18. Smirnov, A. et al. Grad-seq guides the discovery of ProQ as a major small RNA-binding protein. Proc. Natl. Acad. Sci. USA 113, 11591–11596 (2016). · DOI
  19. Gerovac, M. et al. A grad-seq view of RNA and protein complexes in Pseudomonas aeruginosa under standard and bacteriophage predation conditions. mBio 12, https://doi.org/10.1128/mbio.03454-20 (2021). · DOI · Paper page
  20. Hör, J. et al. Grad-seq shines light on unrecognized RNA and protein complexes in the model bacterium Escherichia coli. Nucleic Acids Res. 48, 9301–9319 (2020). · DOI
  21. Lamm-Schmidt, V. et al. Grad-seq identifies KhpB as a global RNA-binding protein in Clostridioides difficile that regulates toxin production. Microlife 2, uqab004 (2021). · DOI
  22. Michaux, C., Gerovac, M., Hansen, E. E., Barquist, L. & Vogel, J. Grad-seq analysis of Enterococcus faecalis and Enterococcus faecium provides a global view of RNA and protein complexes in these two opportunistic pathogens. Microlife 4, uqac027 (2023). · DOI
  23. Riediger, M. et al. Analysis of a photosynthetic cyanobacterium rich in internal membrane systems via gradient profiling by sequencing (Grad-seq). Plant Cell 33, 248–269 (2021). · DOI
  24. Chihara, K., Gerovac, M., Hörb, J. & Vogel, J. Global profiling of the RNA and protein complexes of Escherichia coli by size exclusion chromatography followed by RNA sequencing and mass spectrometry (SEC-seq). RNA 29, 123–139 (2023). · DOI
  25. Caudron-Herger, M. et al. R-DeeP: Proteome-wide and quantitative identification of RNA-dependent proteins by density gradient ultracentrifugation. Mol. Cell 75, 184–199.e10 (2019). · DOI
  26. Gerovac, M. et al. Global discovery of bacterial RNA-binding proteins by RNase-sensitive gradient profiles reports a new FinO domain protein. RNA 26, 1448–1463 (2020). · DOI · Paper page
  27. Mahbub, M. et al. mRNA localization, reaction centre biogenesis and thylakoid membrane targeting in cyanobacteria. Nat. Plants 6, 1179–1191 (2020). · DOI
  28. Hemm, L. et al. The RRM domain-containing protein Rbp3 interacts with ribosomes and the 3’ ends of mRNAs encoding photosynthesis proteins. Proc. Natl. Acad. Sci. USA 122, e2506275122 (2025). · DOI · Paper page
  29. Klähn, S. et al. The sRNA NsiR4 is involved in nitrogen assimilation control in cyanobacteria by targeting glutamine synthetase inactivating factor IF7. Proc. Natl. Acad. Sci. USA 112, E6243–E6252 (2015). · DOI
  30. de Porcellinis, A. J. et al. The non-coding RNA Ncr0700/PmgR1 is required for photomixotrophic growth and the regulation of glycogen accumulation in the cyanobacterium Synechocystis sp. PCC 6803. Plant Cell Physiol. 57, 2091–2103 (2016). · DOI
  31. Georg, J. et al. Acclimation of oxygenic photosynthesis to iron starvation Is controlled by the sRNA IsaR1. Curr. Biol. 27, 1425–1436 (2017). · DOI
  32. Klähn, S. et al. A glutamine riboswitch is a key element for the regulation of glutamine synthetase in cyanobacteria. Nucleic Acids Res. 46, 10082–10094 (2018).
  33. Brenes-Álvarez, M., Vioque, A. & Muro-Pastor, A. M. The integrity of the cell wall and its remodeling during heterocyst differentiation are regulated by phylogenetically conserved small RNA Yfr1 in Nostoc sp. strain PCC 7120. mBio 11, https://doi.org/10.1128/mbio.02599-19 (2020). · DOI
  34. Brenes-Álvarez, M., Vioque, A. & Muro-Pastor, A. M. The heterocyst-specific small RNA NsiR1 regulates the commitment to differentiation in Nostoc. Microbiol. Spectr. 10, e02274–21 (2022). · DOI
  35. Schuergers, N. et al. Binding of the RNA chaperone Hfq to the type IV pilus base is crucial for its function in Synechocystis sp. PCC 6803. Mol. Microbiol. 92, 840–852 (2014). · DOI
  36. Hemm, L. et al. Interactors and effects of overexpressing YlxR/RnpM, a conserved RNA binding protein in cyanobacteria. RNA Biol. 21, 1308–1326 (2024). · DOI
  37. Martinez-Val, A. et al. Spatial-proteomics reveals phospho-signaling dynamics at subcellular resolution. Nat. Commun. 12, 7113 (2021). · DOI · Paper page
  38. Vioque, A. Analysis of the gene encoding the RNA subunit of ribonuclease P from cyanobacteria. Nucleic Acids Res. 20, 6331–6337 (1992). · DOI
  39. de la Cruz, J. & Vioque, A. Increased sensitivity to protein synthesis inhibitors in cells lacking tmRNA. RNA 7, 1708–1716 (2001).
