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Size-Distribution Analysis of Macromolecules by Sedimentation Velocity Ultracentrifugation and Lamm Equation Modeling
Open accessAbstract
A new method for the size-distribution analysis of polymers by sedimentation velocity analytical ultracentrifugation is described. It exploits the ability of Lamm equation modeling to discriminate between the spreading of the sedimentation boundary arising from sample heterogeneity and from diffusion. Finite element solutions of the Lamm equation for a large number of discrete noninteracting species are combined with maximum entropy regularization to represent a continuous size-distribution. As in the program CONTIN, the parameter governing the regularization constraint is adjusted by variance analysis to a predefined confidence level. Estimates of the partial specific volume and the frictional ratio of the macromolecules are used to calculate the diffusion coefficients, resulting in relatively high-resolution sedimentation coefficient distributions c(s) or molar mass distributions c(M). It can be applied to interference optical data that exhibit systematic noise components, and it does not require solution or solvent plateaus to be established. More details on the size-distribution can be obtained than from van Holde-Weischet analysis. The sensitivity to the values of the regularization parameter and to the shape parameters is explored with the help of simulated sedimentation data of discrete and continuous model size distributions, and by applications to experimental data of continuous and discrete protein mixtures.
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Cites
Solving Least Squares Problems
Lawson, C. L., & Hanson, R. J. (1995) · doi:10.1137/1.9781611971217 · Cited by 7,103
Cited by
Zhang, L., Lin, D., Sun, X., Curth, U., Drosten, C., Sauerhering, L., Becker, S., Rox, K., & Hilgenfeld, R. (2020) · Science · doi:10.1126/science.abb3405 · Cited by 2,895
G3BP1 is a tunable switch that triggers phase separation to assemble stress granules
Yang, P., Mathieu, C., Kolaitis, R.-M., Zhang, P., Messing, J., Yurtsever, U., Yang, Z., Wu, J., Li, Y., Pan, Q., et al. (2020) · Cell · doi:10.1016/j.cell.2020.03.046 · Cited by 1,249
Discovery of the once-weekly glucagon-like peptide-1 (GLP-1) analogue semaglutide
Lau, J., Bloch, P., Schäffer, L., Pettersson, I., Spetzler, J., Kofoed, J., Madsen, K., Knudsen, L. B., McGuire, J., Steensgaard, D. B., et al. (2015) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b00726 · Cited by 1,105
Cas1–Cas2 complex formation mediates spacer acquisition during CRISPR–Cas adaptive immunity
Nuñez, J. K., Kranzusch, P. J., Noeske, J., Wright, A. V., Davies, C. W., & Doudna, J. A. (2014) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2820 · Cited by 458
Structural basis of CpG and inhibitory DNA recognition by Toll-like receptor 9
Ohto, U., Shibata, T., Tanji, H., Ishida, H., Krayukhina, E., Uchiyama, S., Miyake, K., & Shimizu, T. (2015) · Nature · doi:10.1038/nature14138 · Cited by 377
Estimating the effective density of engineered nanomaterials for in vitro dosimetry
DeLoid, G., Cohen, J. M., Darrah, T., Derk, R., Rojanasakul, L., Pyrgiotakis, G., Wohlleben, W., & Demokritou, P. (2014) · Nature Communications · doi:10.1038/ncomms4514 · Cited by 327
Structural basis of indisulam-mediated RBM39 recruitment to DCAF15 E3 ligase complex
Bussiere, D. E., Xie, L., Srinivas, H., Shu, W., Burke, A., Be, C., Zhao, J., Godbole, A., King, D., Karki, R. G., et al. (2020) · Nature Chemical Biology · doi:10.1038/s41589-019-0411-6 · Cited by 257
Conrady, D. G., Brescia, C. C., Horii, K., Weiss, A. A., Hassett, D. J., & Herr, A. B. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0807717105 · Cited by 216
A protein fold switch joins the circadian oscillator to clock output in cyanobacteria
Chang, Y.-G., Cohen, S. E., Phong, C., Myers, W. K., Kim, Y.-I., Tseng, R., Lin, J., Zhang, L., Boyd, J. S., Lee, Y., et al. (2015) · Science · doi:10.1126/science.1260031 · Cited by 212
Structure of the nucleotide exchange factor eIF2B reveals mechanism of memory-enhancing molecule
