The DOI matches its Crossref record; 109 of the 109 references it cites were found in a registry or an index.
Small Proteins Can No Longer Be Ignored
Open accessAbstract
Small proteins, here defined as proteins of 50 amino acids or fewer in the absence of processing, have traditionally been overlooked due to challenges in their annotation and biochemical detection. In the past several years, however, increasing numbers of small proteins have been identified either through the realization that mutations in intergenic regions are actually within unannotated small protein genes or through the discovery that some small, regulatory RNAs encode small proteins. These insights, together with comparative sequence analysis, indicate that tens if not hundreds of small proteins are synthesized in a given organism. This review summarizes what has been learned about the functions of several of these bacterial small proteins, most of which act at the membrane, illustrating the astonishing range of processes in which these small proteins act and suggesting several general conclusions. Important questions for future studies of these overlooked proteins are also discussed.
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.
Integrity signals
Registry
Cites
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.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The cited source says what the claim attributes to it.
In the citing paper
“However, growing experimental evidence in mycobacteria and other prokaryotes has shown that many sproteins are functional, requiring a rethinking of gene definitions (71–75).”
From Mycobacterium smegmatis: The Vanguard of Mycobacterial Research (2023) · cites this paper as [71]
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
Regulation by Small RNAs in Bacteria: Expanding Frontiers
Storz, G., Vogel, J., & Wassarman, K. M. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.08.022 · Cited by 1,181
Self-citationSTRUCTURE AND FUNCTION OF PHOTOSYSTEMS I AND II
Nelson, N., & Yocum, C. F. (2006) · Annual Review of Plant Biology · doi:10.1146/annurev.arplant.57.032905.105350 · Cited by 1,039
Some like it hot: the structure and function of small heat-shock proteins
Haslbeck, M., Franzmann, T. M., Weinfurtner, D., & Büchner, J. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb993 · Cited by 858
Mathematical models of infectious disease transmission
Grassly, N. C., & Fraser, C. (2008) · Nature Reviews Microbiology · doi:10.1038/nrmicro1845 · Cited by 766
Phenotypic Landscape of a Bacterial Cell
Nichols, R. J., Sen, Ś., Choo, Y. J., Beltrão, P., Zietek, M., Chaba, R., Lee, S., Kazmierczak, K. M., Lee, K. J., Wong, A., et al. (2010) · Cell · doi:10.1016/j.cell.2010.11.052 · Cited by 723
Robinson, N. J., & Winge, D. R. (2010) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-030409-143539 · Cited by 722
Proto-genes and de novo gene birth
Carvunis, A.-R., Rolland, T., Wapinski, I., Calderwood, M. A., Yildirim, M. A., Simonis, N., Charloteaux, B., Hidalgo, C. A., Barbette, J., Santhanam, B., et al. (2012) · Nature · doi:10.1038/nature11184 · Cited by 669
MOLECULAR GENETICS OF SPORULATION IN BACILLUS SUBTILIS
Stragier, P., & Losick, R. M. (1996) · Annual Review of Genetics · doi:10.1146/annurev.genet.30.1.297 · Cited by 647
FtsZ in Bacterial Cytokinesis: Cytoskeleton and Force Generator All in One
Erickson, H., Anderson, D. E., & Osawa, M. (2010) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00021-10 · Cited by 646
The anti-Shine–Dalgarno sequence drives translational pausing and codon choice in bacteria
Li, G., Oh, E., & Weissman, J. S. (2012) · Nature · doi:10.1038/nature10965 · Cited by 644
Research works printed but not linked: 2
- Natl. Cent. Biotechnol. 2011. What kind of data can be submitted to GenBank? In GenBank Submissions Handbook, Natl. Cent. Biotechnol., Bethesda, Md.http://www.ncbi.nlm.nih.gov/books/NBK53707/
- Waters LS, 2011, The Escherichia coli, 193, 5887
Cited by
Sorted by citations
Items 101–200 of 359
The small protein floodgates are opening; now the functional analysis begins
Ramamurthi, K. S., & Storz, G. (2014) · BMC Biology · doi:10.1186/s12915-014-0096-y · Cited by 37
Self-citationsmORFer: a modular algorithm to detect small ORFs in prokaryotes
Bartholomäus, A., Kolte, B., Mustafayeva, A., Goebel, I., Fuchs, S., Benndorf, D., Engelmann, S., & Ignatova, Z. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab477 · Cited by 36
Selenoprotein S: A versatile disordered protein
Ghelichkhani, F., Gonzalez, F. A., Kapitonova, M. A., Schaefer‐Ramadan, S., Liu, J., Cheng, R., & Rozovsky, S. (2022) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2022.109427 · Cited by 36
Are Antisense Proteins in Prokaryotes Functional?
