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RAPDOR: Using Jensen-Shannon Distance for the computational analysis of complex proteomics datasets
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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.
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Global quantification of mammalian gene expression control
Schwanhäusser, B., Busse, D., Li, N., Dittmar, G., Schuchhardt, J., Wolf, J., Chen, W., & Selbach, M. (2011) · Nature · doi:10.1038/nature10098 · Cited by 6,566
Fast and accurate protein structure search with Foldseek
van Kempen, M., Kim, S. S., Tumescheit, C., Mirdita, M., Lee, J., Gilchrist, C. L. M., Söding, J., & Steinegger, M. (2022) · doi:10.1101/2022.02.07.479398 · Cited by 2,598
Fast and accurate protein structure search with Foldseek
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A large-scale binding and functional map of human RNA-binding proteins
Van Nostrand, E. L., Freese, P., Pratt, G. A., Wang, X., Wei, X., Xiao, R., Blue, S. M., Chen, J.-Y., Cody, N. A. L., Dominguez, D., et al. (2020) · Nature · doi:10.1038/s41586-020-2077-3 · Cited by 1,317
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Flagged first, then by citations
Research works printed but not linked: 107
- 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
- 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
- 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
- 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
- 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
- Moll, I., Leitsch, D., Steinhauser, T. & Bläsi, U. RNA chaperone activity of the Sm-like Hfq protein. EMBO Rep. 4, 284–289 (2003). · DOI
- Møller, T. et al. Hfq: a bacterial Sm-like protein that mediates RNA-RNA interaction. Mol. Cell 9, 23–30 (2002). · DOI
- 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
- 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
- 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
- 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
- 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
- Hör, J. et al. Grad-seq in a Gram-positive bacterium reveals exonucleolytic sRNA activation in competence control. EMBO J. 39, e103852 (2020). · DOI
- 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
- Zhang, X. & Liu, S. RBPPred: predicting RNA-binding proteins from sequence using SVM. Bioinformatics 33, 854–862 (2017). · DOI
- Zheng, J. et al. Deep-RBPPred: Predicting RNA binding proteins in the proteome scale based on deep learning. Sci. Rep. 8, 15264 (2018). · DOI
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- Mahbub, M. et al. mRNA localization, reaction centre biogenesis and thylakoid membrane targeting in cyanobacteria. Nat. Plants 6, 1179–1191 (2020). · DOI
- 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
- 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
- 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
- Georg, J. et al. Acclimation of oxygenic photosynthesis to iron starvation Is controlled by the sRNA IsaR1. Curr. Biol. 27, 1425–1436 (2017). · DOI
- 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).
- 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
- 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
- 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
- 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
- Martinez-Val, A. et al. Spatial-proteomics reveals phospho-signaling dynamics at subcellular resolution. Nat. Commun. 12, 7113 (2021). · DOI · Paper page
- Vioque, A. Analysis of the gene encoding the RNA subunit of ribonuclease P from cyanobacteria. Nucleic Acids Res. 20, 6331–6337 (1992). · DOI
- de la Cruz, J. & Vioque, A. Increased sensitivity to protein synthesis inhibitors in cells lacking tmRNA. RNA 7, 1708–1716 (2001).