Tsai, J. C., Miller-Vedam, L. E., Anand, A. A., Jaishankar, P., Nguyen, H. C., Renslo, A. R., Frost, A., & Walter, P. (2018) · Science · doi:10.1126/science.aaq0939 · Cited by 192
Kabe, Y., Nakane, T., Koike, I., Yamamoto, T., Sugiura, Y., Harada, E., Sugase, K., Shimamura, T., Ohmura, M., Muraoka, K., et al. (2016) · Nature Communications · doi:10.1038/ncomms11030 · Cited by 171
Modulation of the Hsp90 Chaperone Cycle by a Stringent Client Protein
Lorenz, O. R., Freiburger, L., Rutz, D. A., Krause, M., Zierer, B. K., Alvira, S., Cuéllar, J., Valpuesta, J. M., Madl, T., Sattler, M., et al. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.02.003 · Cited by 151
Increased Immune Activation by Pathologic α‐Synuclein in Parkinson's Disease
Grozdanov, V., Bousset, L., Hoffmeister, M., Bliederhaeuser, C., Meier, C., Madiona, K., Pieri, L., Kiechle, M., McLean, P. J., Kassubek, J., et al. (2019) · Annals of Neurology · doi:10.1002/ana.25557 · Cited by 161
Effects of Syringe Material and Silicone Oil Lubrication on the Stability of Pharmaceutical Proteins
Krayukhina, E., Tsumoto, K., Uchiyama, S., & Fukui, K. (2015) · Journal of Pharmaceutical Sciences · doi:10.1002/jps.24184 · Cited by 158
Srivastava, A., Gangnard, S., Round, A., Dechavanne, S., Juillerat, A., Raynal, B., Faure, G., Baron, B., Ramboarina, S., Singh, S. K., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1000951107 · Cited by 149
Burnham, B., Nass, S., Kong, E., Mattingly, M., Woodcock, D., Song, A., Wadsworth, S., Cheng, S. H., Scaria, A., & O'Riordan, C. R. (2015) · Human Gene Therapy Methods · doi:10.1089/hgtb.2015.048 · Cited by 150
Conformation of the HIV-1 Gag Protein in Solution
Datta, S. A. K., Curtis, J. E., Ratcliff, W., Clark, P. K., Crist, R. M., Lebowitz, J., Krueger, S., & Rein, A. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.10.073 · Cited by 145
HFE and Transferrin Directly Compete for Transferrin Receptor in Solution and at the Cell Surface
Giannetti, A. M., & Björkman, P. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m401467200 · Cited by 143
Defining α-synuclein species responsible for Parkinson’s disease phenotypes in mice
Froula, J. M., Castellana-Cruz, M., Anabtawi, N. M., Camino, J. D., Chen, S. W., Thrasher, D. R., Freire, J., Yazdi, A. A., Fleming, S., Dobson, C. M., et al. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.007743 · Cited by 129
Zanier, K., ould M'hamed ould Sidi, A., Boulade-Ladame, C., Rybin, V., Chappelle, A., Atkinson, A., Kieffer, B., & Travé, G. (2012) · Structure · doi:10.1016/j.str.2012.02.001 · Cited by 125
Atg38 is required for autophagy-specific phosphatidylinositol 3-kinase complex integrity
Araki, Y., Ku, W.-C., Akioka, M., May, A. I., Hayashi, Y., Arisaka, F., Ishihama, Y., & Ohsumi, Y. (2013) · Journal of Cell Biology · doi:10.1083/jcb.201304123 · Cited by 119
Self-association of human apolipoprotein E3 and E4 in the presence and absence of phospholipid
Perugini, M. A., Schuck, P., & Howlett, G. J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m005565200 · Cited by 118
Self-citationMechanism mediating oligomeric Aβ clearance by naïve primary microglia
Yang, C.-N., Shiao, Y.-J., Shie, F.-S., Guo, B.-S., Chen, P.-H., Cho, C.-Y., Chen, Y.-J., Huang, F.-L., & Tsay, H.-J. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.01.005 · Cited by 117
Functional Dissection of Osteoprotegerin and Its Interaction with Receptor Activator of NF-κB Ligand
Schneeweis, L. A., Willard, D., & Milla, M. E. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506366200 · Cited by 116
Amino-terminal domain stability mediates apolipoprotein E aggregation into neurotoxic fibrils
Hatters, D. M., Zhong, N., Rutenber, E., & Weisgraber, K. H. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.06.080 · Cited by 105
Wang, C., Mulagapati, S. H. R., Chen, Z., Du, J., Zhao, X., Xi, G., Chen, L., Linke, T., Gao, C., Schmelzer, A. E., et al. (2019) · Molecular Therapy - Methods & Clinical Development · doi:10.1016/j.omtm.2019.09.006 · Cited by 105