  40. Endres, D. M. & Schindelin, J. E. A new metric for probability distributions. IEEE Trans. Inf. Theory 49, 1858–1860 (2003). · DOI
  41. Clarke, K. R. Non-parametric multivariate analyses of changes in community structure. Austral J. Ecol. 18, 117–143 (1993). · DOI
  42. Branlant, C., Krol, A., Machatt, A. & Ebel, J. P. The secondary structure of the protein L1 binding region of ribosomal 23S RNA. Homologies with putative secondary structures of the L11 mRNA and of a region of mitochondrial 16S rRNA. Nucleic Acids Re.s 9, 293–307 (1981). · DOI
  43. Nikonov, S. et al. Crystal structure of the RNA binding ribosomal protein L1 from Thermus thermophilus. EMBO J. 15, 1350–1359 (1996). · DOI
  44. Brenes-Álvarez, M. et al. R-DeeP/TripepSVM identifies the RNA-binding OB-fold-like protein PatR as regulator of heterocyst patterning. Nucleic Acids Res. 53, gkae1247 (2025). · DOI
  45. Phillips, G. J. & Silhavy, T. J. The E. coli ffh gene is necessary for viability and efficient protein export. Nature 359, 744–746 (1992). · DOI
  46. Zhang, Y., Wu, D., Wang, Y. & Xu, X. Two types of C-terminal regions of RNA-binding proteins play distinct roles in stress tolerance of Synechocystis sp. PCC 6803. FEMS Microbiol. Lett. 369, fnac021 (2022). · DOI
  47. Tan, X. et al. Role of Rbp1 in the acquired chill-light tolerance of cyanobacteria. J. Bacteriol. 193, 2675–2683 (2011). · DOI
  48. Jiang, Y. et al. Unveiling the structural features that determine the dual methyltransferase activities of Streptococcus pneumoniae RlmCD. PLoS Pathog. 14, e1007379 (2018). · DOI
  49. Jensen, P. E., Gibson, L. C. D., Henningsen, K. W. & Hunter, C. N. Expression of the chlI, chlD, and chlH genes from the cyanobacterium Synechocystis PCC6803 in Escherichia coli and demonstration that the three cognate proteins are required for magnesium-protoporphyrin chelatase activity. J. Biol. Chem. 271, 16662–16667 (1996). · DOI
  50. Chen, X. et al. Crystal structure of the catalytic subunit of magnesium chelatase. Nat. Plants 1, 1–5 (2015). · DOI
  51. Osanai, T. et al. ChlH, the H subunit of the Mg-chelatase, is an anti-sigma factor for SigE in Synechocystis sp. PCC 6803. Proc. Natl. Acad. Sci. USA 106, 6860–6865 (2009). · DOI
  52. Imamura, S. et al. Purification, characterization, and gene expression of all sigma factors of RNA polymerase in a cyanobacterium. J. Mol. Biol. 325, 857–872 (2003). · DOI
  53. Behler, J. et al. The host-encoded RNase E endonuclease as the crRNA maturation enzyme in a CRISPR–Cas subtype III-Bv system. Nat. Microbiol. 3, 367–377 (2018). · DOI
  54. Samartzidou, H. & Widger, W. R. Transcriptional and posttranscriptional control of mRNA from lrtA, a light-repressed transcript in Synechococcus sp. PCC 7002. Plant Physiol. 117, 225–234 (1998). · DOI
  55. Kopfmann, S., Roesch, S. K. & Hess, W. R. Type II toxin-antitoxin systems in the unicellular cyanobacterium Synechocystis sp. PCC 6803. Toxins 8, 228.1–228.23 (2016). · DOI
  56. Díaz-Rullo, J. & González-Pastor, J. E. tRNA queuosine modification is involved in biofilm formation and virulence in bacteria. Nucleic Acids Res. 51, 9821–9837 (2023). · DOI
  57. Yoshimura, H., Hisabori, T., Yanagisawa, S. & Ohmori, M. Identification and characterization of a novel cAMP receptor protein in the cyanobacterium Synechocystis sp. PCC 6803. J. Biol. Chem. 275, 6241–6245 (2000). · DOI
