Research Articles
114
Dimerisation of European robin crypto chrome 4a
Hanic M., Antill, L., Gehrckens, A., Schmidt, J., Gortemaker, K., Bartolke, R., El-Bab, T., Xu, J., Koch, KW., Mouritsen, H., Benesch, J.L.P., Hore, P., Solov'yov, I.
Journal of Physical Chemistry B, publication pending
Hanic M., Antill, L., Gehrckens, A., Schmidt, J., Gortemaker, K., Bartolke, R., El-Bab, T., Xu, J., Koch, KW., Mouritsen, H., Benesch, J.L.P., Hore, P., Solov'yov, I.
Journal of Physical Chemistry B, publication pending
113
Fortuitously compatible protein surfaces primed allosteric control in Cyanobacteria photo protection
Steube, N., Moldehauer, M., Weiland, P., Saman, D., Kilb, A., Ramirez-Rojas, A.A., Garg, S.G., Grauman, P.L., Benesch, J.L.P., Bange, G., Friedrich, T., Hochberg, G.K.A.
Nature Ecology and Evolution, (2023), 7 (5): 756-767
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Steube, N., Moldehauer, M., Weiland, P., Saman, D., Kilb, A., Ramirez-Rojas, A.A., Garg, S.G., Grauman, P.L., Benesch, J.L.P., Bange, G., Friedrich, T., Hochberg, G.K.A.
Nature Ecology and Evolution, (2023), 7 (5): 756-767
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112
Expansion and Neofunctionalization of Actinoporin-like Genes in Mediterranean Mussels (Mytilus galloprovincialis)
Koritnik, N., Gerdol, M., Solinc, G., Svigelj, T., Caserman, S., Merzel, F., Holden, E., Benesch, J.L.P., Trenti, F., Guella, G., Pallavicini, A., Modica, M.V., Podobnik, M., Anderluh, G.
Genome Biology Evol., (2022), 14 (11): evac151
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Koritnik, N., Gerdol, M., Solinc, G., Svigelj, T., Caserman, S., Merzel, F., Holden, E., Benesch, J.L.P., Trenti, F., Guella, G., Pallavicini, A., Modica, M.V., Podobnik, M., Anderluh, G.
Genome Biology Evol., (2022), 14 (11): evac151
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111
Mass-selective and ice-free cryo-EM protein sample preparation via native electro spray ion-beam deposition.
Esser, T.K., Böhning, K., Fremdling, P., Agasid, M.T., Costin, A., Fort, K., Konijnenberg, A., Gilbert, J.D., Bahm, A., Makarov, A., Robinson, C.V., Benesch, J.L.P., Baker, L., Bharat, T.A.M., Gault, J., Rauschenbach, S.
PNAS Nexus, (2022), 1 (4): pgac153
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Esser, T.K., Böhning, K., Fremdling, P., Agasid, M.T., Costin, A., Fort, K., Konijnenberg, A., Gilbert, J.D., Bahm, A., Makarov, A., Robinson, C.V., Benesch, J.L.P., Baker, L., Bharat, T.A.M., Gault, J., Rauschenbach, S.
PNAS Nexus, (2022), 1 (4): pgac153
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110
Complementing machine learning-based structure predictions with native mass spectrometry
Allison, T.M., Degiacomi, M.T., Marklund, E.G., Jovine, L., Elofsson, A., Benesch, J.L.P., Landreh, M.
Protein Science, (2022), 31 (6): e4333
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Allison, T.M., Degiacomi, M.T., Marklund, E.G., Jovine, L., Elofsson, A., Benesch, J.L.P., Landreh, M.