Bonten, E. J., Campos, Y., Zaitsev, V., Nourse, A., Waddell, B., Lewis, W., Taylor, G., & d'Azzo, A. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.031419 · Cited by 87
Structure of PDE3A-SLFN12 complex reveals requirements for activation of SLFN12 RNase
Garvie, C. W., Wu, X., Papanastasiou, M., Lee, S., Fuller, J., Schnitzler, G. R., Horner, S. W., Baker, A., Zhang, T., Mullahoo, J. P., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-24495-w · Cited by 85
Steensgaard, D. B., Schluckebier, G., Strauss, H. M., Norrman, M., Thomsen, J. K., Friderichsen, A. V., Havelund, S., & Jonassen, I. (2013) · Biochemistry · doi:10.1021/bi3008609 · Cited by 86
Allosteric Inhibition of Human Immunodeficiency Virus Integrase
Gupta, K., Brady, T., Dyer, B. M., Malani, N., Hwang, Y., Male, F., Nolte, R. T., Wang, L., Velthuisen, E., Jeffrey, J., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.551119 · Cited by 81
Fu, X., Chen, W.-C., Argento, C., Clarner, P., Bhatt, V., Dickerson, R., Bou-Assaf, G., Bakhshayeshi, M., Lu, X., Bergelson, S., et al. (2019) · Human Gene Therapy Methods · doi:10.1089/hgtb.2019.088 · Cited by 77
Determining crystal structures through crowdsourcing and coursework
Horowitz, S., Koepnick, B., Martin, R., Tymieniecki, A., Winburn, A. A., Cooper, S., Flatten, J., Rogawski, D. S., Koropatkin, N. M., Hailu, T. T., et al. (2016) · Nature Communications · doi:10.1038/ncomms12549 · Cited by 75
Tran, N. T., Lecomte, E., Saleun, S., Namkung, S., Robin, C., Weber, K., Devine, E., Blouin, V., Adjali, O., Ayuso, E., et al. (2022) · Human Gene Therapy · doi:10.1089/hum.2022.050 · Cited by 74
Brautigam, C. A., Wynn, R. M., Chuang, J. L., & Chuang, D. T. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m806563200 · Cited by 70
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Gupta, K., Turkki, V., Sherrill-Mix, S., Hwang, Y., Eilers, G., Taylor, L., McDanal, C., Wang, P., Temelkoff, D., Nolte, R. T., et al. (2016) · PLOS Biology · doi:10.1371/journal.pbio.1002584 · Cited by 68
The Association−Dissociation Behavior of the ApoE Proteins: Kinetic and Equilibrium Studies
Garai, K., & Frieden, C. (2010) · Biochemistry · doi:10.1021/bi101407m · Cited by 67
Chou, C.-Y., Lin, Y.-L., Huang, Y.-C., Sheu, S.-Y., Lin, T.-H., Tsay, H.-J., Chang, G.-G., & Shiao, M.-S. (2005) · Biophysical Journal · doi:10.1529/biophysj.104.046813 · Cited by 66
Gabrielson, J. P., Arthur, K. K., Stoner, M. R., Winn, B. C., Kendrick, B. S., Razinkov, V., Svitel, J., Jiang, Y., Voelker, P. J., Fernandes, C. A., et al. (2010) · Analytical Biochemistry · doi:10.1016/j.ab.2009.09.036 · Cited by 56
Melo, G. B., Figueira, A. C. M., Batista, F. A. H., Filho, A. A. S. L., Rodrigues, E. B., Belfort, R., & Maia, M. (2019) · Ophthalmic Surgery, Lasers and Imaging Retina · doi:10.3928/23258160-20190503-05 · Cited by 51
Analysis of High-Affinity Binding of Protein Kinase R to Double-Stranded RNA
Husain, B., Mukerji, I., & Cole, J. L. (2012) · Biochemistry · doi:10.1021/bi301226h · Cited by 51
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Deka, R. K., Brautigam, C. A., Tomson, F. L., Lumpkins, S. B., Tomchick, D. R., Machius, M., & Norgard, M. V. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m610215200 · Cited by 50
Lenoir, M., Ustunel, C., Rajesh, S., Kaur, J., Moreau, D., Gruenberg, J., & Overduin, M. (2018) · Nature Communications · doi:10.1038/s41467-018-03370-1 · Cited by 49
HIV-1 matrix-tRNA complex structure reveals basis for host control of Gag localization
Bou-Nader, C., Muecksch, F., Brown, J. B., Gordon, J. M., York, A., Peng, C., Ghirlando, R., Summers, M. F., Bieniasz, P. D., & Zhang, J. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2021.07.006 · Cited by 48
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Lizatović, R., Aurelius, O., Stenström, O., Drakenberg, T., Akke, M., Logan, D. T., & André, I. (2016) · Structure · doi:10.1016/j.str.2016.03.027 · Cited by 48
Raulin, A.-C., Kraft, L., Al-Hilaly, Y. K., Xue, W.-F., McGeehan, J. E., Atack, J. R., & Serpell, L. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.04.019 · Cited by 47
Structural and functional variations in human apolipoprotein E3 and E4.
Chou, C.-Y., Jen, W.-P., Hsieh, Y.-H., Shiao, M.-S., & Chang, G.-G. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m511077200 · Cited by 46
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Dörner, K., Gut, M. J., Overwijn, D., Cao, F., Siketanc, M., Heinrich, S., Beuret, N., Meyer, J., Sharpe, T., Lindorff-Larsen, K., et al. (2026) · EMBO Reports · doi:10.1038/s44319-025-00626-y · Cited by 45
A switch point in the molecular chaperone Hsp90 responding to client interaction
Rutz, D. A., Luo, Q., Freiburger, L., Madl, T., Kaila, V. R. I., Sattler, M., & Buchner, J. (2018) · Nature Communications · doi:10.1038/s41467-018-03946-x · Cited by 37
Ca2+-stabilized adhesin helps an Antarctic bacterium reach out and bind ice.
Vance, T. D. R., Olijve, L. L. C., Campbell, R. L., Voets, I. K., Davies, P. L., & Guo, S. (2014) · Bioscience Reports · doi:10.1042/bsr20140083 · Cited by 40
Jensen, J. K., Dolmer, K., Schar, C., & Gettins, P. G. W. (2009) · Biochemical Journal · doi:10.1042/bj20090175 · Cited by 39
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Pitsawong, W., Pádua, R. A. P., Grant, T., Hoemberger, M., Otten, R., Bradshaw, N., Grigorieff, N., & Kern, D. (2023) · Nature · doi:10.1038/s41586-023-05836-9 · Cited by 37
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Nowak, E., Miller, J. T., Bona, M. K., Studnicka, J., Szczepanowski, R. H., Jurkowski, J., Le Grice, S. F. J., & Nowotny, M. (2014) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2785 · Cited by 31
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Davies, J. S., Currie, M. J., North, R. A., Scalise, M., Wright, J. D., Copping, J. M., Remus, D. M., Gulati, A., Morado, D. R., Jamieson, S. A., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-36590-1 · Cited by 34
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Fu, J., Li, S., Guan, H., Li, C., Zhao, Y.-B., Chen, T.-T., Xian, W., Zhang, Z., Liu, Y., Guan, Q., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-50311-2 · Cited by 34
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Ngoei, K. R. W., Catimel, B., Church, N., Lio, D. S., Dogovski, C., Perugini, M. A., Watt, P. M., Cheng, H.-C., Ng, D. C. H., & Bogoyevitch, M. A. (2011) · Biochemical Journal · doi:10.1042/bj20101244 · Cited by 31
Urano, F., Hayashi, N., Arisaka, F., Kurita, H., Murata, S., & Ichinose, H. (2006) · The Journal of Biochemistry · doi:10.1093/jb/mvj073 · Cited by 30
Keppel, T. R., Sarpong, K., Murray, E. M., Monsey, J., Zhu, J., & Bose, R. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.747485 · Cited by 29
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
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Tsirigotaki, A., Dansercoer, A., Verschueren, K. H. G., Marković, I., Pollmann, C., Hafer, M., Felix, J., Birck, C., Van Putte, W., Catteeuw, D., et al. (2023) · Nature Structural & Molecular Biology · doi:10.1038/s41594-023-00941-9 · Cited by 29
Lst4, the yeast Fnip1/2 orthologue, is a DENN-family protein
Pacitto, A., Ascher, D. B., Wong, L. H., Blaszczyk, B. K., Nookala, R. K., Zhang, N., Dokudovskaya, S., Levine, T. P., & Blundell, T. L. (2015) · Open Biology · doi:10.1098/rsob.150174 · Cited by 28
Yamamoto, K., Ishibashi, O., Sugiura, K., Ubatani, M., Sakaguchi, M., Nakatsuji, M., Shimamoto, S., Noda, M., Uchiyama, S., Fukutomi, Y., et al. (2019) · Scientific Reports · doi:10.1038/s41598-018-38134-w · Cited by 27
Ton motor conformational switch and peptidoglycan role in bacterial nutrient uptake