Ardern, Z., Neuhaus, K., & Scherer, S. (2020) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2020.00187 · Cited by 36
Role of LncRNAs in regulating cancer amino acid metabolism
Guo, Y., Lv, B., Liu, R., Dai, Z., Zhang, F., Liang, Y., Yu, B., Zeng, D., Lv, X., & Zhang, Z. (2021) · Cancer Cell International · doi:10.1186/s12935-021-01926-8 · Cited by 35
Posttranslational insertion of small membrane proteins by the bacterial signal recognition particle.
Steinberg, R., Origi, A., Natriashvili, A., Sarmah, P., Licheva, M., Walker, P. M., Kraft, C., High, S., Luirink, J., Shi, W. Q., et al. (2020) · PLOS Biology · doi:10.1371/journal.pbio.3000874 · Cited by 34
A catalog of small proteins from the global microbiome
Duan, Y., Júnior, C. D. S., Schmidt, T., Fullam, A., de Almeida, B. L. S., Zhu, C., Kuhn, M., Zhao, X., Bork, P., & Coelho, L. P. (2024) · Nature Communications · doi:10.1038/s41467-024-51894-6 · Cited by 36
Wicke, L., Ponath, F., Coppens, L., Gerovac, M., Lavigne, R., & Vogel, J. (2020) · RNA Biology · doi:10.1080/15476286.2020.1827785 · Cited by 33
Small proteins in bacteria – Big challenges in prediction and identification
Fuchs, S., & Engelmann, S. (2023) · PROTEOMICS · doi:10.1002/pmic.202200421 · Cited by 34
Neuhaus, K., Landstorfer, R., Fellner, L., Simon, S., Schafferhans, A., Goldberg, T., Marx, H., Ozoline, O. N., Rost, B., Küster, B., et al. (2016) · BMC Genomics · doi:10.1186/s12864-016-2456-1 · Cited by 33
You, J., Sun, L., Yang, X., Pan, X., Huang, Z., Zhang, X., Gong, M., Fan, Z., Li, L., Cui, X., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-04232-6 · Cited by 33
Dual-function AzuCR RNA modulates carbon metabolism
Raina, M., Aoyama, J. J., Bhatt, S., Paul, B. J., Zhang, A., Updegrove, T. B., Miranda‐Ríos, J., & Storz, G. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2117930119 · Cited by 33
Self-citationHidden in plain sight: challenges in proteomics detection of small ORF-encoded polypeptides
Fijałkowski, I., Willems, P. J., Jonckheere, V., Simoens, L., & Damme, P. V. (2022) · microLife · doi:10.1093/femsml/uqac005 · Cited by 33
Adaptor proteins in long noncoding RNA biology
Dangelmaier, E. A., & Lal, A. (2019) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2019.03.003 · Cited by 32
Zanker, D. J., Oveissi, S., Tscharke, D. C., Duan, M., Wan, S., Zhang, X., Xiao, K., Mifsud, N. A., Gibbs, J. S., Izzard, L., et al. (2019) · The Journal of Immunology · doi:10.4049/jimmunol.1900070 · Cited by 32
Mechanism of d-alanine transfer to teichoic acids shows how bacteria acylate cell envelope polymers
Schultz, B. J., Snow, E. D., & Walker, S. (2023) · Nature Microbiology · doi:10.1038/s41564-023-01411-0 · Cited by 36
Comparative Genomic Analysis of Holospora spp., Intranuclear Symbionts of Paramecia
Garushyants, S. K., Beliavskaia, A. Y., Malko, D. B., Logacheva, M. D., Rautian, M. S., & Gelfand, M. S. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.00738 · Cited by 31
Kaulich, P. T., Cassidy, L., Weidenbach, K., Schmitz, R. A., & Tholey, A. (2020) · PROTEOMICS · doi:10.1002/pmic.202000084 · Cited by 31
Brandenburg, F., & Klähn, S. (2020) · Life · doi:10.3390/life10120322 · Cited by 31
Proteoforms expand the world of microproteins and short open reading frame-encoded peptides
