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Aggregation of a Slow-Folding Mutant of a β-Clam Protein Proceeds through a Monomeric Nucleus
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What this work says
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inferred← citeshttps://doi.org/10.1002/pro.615openalex-snapshot
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inferred← citeshttps://doi.org/10.1002/prot.20861openalex-snapshot
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inferred← citeshttps://doi.org/10.1007/978-0-387-68372-0_9openalex-snapshot
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inferred← citeshttps://doi.org/10.1007/978-1-59745-367-7_7openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.abb.2007.08.033openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.abb.2008.10.017openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.bbapap.2010.03.002openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.bpc.2006.09.010openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.bpc.2013.11.005openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.bpj.2008.12.3903openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.colsurfb.2021.111696openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.jmb.2008.03.020openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.jmb.2025.169055openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.plefa.2014.08.001openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.saa.2018.05.083openalex-snapshot
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inferred← citeshttps://doi.org/10.1021/bi101312hopenalex-snapshot
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inferred← citeshttps://doi.org/10.1021/bi401467popenalex-snapshot
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inferred← citeshttps://doi.org/10.1021/bi800002jopenalex-snapshot
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inferred← citeshttps://doi.org/10.1021/jp070212jopenalex-snapshot
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inferred← citeshttps://doi.org/10.1021/jp401586popenalex-snapshot
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inferred← citeshttps://doi.org/10.1021/jp8083088openalex-snapshot
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inferred← citeshttps://doi.org/10.1038/nchembio.2007.49openalex-snapshot
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inferred← citeshttps://doi.org/10.1038/nchembio1005-239openalex-snapshot
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inferred← citeshttps://doi.org/10.1039/b817782aopenalex-snapshot
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inferred← citeshttps://doi.org/10.1039/c2mb25148eopenalex-snapshot
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inferred← citeshttps://doi.org/10.1063/1.2779323openalex-snapshot
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inferred← citeshttps://doi.org/10.1073/pnas.0603772103openalex-snapshot
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inferred← citeshttps://doi.org/10.1073/pnas.0711664105openalex-snapshot
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inferred← citeshttps://doi.org/10.1074/jbc.m511523200openalex-snapshot
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inferred← citeshttps://doi.org/10.1074/jbc.m703682200openalex-snapshot
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inferred← citeshttps://doi.org/10.1074/jbc.m800247200openalex-snapshot
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inferred← citeshttps://doi.org/10.1111/j.1365-2958.2006.05394.xopenalex-snapshot
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inferred← citeshttps://doi.org/10.1371/journal.pone.0022154openalex-snapshot
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inferred← citeshttps://doi.org/10.1385/1-59745-217-3:209openalex-snapshot
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inferred← citeshttps://doi.org/10.4161/pri.3.3.9922openalex-snapshot
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inferred← citeshttps://doi.org/10.7275/1vz6-td16openalex-snapshot
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