Zinke, M., Lejeune, M., Mechaly, A., Bardiaux, B., Boneca, I. G., Delepelaire, P., & Izadi-Pruneyre, N. (2024) · Nature Communications · doi:10.1038/s41467-023-44606-z · Cited by 27
Wachnowsky, C., Wesley, N. A., Fidai, I., & Cowan, J. A. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.01.021 · Cited by 25
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Seraphim, T. V., Gava, L. M., Mokry, D. Z., Cagliari, T. C., Barbosa, L. R. S., Ramos, C. H. I., & Borges, J. C. (2015) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2014.10.015 · Cited by 27
Manna, A., Zhao, H., Wada, J., Balagopalan, L., Tagad, H. D., Appella, E., Schuck, P., & Samelson, L. E. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1817142115 · Cited by 24
Self-citationLaroussi, H., Juarez‐Martinez, A. B., Le Roy, A., Boeri Erba, E., Gabel, F., de Massy, B., & Kadlec, J. (2023) · The EMBO Journal · doi:10.15252/embj.2023113866 · Cited by 22
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Skořepa, O., Pazicky, S., Kalousková, B., Bláha, J., Abreu, C., Ječmen, T., Rosůlek, M., Fish, A., Sedivy, A., Harlos, K., et al. (2020) · Cancers · doi:10.3390/cancers12071998 · Cited by 21
Gupta, K., Allen, A., Giraldo, C., Eilers, G., Sharp, R., Hwang, Y., Murali, H., Cruz, K., Janmey, P., Bushman, F., et al. (2021) · Structure · doi:10.1016/j.str.2020.12.001 · Cited by 19
“…(Humphrey et al., 1996)) https://www.ks.uiuc.edu/Research/vmd/ Mantidplot Mantid Project https://download.mantidproject.org/ SEDFIT (Schuck, 2000) http://www.analyticalultracentrifugation.com/ download.htm SEDPHAT (Vistica et al., 2004) http://www.analyticalultracentrifugation.com/…”
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Cho, E. J., Doh, K.-O., Park, J., Hyun, H., Wilson, E. M., Snyder, P. W., Tsifansky, M. D., & Yeo, Y. (2016) · Scientific Reports · doi:10.1038/srep29739 · Cited by 18
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Zhou, X., Zhang, H., Wang, Y., Wang, D., Lin, Z., Zhang, Y., Tang, Y., Liu, J., Yao, Y.-F., Zhang, Y., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-58432-y · Cited by 17
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Consalvo, C. D., Aderounmu, A. M., Donelick, H. M., Aruscavage, P. J., Eckert, D. M., Shen, P. S., & Bass, B. L. (2024) · eLife · doi:10.7554/elife.93979.3 · Cited by 12
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Bravo-Plaza, I., Tagua, V. G., Arst, H. N., Alonso, A., Pinar, M., Monterroso, B., Galindo, A., & Peñalva, M. A. (2023) · eLife · doi:10.7554/elife.85079 · Cited by 10
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Webb, J. A., Farrow, E., Cain, B., Yuan, Z., Yarawsky, A. E., Schoch, E., Gagliani, E. K., Herr, A. B., Gebelein, B., & Kovall, R. A. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae522 · Cited by 7
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Yarawsky, A. E., Dinu, V., Harding, S. E., & Herr, A. B. (2023) · European Biophysics Journal · doi:10.1007/s00249-023-01648-x · Cited by 7
Frampton, S. L., Sutcliffe, C., Baldock, C., & Ashe, H. L. (2022) · Biology Open · doi:10.1242/bio.059199 · Cited by 5
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Metadata
- Authors
- Schuck, P.
- Venue
- Biophysical Journal
- Publisher
- Elsevier BV
- Published
- 2000-03
- Volume
- 78
- Issue
- 3
- Pages
- 1606-1619
- ISSN
- 0006-3495 (ISSN-L)
- OpenAlex
- W1975317507
- Cited by
- 3,868
- References
- 1
- FWCI
- 8.22
- Type
- journal article
- Language
- en
- Open access
- bronze
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.