  58. Kujirai, J. et al. Interaction of the GntR-family transcription factor Sll1961 with thioredoxin in the cyanobacterium Synechocystis sp. PCC 6803. Sci. Rep. 8, 6666 (2018). · DOI
  59. Sakaki, K. et al. A suicide enzyme catalyzes multiple reactions for biotin biosynthesis in cyanobacteria. Nat. Chem. Biol. 16, 415–422 (2020). · DOI
  60. Hill, C. S. Nucleocytoplasmic shuttling of Smad proteins. Cell Res. 19, 36–46 (2009). · DOI
  61. Fankhauser, C. & Chen, M. Transposing phytochrome into the nucleus. Trends Plant Sci. 13, 596–601 (2008). · DOI
  62. Banushi, B., Joseph, S. R., Lum, B., Lee, J. J. & Simpson, F. Endocytosis in cancer and cancer therapy. Nat. Rev. Cancer 23, 450–473 (2023). · DOI
  63. Jeffery, C. J. An enzyme in the test tube, and a transcription factor in the cell: Moonlighting proteins and cellular factors that affect their behavior. Protein Sci. 28, 1233–1238 (2019). · DOI
  64. Kreß, J. K. C., Jessen, C., Marquardt, A., Hufnagel, A. & Meierjohann, S. NRF2 enables EGFR signaling in melanoma cells. Int. J. Mol. Sci. 22, 3803 (2021). · DOI
  65. Okur, M. N. et al. Intersectin 1 enhances Cbl ubiquitylation of epidermal growth factor receptor through regulation of Sprouty2-Cbl interaction. Mol. Cell Biol. 32, 817–825 (2012). · DOI
  66. Zhao, H., Yang, Y. & Zhou, Y. Highly accurate and high-resolution function prediction of RNA binding proteins by fold recognition and binding affinity prediction. RNA Biol. 8, 988–996 (2011). · DOI
  67. Yang, Y., Zhao, H., Wang, J. & Zhou, Y. SPOT-Seq-RNA: predicting protein-RNA complex structure and RNA-binding function by fold recognition and binding affinity prediction. Methods Mol. Biol. 1137, 119–130 (2014). · DOI
  68. Queiroz, R. M. L. et al. Comprehensive identification of RNA–protein interactions in any organism using orthogonal organic phase separation (OOPS). Nat. Biotechnol. 37, 169–178 (2019). · DOI
  69. Shchepachev, V. et al. Defining the RNA interactome by total RNA-associated protein purification. Mol. Syst. Biol. 15, e8689 (2019). · DOI
  70. Asencio, C., Chatterjee, A. & Hentze, M. W. Silica-based solid-phase extraction of cross-linked nucleic acid-bound proteins. Life Sci. Alliance 1, e201800088 (2018). · DOI
  71. Yusupova, G. & Yusupov, M. High-resolution structure of the eukaryotic 80S ribosome. Annu Rev. Biochem. 83, 467–486 (2014). · DOI
  72. Mutsuda, M. & Sugiura, M. Translation initiation of cyanobacterial rbcS mRNAs requires the 38-kDa ribosomal protein S1 but not the Shine-Dalgarno sequence. J. Biol. Chem. 281, 38314–38321 (2006). · DOI
  73. Nakagawa, S., Niimura, Y., Miura, K. & Gojobori, T. Dynamic evolution of translation initiation mechanisms in prokaryotes. Proc. Natl. Acad. Sci. USA 107, 6382–6387 (2010). · DOI
  74. Castello, A., Hentze, M. W. & Preiss, T. Metabolic enzymes enjoying new partnerships as RNA-binding proteins. Trends Endocrinol. Metab. 26, 746–757 (2015). · DOI
  75. Fuller, G. G. et al. RNA promotes phase separation of glycolysis enzymes into yeast G bodies in hypoxia. ELife 9, e48480 (2020). · DOI
  76. Wegener, M. & Dietz, K.-J. The mutual interaction of glycolytic enzymes and RNA in post-transcriptional regulation. RNA 28, 1446–1468 (2022). · DOI
  77. Agarwalla, S., Kealey, J. T., Santi, D. V. & Stroud, R. M. Characterization of the 23 S ribosomal RNA m5U1939 methyltransferase from Escherichia coli. J. Biol. Chem. 277, 8835–8840 (2002). · DOI