Cassidy, L., Kaulich, P. T., & Tholey, A. (2023) · iScience · doi:10.1016/j.isci.2023.106069 · Cited by 32
First description of small proteins encoded by spRNAs in Methanosarcina mazei strain Gö1
Prasse, D., Thomsen, J. K., Santis, R. D., Muntel, J., Becher, D., & Schmitz, R. A. (2015) · Biochimie · doi:10.1016/j.biochi.2015.04.007 · Cited by 31
Hücker, S. M., Ardern, Z., Goldberg, T., Schafferhans, A., Bernhofer, M., Vestergaard, G., Nelson, C. W., Schloter, M., Rost, B., Scherer, S., et al. (2017) · PLoS ONE · doi:10.1371/journal.pone.0184119 · Cited by 31
Neuhaus, K., Landstorfer, R., Simon, S., Schober, S., Wright, P. R., Smith, C., Backofen, R., Wecko, R., Keim, D. A., & Scherer, S. (2017) · BMC Genomics · doi:10.1186/s12864-017-3586-9 · Cited by 30
Comparative Proteomics Enables Identification of Nonannotated Cold Shock Proteins in E. coli
D’Lima, N. G., Khitun, A., Rosenbloom, A. D., Yuan, P., Gassaway, B. M., Barber, K. W., Rinehart, J., & Slavoff, S. A. (2017) · Journal of Proteome Research · doi:10.1021/acs.jproteome.7b00419 · Cited by 30
Evolution and adaptation of single-pass transmembrane proteins
Pogozheva, I. D., & Lomize, A. L. (2017) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2017.11.002 · Cited by 30
Choe, D., Szubin, R., Dahesh, S., Cho, S., Nizet, V., Palsson, B. Ø., & Cho, B. (2018) · Scientific Reports · doi:10.1038/s41598-018-20661-1 · Cited by 30
Frumkin, I., & Laub, M. T. (2023) · Nature Ecology & Evolution · doi:10.1038/s41559-023-02224-4 · Cited by 30
Kristiansen, K. I., Weel-Sneve, R., Booth, J. A., & Bjørås, M. (2016) · RNA · doi:10.1261/rna.058461.116 · Cited by 30
Comparative Membrane Proteomics Reveals a Nonannotated E. coli Heat Shock Protein
Yuan, P., D’Lima, N. G., & Slavoff, S. A. (2017) · Biochemistry · doi:10.1021/acs.biochem.7b00864 · Cited by 30
Fei, J., & Sharma, C. M. (2018) · Microbiology Spectrum · doi:10.1128/microbiolspec.rwr-0024-2018 · Cited by 35
Kubatova, N., Pyper, D. J., Jonker, H. R. A., Saxena, K., Remmel, L., Richter, C. P., Brantl, S., Evguenieva‐Hackenberg, E., Hess, W. R., Klug, G., et al. (2019) · ChemBioChem · doi:10.1002/cbic.201900677 · Cited by 29
devIIs an Evolutionarily Young Negative Regulator of Myxococcus xanthus Development
Rajagopalan, R. M., Wielgoss, S., Lippert, G., Velicer, G. J., & Kroos, L. (2015) · Journal of Bacteriology · doi:10.1128/jb.02542-14 · Cited by 28
Gopalkrishnan, S., Ross, W., Chen, A. Y., & Gourse, R. L. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1704105114 · Cited by 28
Nagel, C., Machulla, A., Zahn, S., & Soppa, J. (2019) · Genes · doi:10.3390/genes10050361 · Cited by 28
Gutt, M., Jordan, B., Weidenbach, K., Gudzuhn, M., Kießling, C., Cassidy, L., Helbig, A. O., Tholey, A., Pyper, D. J., Kubatova, N., et al. (2021) · FEBS Journal · doi:10.1111/febs.15799 · Cited by 28
Hadjeras, L., Bartel, J., Maier, L., Maaß, S., Vogel, V., Svensson, S. L., Eggenhofer, F., Gelhausen, R., Müller, T., Alkhnbashi, O. S., et al. (2023) · microLife · doi:10.1093/femsml/uqad001 · Cited by 28
Quest for Orthologs in the Era of Biodiversity Genomics
Langschied, F., Bordin, N., Cosentino, S., Fuentes-Palacios, D., Glover, N., Hiller, M., Hu, Y., Huerta-Cepas, J., Coelho, L. P., Iwasaki, W., et al. (2024) · Genome Biology and Evolution · doi:10.1093/gbe/evae224 · Cited by 26