- Endres, D. M. & Schindelin, J. E. A new metric for probability distributions. IEEE Trans. Inf. Theory 49, 1858–1860 (2003). · DOI
- Clarke, K. R. Non-parametric multivariate analyses of changes in community structure. Austral J. Ecol. 18, 117–143 (1993). · DOI
- 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
- Nikonov, S. et al. Crystal structure of the RNA binding ribosomal protein L1 from Thermus thermophilus. EMBO J. 15, 1350–1359 (1996). · DOI
- 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
- 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
- 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
- Tan, X. et al. Role of Rbp1 in the acquired chill-light tolerance of cyanobacteria. J. Bacteriol. 193, 2675–2683 (2011). · DOI
- Jiang, Y. et al. Unveiling the structural features that determine the dual methyltransferase activities of Streptococcus pneumoniae RlmCD. PLoS Pathog. 14, e1007379 (2018). · DOI
- 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
- Chen, X. et al. Crystal structure of the catalytic subunit of magnesium chelatase. Nat. Plants 1, 1–5 (2015). · DOI
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- Sakaki, K. et al. A suicide enzyme catalyzes multiple reactions for biotin biosynthesis in cyanobacteria. Nat. Chem. Biol. 16, 415–422 (2020). · DOI
- Hill, C. S. Nucleocytoplasmic shuttling of Smad proteins. Cell Res. 19, 36–46 (2009). · DOI
- Fankhauser, C. & Chen, M. Transposing phytochrome into the nucleus. Trends Plant Sci. 13, 596–601 (2008). · DOI
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- Shchepachev, V. et al. Defining the RNA interactome by total RNA-associated protein purification. Mol. Syst. Biol. 15, e8689 (2019). · DOI
- 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
- Yusupova, G. & Yusupov, M. High-resolution structure of the eukaryotic 80S ribosome. Annu Rev. Biochem. 83, 467–486 (2014). · DOI
- 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
- 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
- Castello, A., Hentze, M. W. & Preiss, T. Metabolic enzymes enjoying new partnerships as RNA-binding proteins. Trends Endocrinol. Metab. 26, 746–757 (2015). · DOI
- Fuller, G. G. et al. RNA promotes phase separation of glycolysis enzymes into yeast G bodies in hypoxia. ELife 9, e48480 (2020). · DOI
- Wegener, M. & Dietz, K.-J. The mutual interaction of glycolytic enzymes and RNA in post-transcriptional regulation. RNA 28, 1446–1468 (2022). · DOI
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- 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
- Doello, S. & Forchhammer, K. Phosphoglucomutase comes into the spotlight. J. Exp. Bot. 74, 1293–1296 (2023). · DOI
- 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
- 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
- Lee, M. W., Rogers, E. E. & Stenger, D. C. Xylella fastidiosa Plasmid-encoded PemK toxin is an endoribonuclease. Phytopathology 102, 32–40 (2012). · DOI
- 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
- 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
- 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
- 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
- Deutsch, E. W. et al. The ProteomeXchange consortium at 10 years: 2023 update. Nucleic Acids Res. 51, D1539–D1548 (2023). · DOI
- Perez-Riverol, Y. et al. The PRIDE database at 20 years: 2025 update. Nucleic Acids Res. 53, D543–D553 (2025). · DOI
- 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
- Beyer, H. M. et al. AQUA cloning: a versatile and simple enzyme-free cloning approach. PLOS ONE 10, e0137652 (2015). · DOI
- 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
- Kraus, A. et al. Protein NirP1 regulates nitrite reductase and nitrite excretion in cyanobacteria. Nat. Commun. 15, 1911 (2024). · DOI · Paper page
- Stenum, T. S. et al. RNA interactome capture in Escherichia coli globally identifies RNA-binding proteins. Nucleic Acids Res. 51, 4572–4587 (2023). · DOI
- Boyd, S. P. & Vandenberghe, L. Convex Optimization. (Cambridge University Press, 2004). · DOI · Paper page
- 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
- The UniProt Consortium UniProt: the universal protein knowledgebase in 2023. Nucleic Acids Res. 51, D523–D531 (2023). · DOI · Paper page
- 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
- 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
- ORCID
- Venue
- Nature Communications
- Published
- 2025-09-26
- Volume
- 16
- Issue
- 1
- Pages
- 8527-8527
- ISSN
- 2041-1723 (ISSN-L)
- PMC
- PMC12475003
- OpenAlex
- W4414534912
- Cited by
- 5
- References
- 5
- Citations by year
- 2026: 3 · 2025: 2
- FWCI
- 1.27
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- 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
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