  78. Madsen, C. T., Mengel-Jørgensen, J., Kirpekar, F. & Douthwaite, S. Identifying the methyltransferases for m5U747 and m5U1939 in 23S rRNA using MALDI mass spectrometry. Nucleic Acids Res. 31, 4738–4746 (2003). · DOI
  79. Desmolaize, B. et al. A single methyltransferase YefA (RlmCD) catalyses both m5U747 and m5U1939 modifications in Bacillus subtilis 23S rRNA. Nucleic Acids Res. 39, 9368–9375 (2011). · DOI
  80. De Crécy-Lagard, V. et al. Biosynthesis and function of 7-deazaguanine derivatives in bacteria and phages. Microbiol. Mol. Biol. Rev. 88, e00199–23 (2024). · DOI
  81. Keffer-Wilkes, L. C., Veerareddygari, G. R. & Kothe, U. RNA modification enzyme TruB is a tRNA chaperone. Proc. Natl. Acad. Sci. USA 113, 14306–14311 (2016). · DOI
  82. Keffer-Wilkes, L. C., Soon, E. F. & Kothe, U. The methyltransferase TrmA facilitates tRNA folding through interaction with its RNA-binding domain. Nucleic Acids Res. 48, 7981–7990 (2020). · DOI
  83. Tan, X., Varughese, M. & Widger, W. R. A light-repressed transcript found in Synechococcus PCC 7002 is similar to a chloroplast-specific small subunit ribosomal protein and to a transcription modulator protein associated with sigma 54. J. Biol. Chem. 269, 20905–20912 (1994). · DOI
  84. Galmozzi, C. V., Florencio, F. J. & Muro-Pastor, M. I. The cyanobacterial ribosomal-associated orotein LrtA is involved in post-stress survival in Synechocystis sp. PCC 6803. PLOS ONE 11, e0159346 (2016). · DOI
  85. Lang, M. et al. Sleeping ribosomes: Bacterial signaling triggers RaiA mediated persistence to aminoglycosides. iScience 24, https://doi.org/10.1016/j.isci.2021.103128 (2021). · DOI
  86. Lindahl, M. & Florencio, F. J. Thioredoxin-linked processes in cyanobacteria are as numerous as in chloroplasts, but targets are different. Proc. Natl. Acad. Sci. USA 100, 16107–16112 (2003). · DOI
  87. Liu, L., Hu, H., Gao, H. & Xu, X. Role of two phosphohexomutase genes in glycogen synthesis in Synechocystis sp. PCC6803. Chin. Sci. Bull. 58, 4616–4621 (2013). · DOI
  88. Doello, S. & Forchhammer, K. Phosphoglucomutase comes into the spotlight. J. Exp. Bot. 74, 1293–1296 (2023). · DOI
  89. Ortega-Martínez, P., Roldán, M., Díaz-Troya, S. & Florencio, F. J. Stress response requires an efficient connection between glycogen and central carbon metabolism by phosphoglucomutases in cyanobacteria. J. Exp. Bot. 74, 1532–1550 (2023). · DOI
  90. Agarwal, S., Mishra, N. K., Bhatnagar, S. & Bhatnagar, R. PemK toxin of Bacillus anthracis is a ribonuclease: an insight into its active site, structure, and function. J. Biol. Chem. 285, 7254–7270 (2010). · DOI
  91. Lee, M. W., Rogers, E. E. & Stenger, D. C. Xylella fastidiosa Plasmid-encoded PemK toxin is an endoribonuclease. Phytopathology 102, 32–40 (2012). · DOI
  92. Trautmann, D., Voss, B., Wilde, A., Al-Babili, S. & Hess, W. R. Microevolution in cyanobacteria: re-sequencing a motile substrain of Synechocystis sp. PCC 6803. DNA Res. 19, 435–448 (2012). · DOI
  93. Rippka, R., Deruelles, J., Waterbury, J. B., Herdman, M. & Stanier, R. Y. Generic assignments, strain histories and properties of pure cultures of cyanobacteria. Microbiology 111, 1–61 (1979). · DOI · Paper page
  94. Cox, J. & Mann, M. MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nat. Biotechnol. 26, 1367–1372 (2008). · DOI · Paper page
  95. Cox, J. et al. Accurate proteome-wide label-free quantification by delayed normalization and maximal peptide ratio extraction, termed MaxLFQ. Mol. Cell. Proteom. 13, 2513 (2014). · DOI · Paper page