de Alvarenga, L. V., Hess, W. R., & Hagemann, M. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.01445 · Cited by 27
Grützner, J., Billenkamp, F., Spanka, D.-T., Rick, T., Monzon, V., Förstner, K. U., & Klug, G. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab146 · Cited by 26
The Origin(s) of Cell(s): Pre-Darwinian Evolution from FUCAs to LUCA
Tang, S. (2021) · Journal of Molecular Evolution · doi:10.1007/s00239-021-10014-4 · Cited by 26
Tufail, M. A., Jordan, B., Hadjeras, L., Gelhausen, R., Cassidy, L., Habenicht, T., Gutt, M., Hellwig, L., Backofen, R., Tholey, A., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-53008-8 · Cited by 26
Gelhausen, R., Müller, T., Svensson, S. L., Alkhnbashi, O. S., Sharma, C. M., Eggenhofer, F., & Backofen, R. (2021) · Briefings in Bioinformatics · doi:10.1093/bib/bbab549 · Cited by 22
Hadjeras, L., Heiniger, B., Maaß, S., Scheuer, R., Gelhausen, R., Azarderakhsh, S., Barth-Weber, S., Backofen, R., Becher, D., Ahrens, C. H., et al. (2023) · microLife · doi:10.1093/femsml/uqad012 · Cited by 26
Small Peptides as Newcomers in the Control of Drosophila Development
Zanet, J., Chanut-Delalande, H., Plaza, S., & Payre, F. (2016) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/bs.ctdb.2015.11.004 · Cited by 30
Vanderhaeghen, S., Zehentner, B., Scherer, S., Neuhaus, K., & Ardern, Z. (2018) · Scientific Reports · doi:10.1038/s41598-018-35756-y · Cited by 26
Kraus, A., Weskamp, M., Zierles, J., Balzer, M., Busch, R., Eisfeld, J., Lambertz, J., Nowaczyk, M. M., & Narberhaus, F. (2020) · Journal of Bacteriology · doi:10.1128/jb.00309-20 · Cited by 25
Teikari, J. E., Hou, S., Wahlsten, M., Hess, W. R., & Sivonen, K. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.00356 · Cited by 24
Rescue of Escherichia coli auxotrophy by de novo small proteins
Babina, A. M., Surkov, S., Ye, W., Jerlström-Hultqvist, J., Larsson, M., Holmqvist, E., Jemth, P., Andersson, D. I., & Knopp, M. (2023) · eLife · doi:10.7554/elife.78299 · Cited by 24
Bacterial and Cellular RNAs at Work During Listeria Infection
Sesto, N., Koutero, M., & Cossart, P. (2014) · Future Microbiology · doi:10.2217/fmb.14.79 · Cited by 24
Wheat Encodes Small, Secreted Proteins That Contribute to Resistance to Septoria Tritici Blotch
Zhou, B., Benbow, H. R., Brennan, C. J., Arunachalam, C., Karki, S. J., Mullins, E. D., Feechan, A., Burke, J. I., & Doohan, F. M. (2020) · Frontiers in Genetics · doi:10.3389/fgene.2020.00469 · Cited by 24
Unusually Situated Binding Sites for Bacterial Transcription Factors Can Have Hidden Functionality
Haycocks, J. R. J., & Grainger, D. C. (2016) · PLoS ONE · doi:10.1371/journal.pone.0157016 · Cited by 23
Haq, I. U., Müller, P., & Brantl, S. (2020) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2020.00178 · Cited by 22
CdrS Is a Global Transcriptional Regulator Influencing Cell Division in Haloferax volcanii
Liao, Y., Vogel, V., Hauber, S., Bartel, J., Alkhnbashi, O. S., Maaß, S., Schwarz, T. S., Backofen, R., Becher, D., Duggin, I. G., et al. (2021) · mBio · doi:10.1128/mbio.01416-21 · Cited by 22
Small Proteins in Archaea, a Mainly Unexplored World
Weidenbach, K., Gutt, M., Cassidy, L., Chibani, C. M., & Schmitz, R. A. (2021) · Journal of Bacteriology · doi:10.1128/jb.00313-21 · Cited by 25
Jiang, W., Chen, Y., Sun, M.-J., Huang, X. B., Zhang, H., Fu, Z., Wang, J., Zhang, S., Lian, C., Tang, B., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112969 · Cited by 23
Ribosomal Peptides and Small Proteins on the Rise
Scheidler, C. M., Kick, L. M., & Schneider, S. (2019) · ChemBioChem · doi:10.1002/cbic.201800715 · Cited by 23
Longmuir, S., Akhtar, N., & MacNeill, S. A. (2019) · BMC Research Notes · doi:10.1186/s13104-019-4228-x · Cited by 22
The World of Stable Ribonucleoproteins and Its Mapping With Grad-Seq and Related Approaches
Gerovac, M., Vogel, J., & Smirnov, A. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.661448 · Cited by 24
Kreitmeier, M., Ardern, Z., Abele, M., Ludwig, C., Scherer, S., & Neuhaus, K. (2022) · iScience · doi:10.1016/j.isci.2022.103844 · Cited by 25
Hücker, S. M., Vanderhaeghen, S., Abellan-Schneyder, I., Scherer, S., & Neuhaus, K. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.00931 · Cited by 20
Characterization of Three Small Proteins in Brucella abortus Linked to Fucose Utilization
Budnick, J. A., Sheehan, L. M., Kang, L., Michalak, P., & Caswell, C. C. (2018) · Journal of Bacteriology · doi:10.1128/jb.00127-18 · Cited by 20
Lemaire, O. N., Infossi, P., Chaouche, A. A., Espinosa, L., Leimkühler, S., Giudici‐Orticoni, M., Méjean, V., & Iobbi‐Nivol, C. (2018) · Scientific Reports · doi:10.1038/s41598-018-31851-2 · Cited by 20
Landscape of the Dark Transcriptome Revealed Through Re-mining Massive RNA-Seq Data
Li, J., Singh, U., Arendsee, Z. W., & Wurtele, E. S. (2021) · Frontiers in Genetics · doi:10.3389/fgene.2021.722981 · Cited by 18
Ribosomal stalling landscapes revealed by high-throughput inverse toeprinting of mRNA libraries
Seip, B., Sacheau, G., Dupuy, D., & Innis, C. A. (2018) · Life Science Alliance · doi:10.26508/lsa.201800148 · Cited by 19
Mapping Microproteins and ncRNA-Encoded Polypeptides in Different Mouse Tissues
Ni, P., Wang, Z., Wang, B., Wan, J., & Wan, C. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.687748 · Cited by 19
Elucidating the functional roles of prokaryotic proteins using big data and artificial intelligence
Ardern, Z., Chakraborty, S., Lenk, F., & Kaster, A. (2023) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuad003 · Cited by 22
Huang, A. T.-L., Wang, H.-J., Chang, Y.-C., Wang, S.-W., & Hsia, K. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.107836 · Cited by 19
YshB Promotes Intracellular Replication and Is Required for Salmonella Virulence
Bomjan, R., Zhang, M., & Zhou, D. (2019) · Journal of Bacteriology · doi:10.1128/jb.00314-19 · Cited by 18
Exposing the small protein load of bacterial life
Simoens, L., Fijałkowski, I., & Damme, P. V. (2023) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuad063 · Cited by 17
High-throughput discovery of inhibitory protein fragments with AlphaFold
Savinov, A., Swanson, S., Keating, A. E., & Li, G.-W. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2322412122 · Cited by 18
Riboregulators: Fine-Tuning Virulence in Shigella
Fris, M. E., & Murphy, E. R. (2016) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2016.00002 · Cited by 18
Broach, W. H., Weiss, A., & Shaw, L. N. (2016) · Microbial Genomics · doi:10.1099/mgen.0.000065 · Cited by 18
Cao, S., Liu, X., Huang, Y., Yan, Y., Zhou, C., Shao, C., Yang, R., Zhu, W., Du, Z., & Jia, C. (2021) · Communications Biology · doi:10.1038/s42003-021-02759-x · Cited by 18
Okrent, R. A., Trippe, K. M., Maselko, M., & Manning, V. A. (2016) · Microbiology · doi:10.1099/mic.0.000418 · Cited by 18
Varadarajan, A. R., Götze, S., Pavlou, M. P., Grosboillot, V., Shen, Y., Loessner, M. J., Ahrens, C. H., & Wollscheid, B. (2020) · Journal of Proteome Research · doi:10.1021/acs.jproteome.9b00842 · Cited by 18
HRIBO: high-throughput analysis of bacterial ribosome profiling data
Gelhausen, R., Svensson, S. L., Froschauer, K., Heyl, F., Hadjeras, L., Sharma, C. M., Eggenhofer, F., & Backofen, R. (2020) · Bioinformatics · doi:10.1093/bioinformatics/btaa959 · Cited by 17
AssessORF: combining evolutionary conservation and proteomics to assess prokaryotic gene predictions
Korandla, D. R., Wozniak, J. M., Campeau, A., Gonzalez, D. J., & Wright, E. S. (2019) · Bioinformatics · doi:10.1093/bioinformatics/btz714 · Cited by 16
Melior, H., Maaß, S., Li, S., Förstner, K. U., Azarderakhsh, S., Varadarajan, A. R., Stötzel, M., Elhossary, M., Barth-Weber, S., Ahrens, C. H., et al. (2020) · mBio · doi:10.1128/mbio.01027-20 · Cited by 16
Small membrane proteins – elucidating the function of the needle in the haystack
Kemp, G., & Cymer, F. (2014) · Biological Chemistry · doi:10.1515/hsz-2014-0213 · Cited by 16
The dev Operon Regulates the Timing of Sporulation during Myxococcus xanthus Development
Rajagopalan, R. M., & Kroos, L. (2017) · Journal of Bacteriology · doi:10.1128/jb.00788-16 · Cited by 15
Olvera, M. R., Vivès, É., Molle, V., Blanc‐Potard, A., & Gannoun-Zaki, L. (2017) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2017.00115 · Cited by 15
Vassallo, A., Palazzotto, E., Renzone, G., Botta, L., Faddetta, T., Scaloni, A., Puglia, A. M., & Gallo, G. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.00224 · Cited by 15
Melior, H., Maaß, S., Stötzel, M., Li, S., Förstner, K. U., Schütz, R., Azarderakhsh, S., Shevkoplias, A., Barth-Weber, S., Varadarajan, A. R., et al. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab093 · Cited by 15
The pseudo-atomic structure of an RND-type tripartite multidrug efflux pump
Du, D., Voss, J. E., Wang, Z., Chiu, W., & Luisi, B. F. (2015) · Biological Chemistry · doi:10.1515/hsz-2015-0118 · Cited by 14
Sibling sRNA RyfA1 Influences Shigella dysenteriae Pathogenesis
Fris, M. E., Broach, W. H., Klim, S. E., Coschigano, P. W., Carroll, R. K., Caswell, C. C., & Murphy, E. R. (2017) · Genes · doi:10.3390/genes8020050 · Cited by 14
SR7 – a dual-function antisense RNA from Bacillus subtilis
Haq, I. U., Müller, P., & Brantl, S. (2020) · RNA Biology · doi:10.1080/15476286.2020.1798110 · Cited by 14
Proteomics‐driven identification of short open reading frame‐encoded peptides
Zhang, Z., Li, Y., Yuan, W., Wang, Z., & Wan, C. (2022) · PROTEOMICS · doi:10.1002/pmic.202100312 · Cited by 15
Tailoring regulatory components for metabolic engineering in cyanobacteria
Bolay, P., Dodge, N., Janssen, K., Jensen, P. E., & Lindberg, P. (2024) · Physiologia Plantarum · doi:10.1111/ppl.14316 · Cited by 13
Workflow for a Computational Analysis of an sRNA Candidate in Bacteria
Wright, P. R., & Georg, J. (2018) · Methods in molecular biology · doi:10.1007/978-1-4939-7634-8_1 · Cited by 13
Microproteins: from behind the scenes to the spotlight
Jiang, M., Lou, H., & Hou, W. (2021) · Genome Instability & Disease · doi:10.1007/s42764-021-00040-3 · Cited by 12
Hartford, C. C. R., Shrestha, R. L., Pongor, L. S., Zhao, Y., Chen, X., Fromont, C., Chaudhary, R., Li, X. L., Pasterczyk, K. R., Kumar, R. S., et al. (2022) · Molecular and Cellular Biology · doi:10.1128/mcb.00289-22 · Cited by 13
Identification and validation of novel small proteins in Pseudomonas putida
Yang, X., Jensen, S. I., Wulff, T., Harrison, S. J., & Long, K. S. (2016) · Environmental Microbiology Reports · doi:10.1111/1758-2229.12473 · Cited by 13
Tantoso, E., Eisenhaber, B., Sinha, S., Jensen, L. J., & Eisenhaber, F. (2023) · Biology Direct · doi:10.1186/s13062-023-00362-0 · Cited by 13
Alternative Reading Frames are an Underappreciated Source of Protein Sequence Novelty
Ardern, Z. (2023) · Journal of Molecular Evolution · doi:10.1007/s00239-023-10122-3 · Cited by 15
Meier‐Credo, J., Heiniger, B., Schori, C., Rupprecht, F., Michel, H., Ahrens, C. H., & Langer, J. D. (2023) · Analytical Chemistry · doi:10.1021/acs.analchem.3c00676 · Cited by 12
Jaunbocus, N., Ebenki, V., Su, H., & Slavoff, S. A. (2025) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-080124-012840 · Cited by 18
Widespread Antisense Transcription in Prokaryotes
Georg, J., & Hess, W. R. (2018) · ASM Press eBooks · doi:10.1128/9781683670247.ch12 · Cited by 13
Shankar, M., Hossain, M. S., & Biswas, I. (2017) · Journal of Bacteriology · doi:10.1128/jb.00847-16 · Cited by 11
Zahn, S., Kubatova, N., Pyper, D. J., Cassidy, L., Saxena, K., Tholey, A., Schwalbe, H., & Soppa, J. (2020) · FEBS Journal · doi:10.1111/febs.15559 · Cited by 12
Flipping the switch: dynamic modulation of membrane transporter activity in bacteria
Elston, R., Mulligan, C., & Thomas, G. H. (2023) · Microbiology · doi:10.1099/mic.0.001412 · Cited by 13
Metadata
- Authors
- Storz, G., Wolf, Y. I., & Ramamurthi, K. S.
- Affiliations
- National Institutes of Health (US)
- Corresponding author
- Storz, Gisela
- Ramamurthi, Kumaran S.
- Venue
- Annual Review of Biochemistry
- Publisher
- Annual Reviews
- Published
- 2014-06-02
- Volume
- 83
- Issue
- 1
- Pages
- 753-777
- ISSN
- 0066-4154 (ISSN-L)
- 1545-4509
- PMC
- PMC4166647
- OpenAlex
- W2121350645
- Cited by
- 359
- References
- 108
- Citations by year
- 2026: 19 · 2025: 27 · 2024: 32 · 2023: 37 · 2022: 22 · 2021: 46 · 2020: 41 · 2019: 29 · 2018: 38 · 2017: 28 · 2016: 24 · 2015: 11 · 2014: 4
- FWCI
- 2.96
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Annual Review of Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health (Z99 LM999999)
- National Cancer Institute (ZIABC011211)
- National Institute of Child Health and Human Development
- U.S. National Library of Medicine
- Eunice Kennedy Shriver National Institute of Child Health and Human Development (ZIAHD008855)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Phylogenetic Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
- Keywords
- small proteins, small regulatory RNAs, protein annotation, membrane proteins, sequence comparison, protein function
- MeSH terms
- Amino Acids, Animals, Bacillus subtilis, Bacterial Proteins, Bacteriophages, Cell Division, Codon, Drosophila, Escherichia coli, Protein Kinases, Proteins, Ribosomes, RNA, Signal Transduction, Open Reading Frames, Computational Biology
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