91

αB-crystallin inhibits amyloidogenesis by disassembling aggregation nuclei
Tkachenko, O., Benesch, J.L.P., Baldwin, A.J.
BioRxiv

90

Analysis of αB-crystallin polydispersity in soluation through native micorfludicid electrophoresis
Wright, M.A., Ruggeri, F.S., Saar, K.L., Challa, P.K., Benesch, J.L.P., Knowles, T.P.J.
Analyst, (2019),144, 4413-4424
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89

HspB1 phosphorylation regulates its intramolecular dynamics and mechanosensitive molecular chaperone interaction with filamin C
Collier, M., Alderson, T.R., de Villiers, C., Nicholls, D., Gastall, H., Allison, T., Degiacomi, M., Fuerst, D., van de Ven, P., Djinovic-Carugo, K., Baldwin, A., Watkins, H., Gehmlich, K., Benesch, J.L.P.
Science Advances, (2019), 5, eeaav8421
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BioRxiv

88

An ultra-stable gold-coordinated protein cage displaying reversible assembly
Malay, A.D., Miyazaki, N., Biela, A., Chakraoborti, S., Majesterkiewicz, K., Stupka, I., Kaplan, C.S., Kowalczyk, A., Piette, B.M.A.G., Hochberg, G.K.A., Wu, D., Wrobel, T.P., Fineberg, A., Kushwah, M.S., Klemen, M., Vavpetic, P., Pelicon, P., Kukura, P., Benesch, J.L.P., Iwasaki, K., Heddle, J.G.
Nature, (2019), 569, 438-42
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87

Local unfolding of the HSP27 monomer regulates chaperone activity
Alderson, T.R., Roche, J., Gastall, H.Y., Pritišanac, I., Ying, J., Bax, A., Benesch, J.L.P., Baldwin, A.J.
Nature Communications, (2019), 10, 1068
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BioRxiv doi:10.1101/345751

86

jbc_ryan_cover
Structural and Functional Consequences of Age-Related Isomerization in α Crystallins
Lyon, Y., Collier, M.P, Riggs, D., Degiacomi, M.T, Benesch, J.L.P, Julian, R.
Journal of Biological Chemistry, (2019), 294,7546-55
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BioRxiv

85

Small heat shock proteins: multifaceted proteins with important implications for life
Carra, S., Albert, S., Benesch J.L.P., Boelens, W., Buchner, J., Carver, J.A., Cecconi, C., Ecroyd, H., Gusev, N., Hightower, L.E., Klevit, R.E., Lee, H.O., Liberek, K., Lockwood, B., Poletti, A., Timmerman, V., Toth, M.E., Vierling, E., Wu, T., Tanguay, R.M.
Cell Stress Chaperones (2019), 24, 295-308
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84

X0959440X
Weighing-up protein dynamics: the combination of native mass spectrometry and molecular dynamics simulations
Marklund, E.G., Benesch, J.L.P.
Current Opinion in Structural Biology, (2019), 54, 50-8
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83

Recommendations for reporting ion mobility mass spectrometry measurements
Gablica, V., Shvartsburg, A.A., Afonso, C., Barran, P.E., Benesch, J.L.P., Bleiholder, C., Bowers, M., Bilbao, A., Bush, M.F., Campbell, J.L., Campuzano, I.D.G., Causon, T.J., Clowers, B.H., Creaser, C., De Pauw, E., Far, J., Fernandez-Lima, F., Fjelsted, J.C., Giles, K., Groessl, M., Hogan, C.J.Jr., Hann, S., Kim, H.I., Kurulugama, R.T., May, J.C., McLean, J.A., Pagel, K., Richardson, K., Ridgeway, M.E., Rosu, F., Sobott, F., Thalassinos, K., Valentine, S.J., Wyttenbach, T.
Mass Spectrometry Reviews, (2019), 38, 291-320
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ChemRXiv

82

Probing the dissociation of protein complexes by means of gas-phase H/D exchange mass spectrometry
Mistarz, U.H. , Chandler, S.A., Brown, J.M., Benesch, J.L.P., Rand, K.D.
Journal of the American Society for Mass Spectrometry, (2019), 30, 45-57
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81

JBC_cover
It takes a dimer to tango: Oligomeric small heat-shock proteins dissociate to capture substrate
Santhanagopalan, I., Degiacomi, M.T., Sheperd, D.A., Hochberg, G.K.A., Benesch, J.L.P., Vierling, E.
Journal of Biological Chemistry, (2018), 293, 19511-21
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bioRxiv