  96. Deutsch, E. W. et al. The ProteomeXchange consortium at 10 years: 2023 update. Nucleic Acids Res. 51, D1539–D1548 (2023). · DOI
  97. Perez-Riverol, Y. et al. The PRIDE database at 20 years: 2025 update. Nucleic Acids Res. 53, D543–D553 (2025). · DOI
  98. Krauspe, V. et al. Discovery of a small protein factor involved in the coordinated degradation of phycobilisomes in cyanobacteria. Proc. Natl. Acad. Sci. USA 118, e2012277118 (2021). · DOI · Paper page
  99. Beyer, H. M. et al. AQUA cloning: a versatile and simple enzyme-free cloning approach. PLOS ONE 10, e0137652 (2015). · DOI
  100. Kaltenbrunner, A. et al. Regulation of pSYSA defense plasmid copy number in Synechocystis through RNase E and a highly transcribed asRNA. Front. Microbiol. 14, 1112307 (2023). · DOI
  101. Kraus, A. et al. Protein NirP1 regulates nitrite reductase and nitrite excretion in cyanobacteria. Nat. Commun. 15, 1911 (2024). · DOI · Paper page
  102. Stenum, T. S. et al. RNA interactome capture in Escherichia coli globally identifies RNA-binding proteins. Nucleic Acids Res. 51, 4572–4587 (2023). · DOI
  103. Boyd, S. P. & Vandenberghe, L. Convex Optimization. (Cambridge University Press, 2004). · DOI · Paper page
  104. Ritchie, M. E. et al. limma powers differential expression analyses for RNA-sequencing and microarray studies. Nucleic Acids Res. 43, e47 (2015). · DOI · Paper page
  105. The UniProt Consortium UniProt: the universal protein knowledgebase in 2023. Nucleic Acids Res. 51, D523–D531 (2023). · DOI · Paper page
  106. Li, W. & Godzik, A. Cd-hit: a fast program for clustering and comparing large sets of protein or nucleotide sequences. Bioinformatics 22, 1658–1659 (2006). · DOI
  107. Palme, J., Hochreiter, S. & Bodenhofer, U. KeBABS: an R package for kernel-based analysis of biological sequences. Bioinformatics 31, 2574–2576 (2015). · DOI

Metadata

Authors
Hemm, L., Rabsch, D., Ropp, H. R., Reimann, V., Gerth, P., Bartel, J., Brenes-Álvarez, M., Maaß, S., Becher, D., Hess, W. R., & Backofen, R.
Affiliations
  • University of Freiburg (DE)
  • Universität Greifswald (DE)
Corresponding author
  • Hess, Wolfgang R.
  • Backofen, Rolf
Venue
Nature Communications
Published
2025-09-26
Volume
16
Issue
1
Pages
8527-8527
ISSN
2041-1723 (ISSN-L)
OpenAlex
W4414534912
Cited by
5
References
5
Citations by year
2026: 3 · 2025: 2
FWCI
1.27
Type
journal article
Language
en
Open access
Locations
  • Nature Communications (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • PubMed Central (publishedVersion, cc-by)
  • FreiDok plus (Universitätsbibliothek Freiburg) (submittedVersion, cc-by)
  • HAL (submittedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
  • Deutsche Forschungsgemeinschaft (322977937/GRK2344, HE 2544/12-2, BA 2168/21-2, BE 3869/5-2, 390939984, CIBSS - EXC-2189 - Project ID 390939984)
  • Alexander von Humboldt-Stiftung (Alexander von Humboldt postdoctoral fellowship)
Topics
  • Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
  • 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
Keywords
Jensen-Shannon distance, RNA-binding proteins, spatial proteomics, Synechocystis sp. PCC 6803, cyanobacteria, protein complex identification
MeSH terms
Algorithms, Bacterial Proteins, Software, RNA-Binding Proteins, Computational Biology, Proteomics, Synechocystis

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