Protein Science, (2022), 31 (6): e4333
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109
Hyperphosphorylated tau self-assembles into amorphous aggregates eliciting TLR4-dependent responses
Meng, J.X., Zhang, Y., Saman, D., Haider, A.M., De, S., Sang, J.S., Brown, K., Jiang, K., Humphrey, J., Julian, L., Hidari, E., Lee, S.F., Balmus, G., Floto, R.A., Bryant, C.E., Benesch, J.L.P., Ye, Y., Klenerman, D. Nature Communications, (2022), 13: 2692
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Meng, J.X., Zhang, Y., Saman, D., Haider, A.M., De, S., Sang, J.S., Brown, K., Jiang, K., Humphrey, J., Julian, L., Hidari, E., Lee, S.F., Balmus, G., Floto, R.A., Bryant, C.E., Benesch, J.L.P., Ye, Y., Klenerman, D. Nature Communications, (2022), 13: 2692
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108
Shape-morphing of an artificial protein cage with unusual geometry induced by a single amino acid change
Sharma, M., Biela, A.P., Kowalcyk, A., Borzecka-Solarz, K., Piette, P.M.A.G., Gawel, S., Bishop, J., Kukura, P., Benesch, J.L.P., Imamura, M. Scheuring, S., Heddle, J.G.
ACS Nano, (2022)
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Sharma, M., Biela, A.P., Kowalcyk, A., Borzecka-Solarz, K., Piette, P.M.A.G., Gawel, S., Bishop, J., Kukura, P., Benesch, J.L.P., Imamura, M. Scheuring, S., Heddle, J.G.
ACS Nano, (2022)
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107
Biobox: A toolbox for biomolecular modelling
Rudden, S.P.lL., Musson, S.M., Benesch, J.L.P., Degiacomi, M.T
Bioinformatics, (2021), 38(4): 1149-1151
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Rudden, S.P.lL., Musson, S.M., Benesch, J.L.P., Degiacomi, M.T
Bioinformatics, (2021), 38(4): 1149-1151
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106
Charge Engineering Reveals the Roles of Ionizable Side Chains in Electrospray Ionization Mass Spectrometry
Abramsson, M.L., Sahin, C., Hopper, T.S., Branca, R.M.M., Danielsson, J., Xu, M., Chandler, S.A., Westerlund, N., Ilag, L.L., Leppert, A., Costeira-Paulo, J., Lang, L., Teilum, K., Laganoswky, A., Benesch, J.L.P., Oliveberg, M., Robinson, C.V., Marklund, E.G., Allison, T.M., Winther, J.R., Landreh, M.
JACS Au 2021
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Abramsson, M.L., Sahin, C., Hopper, T.S., Branca, R.M.M., Danielsson, J., Xu, M., Chandler, S.A., Westerlund, N., Ilag, L.L., Leppert, A., Costeira-Paulo, J., Lang, L., Teilum, K., Laganoswky, A., Benesch, J.L.P., Oliveberg, M., Robinson, C.V., Marklund, E.G., Allison, T.M., Winther, J.R., Landreh, M.
JACS Au 2021
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104
The binding of the small heat-shock protein aB-crystallin to fibrils of a-synuclein is driven by entropic forces
Scheidt, T., Carozza, J.A., Kolbe, C.C., Aprile, F.A., Tkachenko O., Bellaiche M.M.J., Meisl, G., Peter, Q.A.E., Herling, T.W., Ness, S., Castellana-Cruz, M., Benesch, J.L.P., Vendruscolo, M., Dobson, C.M, Arosio, P., Knowles, T.P.J.
PNAS , (2021), 118 (38) e2108790118
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Scheidt, T., Carozza, J.A., Kolbe, C.C., Aprile, F.A., Tkachenko O., Bellaiche M.M.J., Meisl, G., Peter, Q.A.E., Herling, T.W., Ness, S., Castellana-Cruz, M., Benesch, J.L.P., Vendruscolo, M., Dobson, C.M, Arosio, P., Knowles, T.P.J.
PNAS , (2021), 118 (38) e2108790118
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103
A weakened interface in the P182L variant of HSP27 associated with severe Charcot-Marie-Tooth neuropathy causes aberrant binding to interacting proteins.
Alderson, T.R., Adriaenssens, E., Asselbergh, B., Pritisanac, I., Van Lent, J., Gastall, H.Y., Waelti, M., Louis, J.M., Timmermann, V., Baldwin, A.J., Benesch, J.L.P.
EMBO J, (2021), e103811
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Also a pre-print on BioRxiv
Alderson, T.R., Adriaenssens, E., Asselbergh, B., Pritisanac, I., Van Lent, J., Gastall, H.Y., Waelti, M., Louis, J.M., Timmermann, V., Baldwin, A.J., Benesch, J.L.P.
EMBO J, (2021), e103811
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Also a pre-print on BioRxiv
102
Ion mobility-mass spectrometry shows stepwise protein unfolding under alkaline conditions.
Sahin, C., Westerlund, N., Leppert, A., Johansson, J., Marklund, E., Benesch, J.L.P., Slag, L.L., Allison, T.M., Landreh, M,
Chemical Communications, (2021)
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Sahin, C., Westerlund, N., Leppert, A., Johansson, J., Marklund, E., Benesch, J.L.P., Slag, L.L., Allison, T.M., Landreh, M,
Chemical Communications, (2021)
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101
Single-molecule fluorescence-based approach reveals novel mechanistic insights into human small heat shock protein chaperone function.
Johnston, C.L, Marzano, N.R., Paudel, B.P., Wright, G., Benesch, J.L.P., Van Oijen, A.M., Ecroyd, H.
Journal of Biological Chemistry, (2020)
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Johnston, C.L, Marzano, N.R., Paudel, B.P., Wright, G., Benesch, J.L.P., Van Oijen, A.M., Ecroyd, H.
Journal of Biological Chemistry, (2020)
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100
Software requirements for the analysis and interpretation of native ion mobility mass spectrometry data
Allison, T., Barran, P., Benesch, J.LP., Cianferani, S., Degiacomi, M., Gabelica, V., Grandori R., Marklund, E., Menneteau, T., Migas, L., Politis, A., Sharon, M., Sobott, F., Thalassinos, K.
Analytical Chemistry, (2020), 92(16): 110881-10890
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Allison, T., Barran, P., Benesch, J.LP., Cianferani, S., Degiacomi, M., Gabelica, V., Grandori R., Marklund, E., Menneteau, T., Migas, L., Politis, A., Sharon, M., Sobott, F., Thalassinos, K.
Analytical Chemistry, (2020), 92(16): 110881-10890
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99
Computational strategies and challenges for using native ion mobility mass spectrometry in biophysics and structural biology
Allison, T., Barran, P., Cianferani, S., Degiacomi, M., Gabelica, V., Grandori R., Marklund, E., Menneteau, T., Migas, L., Politis, A., Sharon, M., Sobott, F., Thalassinos, K., Benesch, J.LP.
Analytical Chemistry, (2020), 92(16): 10872-10880
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Allison, T., Barran, P., Cianferani, S., Degiacomi, M., Gabelica, V., Grandori R., Marklund, E., Menneteau, T., Migas, L., Politis, A., Sharon, M., Sobott, F., Thalassinos, K., Benesch, J.LP.
Analytical Chemistry, (2020), 92(16): 10872-10880
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98
Origins of complexity in haemoglobin evolution
Pillai, A.S., Chandler, S.A., Liu, Y., Signore, A.V., Cortez-Romero, C.R., Benesch, J.L.P., Laganowsky, A., Storz, J.F., Hochberg, G.K.A., Thornton, J.W.
Nature, (2020), 581 (7809): 480-485
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Pillai, A.S., Chandler, S.A., Liu, Y., Signore, A.V., Cortez-Romero, C.R., Benesch, J.L.P., Laganowsky, A., Storz, J.F., Hochberg, G.K.A., Thornton, J.W.
Nature, (2020), 581 (7809): 480-485
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97
Quantifying the heterogeneity of macromolecular machines by mass photometry
Sonn-Segev, A., Belacic, K., Bodrug, T., Young, G., VanderLinden R.T., Schulman, B.A., Schimpf, J., Friedrich, T., Vinh Dip, P., Schwartz, T.U., Bauer, B., Peters, J-M., Struwe, W.B., Benesch, J.L.P., Brown, N.G., Haselbach, D., Kukura, P.
Nature communications, (2020), 11(1): 1772
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Sonn-Segev, A., Belacic, K., Bodrug, T., Young, G., VanderLinden R.T., Schulman, B.A., Schimpf, J., Friedrich, T., Vinh Dip, P., Schwartz, T.U., Bauer, B., Peters, J-M., Struwe, W.B., Benesch, J.L.P., Brown, N.G., Haselbach, D., Kukura, P.
Nature communications, (2020), 11(1): 1772
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95
Quantifying protein-protein interactions by molecular counting with mass photometry
Soltermann, F., Foley, E.D.B., Pagnoni, V., Galpin, M.R., Benesch, J.L.P., Kukura, P., Struwe, W.B.
Angewandte Chemie, (2020), 59 (27): 10774-10779
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94
Conditional disorder in small heat-shock proteins
Alderson, T.R., Ying, J., Bax, A., Benesch, J.L.P., Baldwin, AJ.
Journal of Molecular Biology, (2020), 432 (9): 3033-3049
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Alderson, T.R., Ying, J., Bax, A., Benesch, J.L.P., Baldwin, AJ.
Journal of Molecular Biology, (2020), 432 (9): 3033-3049
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93
Monitoring protein-metal binding by 19F NMR - a case study with the New Delhi metallo-ß-lactamase 1 Rydzik, A., Brem, J., Chandler, S.A., Benesch, J.L.P., Claridge, T.D.W., Schofield, C.J.,
RSC Medicinal Chemistry, (2020), 11 (3): 387-391
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RSC Medicinal Chemistry, (2020), 11 (3): 387-391
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92
The trajectory taken by dimeric Cu/Zn superoxide dismutase through the protein unfolding and dissociation landscape is modulated by salt-bridge formation
McAlary, L., Harrison, J.A., Aquilina, J.A., Fitzgerald, S.P., Kelso, C., Benesch, J.L.P., Yerbury, J.J
Analytical Chemistry, (2020), 92 (2), 1702-1711
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McAlary, L., Harrison, J.A., Aquilina, J.A., Fitzgerald, S.P., Kelso, C., Benesch, J.L.P., Yerbury, J.J
Analytical Chemistry, (2020), 92 (2), 1702-1711
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91
αB-crystallin inhibits amyloidogenesis by disassembling aggregation nuclei
Tkachenko, O., Benesch, J.L.P., Baldwin, A.J.
BioRxiv
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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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
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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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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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
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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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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80
Terminal regions confer plasticity to the tetrameric assembly of human HspB2 and HspB3
Clark, A.R., Egberts, W.V., Kondrat, F.D.L., Hilton, G.R., Ray, N.J., Cole, A.R., Carver, J.A., Benesch, J.L.P., Keep, N.H., Boelens, W.C., Slingsby, C.
J. Mol. Biol. (2018) , 430 (18), Part B, 3297-3310
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Clark, A.R., Egberts, W.V., Kondrat, F.D.L., Hilton, G.R., Ray, N.J., Cole, A.R., Carver, J.A., Benesch, J.L.P., Keep, N.H., Boelens, W.C., Slingsby, C.
J. Mol. Biol. (2018) , 430 (18), Part B, 3297-3310
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78
The Jumonji-C oxygenase JMJD7 catalyzes (3S)-lysyl hydroxylation of TRAFAC GTPases
Markolovic, S., Zhuang, Q., Wilkins, S.E., Eaton, C.D., Abboud, M., Katz, M.J., McNeil, H.E., Leśniak, R., Hall, C., Struwe, W.B., Konietzny, R., Davis, S., Yang, M., Ge, W., Benesch, J., Kessler, B., Ratcliffe, P., Cockman, M., Fischer, R., Wappner, P., Chowdhury, R., Coleman, M., Schofield, C.J.
Nat. Chem. Biol. (2018), 14, 688-695
Markolovic, S., