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The PRIDE database and related tools and resources in 2019: improving support for quantification data
Open accessAbstract
The PRoteomics IDEntifications (PRIDE) database (https://www.ebi.ac.uk/pride/) is the world's largest data repository of mass spectrometry-based proteomics data, and is one of the founding members of the global ProteomeXchange (PX) consortium. In this manuscript, we summarize the developments in PRIDE resources and related tools since the previous update manuscript was published in Nucleic Acids Research in 2016. In the last 3 years, public data sharing through PRIDE (as part of PX) has definitely become the norm in the field. In parallel, data re-use of public proteomics data has increased enormously, with multiple applications. We first describe the new architecture of PRIDE Archive, the archival component of PRIDE. PRIDE Archive and the related data submission framework have been further developed to support the increase in submitted data volumes and additional data types. A new scalable and fault tolerant storage backend, Application Programming Interface and web interface have been implemented, as a part of an ongoing process. Additionally, we emphasize the improved support for quantitative proteomics data through the mzTab format. At last, we outline key statistics on the current data contents and volume of downloads, and how PRIDE data are starting to be disseminated to added-value resources including Ensembl, UniProt and Expression Atlas.
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Items 101–200 of 251
Starkl, P., Watzenboeck, M. L., Popov, L. M., Zahalka, S., Hladik, A., Lakovits, K., Radhouani, M., Haschemi, A., Marichal, T., Reber, L. L., et al. (2020) · Immunity · doi:10.1016/j.immuni.2020.08.002 · Cited by 59
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So, J., Mabe, N. W., Englinger, B., Chow, K.-H., Moyer, S. M., Yerrum, S., Trissal, M. C., Marques, J. G., Kwon, J. J., Shim, B., et al. (2022) · JCI Insight · doi:10.1172/jci.insight.158755 · Cited by 45
Quantitative phosphoproteomics uncovers dysregulated kinase networks in Alzheimer’s disease
Morshed, N., Lee, M. J., Rodriguez, F. H., Lauffenburger, D. A., Mastroeni, D., & White, F. M. (2021) · Nature Aging · doi:10.1038/s43587-021-00071-1 · Cited by 58
Unexpected complexity of the ammonia monooxygenase in archaea
(2023) · doi:10.1038/s41396-023-01367-3 · Cited by 58
Suo, M., Rommelfanger, M. K., Chen, Y., Amro, E. M., Han, B., Chen, Z., Szafranski, K., Chakkarappan, S. R., Boehm, B. O., MacLean, A. L., et al. (2022) · Blood · doi:10.1182/blood.2021012197 · Cited by 57
Neuropathy-causing TRPV4 mutations disrupt TRPV4-RhoA interactions and impair neurite extension
McCray, B. A., Diehl, E., Sullivan, J. M., Aisenberg, W. H., Zaccor, N. W., Lau, A. R., Rich, D. J., Goretzki, B., Hellmich, U. A., Lloyd, T. E., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-21699-y · Cited by 57
Structural insights into perilipin 3 membrane association in response to diacylglycerol accumulation
Choi, Y. M., Ajjaji, D., Fleming, K. D., Borbat, P. P., Jenkins, M. L., Moeller, B. E., Fernando, S., Bhatia, S. R., Freed, J. H., Burke, J. E., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-38725-w · Cited by 57
The Neurolipid Atlas: a lipidomics resource for neurodegenerative diseases
Feringa, F. M., Koppes-den Hertog, S. J., Wang, L. Y., Derks, R. J. E., Kruijff, I., Erlebach, L., Heijneman, J., Miramontes, R., Pömpner, N., Blomberg, N., et al. (2025) · Nature Metabolism · doi:10.1038/s42255-025-01365-z · Cited by 56
Reuter, L., Schmidt, T., Manishankar, P., Throm, C., Keicher, J., Bock, A., Droste-Borel, I., & Oecking, C. (2021) · Nature Communications · doi:10.1038/s41467-021-26332-6 · Cited by 56
Began, J., Cordier, B., Březinová, J., Delisle, J., Hexnerová, R., Srb, P., Rampírová, P., Kožíšek, M., Baudet, M., Couté, Y., et al. (2020) · The EMBO Journal · doi:10.15252/embj.2019102935 · Cited by 55
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Akter, F., Ponnaiyan, S., Kögler-Mohrbacher, B., Bleibaum, F., Damme, M., Renard, B. Y., & Winter, D. (2020) · doi:10.1101/2020.12.21.423747 · Cited by 55
The final step of 40S ribosomal subunit maturation is controlled by a dual key lock
Plassart, L., Shayan, R., Montellese, C., Rinaldi, D., Larburu, N., Pichereaux, C., Froment, C., Lebaron, S., O'Donohue, M.-F., Kutay, U., et al. (2021) · eLife · doi:10.7554/elife.61254 · Cited by 55
Camões, S. P., Bulut, O., Yazar, V., Gaspar, M. M., Simões, S., Ferreira, R., Vitorino, R., Santos, J. M., Gursel, I., & Miranda, J. P. (2022) · Journal of Advanced Research · doi:10.1016/j.jare.2022.01.013 · Cited by 55
A deeper look at carrier proteome effects for single-cell proteomics
Ye, Z., Batth, T. S., Rüther, P., & Olsen, J. V. (2022) · Communications Biology · doi:10.1038/s42003-022-03095-4 · Cited by 55
Krauspe, V., Fahrner, M., Spät, P., Steglich, C., Frankenberg-Dinkel, N., Maček, B., Schilling, O., & Hess, W. R. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2012277118 · Cited by 54
Oxidized thioredoxin-1 restrains the NLRP1 inflammasome
(2022) · doi:10.1126/sciimmunol.abm7200 · Cited by 53
Adriaenssens, E., Schaar, S., Cook, A. S. I., Stuke, J. F. M., Sawa-Makarska, J., Nguyen, T. N., Ren, X., Schuschnig, M., Romanov, J., Khuu, G., et al. (2025) · Nature Cell Biology · doi:10.1038/s41556-025-01712-y · Cited by 53
Pathogen protein modularity enables elaborate mimicry of a host phosphatase
Li, H., Wang, J., Kuan, T. A., Tang, B., Feng, L., Wang, J., Cheng, Z., Skłenar, J., Derbyshire, P., Hulin, M., et al. (2023) · Cell · doi:10.1016/j.cell.2023.05.049 · Cited by 53
Schnirch, L., Nadler-Holly, M., Siao, S.-W., Frese, C. K., Viner, R., & Liu, F. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.0c01273 · Cited by 53
Structure of Anabaena flos-aquae gas vesicles revealed by cryo-ET
Dutka, P., Metskas, L. A., Hurt, R. C., Salahshoor, H., Wang, T.-Y., Malounda, D., Lu, G. J., Chou, T.-F., Shapiro, M. G., & Jensen, G. J. (2023) · Structure · doi:10.1016/j.str.2023.03.011 · Cited by 51
Deconstructing Methanosarcina acetivorans into an acetogenic archaeon
Schöne, C., Poehlein, A., Jehmlich, N., Adlung, N., Daniel, R., von Bergen, M., Scheller, S., & Rother, M. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2113853119 · Cited by 51
Shuffled ATG8 interacting motifs form an ancestral bridge between UFMylation and autophagy
Picchianti, L., Sánchez de Medina Hernández, V., Zhan, N., Irwin, N. A., Groh, R., Stephani, M., Hornegger, H., Beveridge, R., Sawa‐Makarska, J., Lendl, T., et al. (2023) · The EMBO Journal · doi:10.15252/embj.2022112053 · Cited by 50
ApoC-III is a novel inducer of calcification in human aortic valves
Schlotter, F., de Freitas, R. C. C., Rogers, M. A., Blaser, M. C., Wu, P.-J., Higashi, H., Halu, A., Iqbal, F., Andraski, A. B., Rodia, C. N., et al. (2021) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.015700 · Cited by 49
Hounslow, E., Evans, C. A., Pandhal, J., Sydney, T., Couto, N., Pham, T. K., Gilmour, D. J., & Wright, P. C. (2021) · Biotechnology for Biofuels · doi:10.1186/s13068-021-01970-6 · Cited by 49
H3K4me2 regulates the recovery of protein biosynthesis and homeostasis following DNA damage
Wang, S., Meyer, D. H., & Schumacher, B. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-00513-1 · Cited by 49
Magli, A., Baik, J., Pota, P., Cordero, C. O., Kwak, I.-Y., Garry, D. J., Love, P. E., Dynlacht, B. D., & Perlingeiro, R. C. R. (2019) · Nature Communications · doi:10.1038/s41467-019-10318-6 · Cited by 47
Gerovac, M., El Mouali, Y., Kuper, J., Kisker, C., Barquist, L., & Vogel, J. (2020) · RNA · doi:10.1261/rna.076992.120 · Cited by 47
The TRIM9/TRIM67 neuronal interactome reveals novel activators of morphogenesis
Menon, S., Goldfarb, D., Ho, C. T., Cloer, E. W., Boyer, N. P., Hardie, C., Bock, A. J., Johnson, E. C., Anil, J., Major, M. B., et al. (2021) · Molecular Biology of the Cell · doi:10.1091/mbc.e20-10-0622 · Cited by 46
van Oostrum, M., Campbell, B., Seng, C., Müller, M., tom Dieck, S., Hammer, J., Pedrioli, P. G. A., Földy, C., Tyagarajan, S. K., & Wollscheid, B. (2020) · Nature Communications · doi:10.1038/s41467-020-18494-6 · Cited by 46
Distinct gene clusters drive formation of ferrosome organelles in bacteria
Grant, C. R., Amor, M., Trujillo, H. A., Krishnapura, S., Iavarone, A. T., & Komeili, A. (2022) · Nature · doi:10.1038/s41586-022-04741-x · Cited by 45
Co-occurrence of Fe and P stress in natural populations of the marine diazotroph Trichodesmium
Held, N. A., Webb, E. A., McIlvin, M. M., Hutchins, D. A., Cohen, N. R., Moran, D. M., Kunde, K., Lohan, M. C., Mahaffey, C., Woodward, E. M. S., et al. (2020) · Biogeosciences · doi:10.5194/bg-17-2537-2020 · Cited by 45
Kamrad, S., Grossbach, J., Rodríguez‐López, M., Mülleder, M., Townsend, S., Cappelletti, V., Stojanovski, G., Correia‐Melo, C., Picotti, P., Beyer, A., et al. (2020) · Molecular Systems Biology · doi:10.15252/msb.20199270 · Cited by 40
Jauss, B., Petriman, N.-A., Drepper, F., Franz, L., Sachelaru, I., Welte, T., Steinberg, R., Warscheid, B., & Koch, H.-G. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.010686 · Cited by 43
Enrichment and identification of small proteins in a simplified human gut microbiome
Petruschke, H., Anders, J., Stadler, P. F., Jehmlich, N., & von Bergen, M. (2020) · Journal of Proteomics · doi:10.1016/j.jprot.2019.103604 · Cited by 43
Skin exposure to UVB light induces a skin-brain-gonad axis and sexual behavior
Parikh, R., Sorek, E., Parikh, S., Michael, K., Bikovski, L., Tshori, S., Shefer, G., Mingelgreen, S., Zornitzki, T., Knobler, H., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109579 · Cited by 42
Peptide Correlation Analysis (PeCorA) Reveals Differential Proteoform Regulation
Dermit, M., Peters-Clarke, T. M., Shishkova, E., & Meyer, J. G. (2021) · Journal of Proteome Research · doi:10.1021/acs.jproteome.0c00602 · Cited by 40
Structure and dynamics of the essential endogenous mycobacterial polyketide synthase Pks13
Kim, S. K., Dickinson, M. S., Finer-Moore, J., Guan, Z., Kaake, R. M., Echeverria, I., Chen, J., Pulido, E. H., Sali, A., Krogan, N. J., et al. (2023) · Nature Structural & Molecular Biology · doi:10.1038/s41594-022-00918-0 · Cited by 41
Omenn, G. S., Lane, L., Overall, C. M., Corrales, F. J., Schwenk, J. M., Paik, Y.-K., Van Eyk, J. E., Liu, S., Pennington, S., Snyder, M. P., et al. (2019) · Journal of Proteome Research · doi:10.1021/acs.jproteome.9b00434 · Cited by 40
Anti‐tumor effects of PIM/PI3K/mTOR triple kinase inhibitor IBL‐302 in neuroblastoma
Mohlin, S., Hansson, K., Radke, K., Martinez, S., Blanco‐Apiricio, C., Garcia‐Ruiz, C., Welinder, C., Esfandyari, J., O'Neill, M., Pastor, J., et al. (2019) · EMBO Molecular Medicine · doi:10.15252/emmm.201810058 · Cited by 40
Gerovac, M., Wicke, L., Chihara, K., Schneider, C., Lavigne, R., & Vogel, J. (2021) · mBio · doi:10.1128/mbio.03454-20 · Cited by 40
Mitochondrial matrix RTN4IP1/OPA10 is an oxidoreductase for coenzyme Q synthesis
Park, I., Kim, K.-E., Kim, J., Kim, A.-K., Bae, S., Jung, M., Choi, J., Mishra, P. K., Kim, T.-M., Kwak, C., et al. (2024) · Nature Chemical Biology · doi:10.1038/s41589-023-01452-w · Cited by 39
Jackson-Litteken, C. D., Di Venanzio, G., Le, N.-H., Scott, N. E., Djahanschiri, B., Distel, J. S., Pardue, E. J., Ebersberger, I., & Feldman, M. F. (2022) · mBio · doi:10.1128/mbio.00258-22 · Cited by 38
A conserved cysteine‐based redox mechanism sustains TFEB/HLH‐30 activity under persistent stress
Martina, J. A., Guerrero‐Gómez, D., Gómez‐Orte, E., Antonio Bárcena, J., Cabello, J., Miranda‐Vizuete, A., & Puertollano, R. (2021) · The EMBO Journal · doi:10.15252/embj.2020105793 · Cited by 37
A modified TurboID approach identifies tissue-specific centriolar components in C. elegans
Holzer, E., Rumpf-Kienzl, C., Falk, S., & Dammermann, A. (2022) · PLOS Genetics · doi:10.1371/journal.pgen.1010150 · Cited by 37
Decros, G., Beauvoit, B., Colombié, S., Cabasson, C., Bernillon, S., Arrivault, S., Guenther, M., Belouah, I., Prigent, S., Baldet, P., et al. (2019) · Frontiers in Plant Science · doi:10.3389/fpls.2019.01201 · Cited by 35
Structural mechanism for inhibition of PP2A-B56α and oncogenicity by CIP2A
Pavic, K., Gupta, N., Omella, J. D., Derua, R., Aakula, A., Huhtaniemi, R., Määttä, J. A., Höfflin, N., Okkeri, J., Wang, Z., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-36693-9 · Cited by 36
So, Y.-S., Lee, D.-G., Idnurm, A., Ianiri, G., & Bahn, Y.-S. (2019) · Genetics · doi:10.1534/genetics.119.302191 · Cited by 36
smORFer: 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
THEM6‐mediated reprogramming of lipid metabolism supports treatment resistance in prostate cancer
Blomme, A., Peter, C., Mui, E., Rodriguez Blanco, G., An, N., Mason, L. M., Jamieson, L. E., McGregor, G. H., Lilla, S., Ntala, C., et al. (2022) · EMBO Molecular Medicine · doi:10.15252/emmm.202114764 · Cited by 36
Walker, E. J., Bettinger, J. Q., Welle, K. A., Hryhorenko, J. R., Molina Vargas, A. M., O’Connell, M. R., & Ghaemmaghami, S. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.101872 · Cited by 35
Yu, R., Vorontsov, E., Sihlbom, C., & Nielsen, J. (2021) · eLife · doi:10.7554/elife.65722 · Cited by 35
Salovska, B., Li, W., Di, Y., & Liu, Y. (2021) · Analytical Chemistry · doi:10.1021/acs.analchem.0c04293 · Cited by 35
Profiling the Proteome-Wide Selectivity of Diverse Electrophiles
Zanon, P. R. A., Yu, F., Musacchio, P., Lewald, L., Zollo, M., Krauskopf, K., Mrdović, D., Raunft, P., Maher, T. E., Cigler, M., et al. (2021) · doi:10.26434/chemrxiv.14186561.v1 · Cited by 35
Aggregation and disaggregation features of the human proteome
Määttä, T. A., Rettel, M., Sridharan, S., Helm, D., Kurzawa, N., Stein, F., & Savitski, M. M. (2020) · Molecular Systems Biology · doi:10.15252/msb.20209500 · Cited by 34
A cyclin-dependent kinase-mediated phosphorylation switch of disordered protein condensation
Valverde, J. M., Dubra, G., Phillips, M., Haider, A., Elena-Real, C., Fournet, A., Alghoul, E., Chahar, D., Andrés-Sanchez, N., Paloni, M., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-42049-0 · Cited by 33
Caudal, A., Tang, X., Chavez, J. D., Keller, A., Mohr, J. P., Bakhtina, A. A., Villet, O., Chen, H., Zhou, B., Walker, M. A., et al. (2022) · Nature Cardiovascular Research · doi:10.1038/s44161-022-00127-4 · Cited by 33
Garcia, G., Fernandes, A., Stein, F., & Brites, D. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.833066 · Cited by 32
Van houcke, J., Mariën, V., Zandecki, C., Ayana, R., Pepermans, E., Boonen, K., Seuntjens, E., Baggerman, G., & Arckens, L. (2023) · npj Regenerative Medicine · doi:10.1038/s41536-023-00304-4 · Cited by 29
Harnessing Machine Learning To Unravel Protein Degradation in Escherichia coli
Nagar, N., Ecker, N., Loewenthal, G., Avram, O., Ben-Meir, D., Biran, D., Ron, E., & Pupko, T. (2021) · mSystems · doi:10.1128/msystems.01296-20 · Cited by 31
Cardiopoietic stem cell therapy restores infarction-altered cardiac proteome
Arrell, D. K., Rosenow, C. S., Yamada, S., Behfar, A., & Terzic, A. (2020) · npj Regenerative Medicine · doi:10.1038/s41536-020-0091-6 · Cited by 30
CRYPTOCHROMES promote daily protein homeostasis
Wong, D. C. S., Seinkmane, E., Zeng, A., Stangherlin, A., Rzechorzek, N. M., Beale, A. D., Day, J., Reed, M., Peak‐Chew, S. Y., Styles, C. T., et al. (2022) · The EMBO Journal · doi:10.15252/embj.2021108883 · Cited by 30
Nemergut, M., Marques, S. M., Uhrik, L., Vanova, T., Nezvedova, M., Gadara, D. C., Jha, D., Tulis, J., Novakova, V., Planas-Iglesias, J., et al. (2023) · Molecular Neurodegeneration · doi:10.1186/s13024-023-00620-9 · Cited by 30
Zinnall, U., Milek, M., Minia, I., Vieira-Vieira, C. H., Müller, S., Mastrobuoni, G., Hazapis, O.-G., Del Giudice, S., Schwefel, D., Bley, N., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-30322-7 · Cited by 30
Villar-Vesga, J., Henao-Restrepo, J., Voshart, D. C., Aguillon, D., Villegas, A., Castaño, D., Arias-Londoño, J. D., Zuhorn, I. S., Ribovski, L., Barazzuol, L., et al. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.587989 · Cited by 29
Experimental evidence for temporal uncoupling of brain Aβ deposition and neurodegenerative sequelae
Rother, C., Uhlmann, R. E., Müller, S. A., Schelle, J., Skodras, A., Obermüller, U., Häsler, L. M., Lambert, M., Baumann, F., Xu, Y., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-34538-5 · Cited by 28
Peck Justice, S. A., Barron, M. P., Qi, G. D., Wijeratne, H. R. S., Victorino, J. F., Simpson, E. R., Vilseck, J. Z., Wijeratne, A. B., & Mosley, A. L. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.014576 · Cited by 28
Peck Justice, S. A., Qi, G., Wijeratne, H. R. S., Victorino, J. F., Simpson, E. R., Wijeratne, A. B., & Mosley, A. L. (2019) · doi:10.1101/2019.12.30.891267 · Cited by 28
McIlwain, S. J., Wu, Z., Wetzel, M., Belongia, D., Jin, Y., Wenger, K., Ong, I. M., & Ge, Y. (2020) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.0c00035 · Cited by 27
Dorn, G., Gmeiner, C., de Vries, T., Dedic, E., Novakovic, M., Damberger, F. F., Maris, C., Finol, E., Sarnowski, C. P., Kohlbrecher, J., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-42012-z · Cited by 27
Autophagy-mediated metabolic effects of aspirin
Castoldi, F., Humeau, J., Martins, I., Lachkar, S., Loew, D., Dingli, F., Durand, S., Enot, D., Bossut, N., Chery, A., et al. (2020) · Cell Death Discovery · doi:10.1038/s41420-020-00365-0 · Cited by 27
Targeted Quantification of the Lysosomal Proteome in Complex Samples
Mosen, P., Sanner, A., Singh, J., & Winter, D. (2021) · Proteomes · doi:10.3390/proteomes9010004 · Cited by 26
Skowron, M. A., Eul, K., Stephan, A., Ludwig, G. F., Wakileh, G. A., Bister, A., Söhngen, C., Raba, K., Petzsch, P., Poschmann, G., et al. (2022) · Molecular Oncology · doi:10.1002/1878-0261.13282 · Cited by 20
Zhou, M., Malhan, N., Ahkami, A. H., Engbrecht, K., Myers, G., Dahlberg, J., Hollingsworth, J., Sievert, J. A., Hutmacher, R., Madera, M., et al. (2020) · Methods · doi:10.1016/j.ymeth.2019.10.007 · Cited by 23
Evidence for a trap-and-flip mechanism in a proton-dependent lipid transporter
Lambert, E., Mehdipour, A. R., Schmidt, A., Hummer, G., & Perez, C. (2022) · Nature Communications · doi:10.1038/s41467-022-28361-1 · 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
EROS is a selective chaperone regulating the phagocyte NADPH oxidase and purinergic signalling
Randzavola, L. O., Mortimer, P. M., Garside, E., Dufficy, E. R., Schejtman, A., Roumelioti, G., Yu, L., Pardo, M., Spirohn, K., Tolley, C., et al. (2022) · eLife · doi:10.7554/elife.76387 · Cited by 24
Discovery of Protein Modifications Using Differential Tandem Mass Spectrometry Proteomics
Cifani, P., Li, Z., Luo, D., Grivainis, M., Intlekofer, A. M., Fenyö, D., & Kentsis, A. (2021) · Journal of Proteome Research · doi:10.1021/acs.jproteome.0c00638 · Cited by 24
Schumacher, N., Yan, K., Gandraß, M., Müller, M., Krisp, C., Häsler, R., Carambia, A., Nofer, J.-R., Bernardes, J. P., Khouja, M., et al. (2021) · Journal of Hepatology · doi:10.1016/j.jhep.2020.09.021 · Cited by 24
eIF4E1b is a non-canonical eIF4E protecting maternal dormant mRNAs
Lorenzo-Orts, L., Strobl, M., Steinmetz, B., Leesch, F., Pribitzer, C., Roehsner, J., Schutzbier, M., Dürnberger, G., & Pauli, A. (2023) · EMBO Reports · doi:10.1038/s44319-023-00006-4 · Cited by 23
Healy, M. D., Sacharz, J., McNally, K. E., McConville, C., Tillu, V. A., Hall, R. J., Chilton, M., Cullen, P. J., Mobli, M., Ghai, R., et al. (2022) · Structure · doi:10.1016/j.str.2022.10.001 · Cited by 23
Zhang, Z., Hebert, A. S., Westphall, M. S., Coon, J. J., & Dovichi, N. J. (2019) · Journal of Proteome Research · doi:10.1021/acs.jproteome.9b00244 · Cited by 22
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Moreira, A. M., Ferreira, R. M., Carneiro, P., Figueiredo, J., Osório, H., Barbosa, J., Preto, J., Pinto-do-Ó, P., Carneiro, F., & Seruca, R. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.818552 · Cited by 21
Pinho, N., Bombaça, A. C., Wiśniewski, J. R., Dias-Lopes, G., Saboia-Vahia, L., Cupolillo, E., de Jesus, J. B., de Almeida, R. P., Padrón, G., Menna-Barreto, R., et al. (2022) · Antioxidants · doi:10.3390/antiox11020277 · Cited by 21
Durand, S., Bruelle, M., Bourdelais, F., Bennychen, B., Blin-Gonthier, J., Isaac, C., Huyghe, A., Martel, S., Seyve, A., Vanbelle, C., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-36037-7 · Cited by 21
Spatiotemporal processing of neural cell adhesion molecules 1 and 2 by BACE1 in vivo
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Altered Carbon Partitioning Enhances CO2 to Terpene Conversion in Cyanobacteria
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Ceballos-Garzon, A., Monteoliva, L., Gil, C., Alvarez-Moreno, C., Vega-Vela, N. E., Engelthaler, D. M., Bowers, J., Le Pape, P., & Parra-Giraldo, C. M. (2022) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dkab454 · Cited by 18
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Söhngen, C., Thomas, D. J., Skowron, M. A., Bremmer, F., Eckstein, M., Stefanski, A., Driessen, M. D., Wakileh, G. A., Stühler, K., Altevogt, P., et al. (2023) · The FEBS Journal · doi:10.1111/febs.16880 · Cited by 19
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Progressive axonopathy when oligodendrocytes lack the myelin protein CMTM5
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Dynamics of allosteric regulation of the phospholipase C-γ isozymes upon recruitment to membranes
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Metadata
- Authors
- Perez-Riverol, Y., Csordas, A., Bai, J., Bernal-Llinares, M., Hewapathirana, S., Kundu, D. J., Inuganti, A., Griss, J., Mayer, G., Eisenacher, M., Pérez, E., Uszkoreit, J., Pfeuffer, J., Sachsenberg, T., Yılmaz, Ş., Tiwary, S., Cox, J., Audain, E., Walzer, M., Jarnuczak, A. F., Ternent, T., Brazma, A., & Vizcaíno, J. A.
- Venue
- Nucleic Acids Research
- Publisher
- Oxford University Press (OUP)
- Published
- 2018-11-05
- Volume
- 47
- Issue
- D1
- Pages
- D442-D450
- ISSN
- 0305-1048 (ISSN-L)
- 1362-4962
- OpenAlex
- W2899760200
- Cited by
- 6,693
- References
- 0
- FWCI
- 384.44
- Type
- journal article
- Language
- en
- Open access
- gold
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 ›
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Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.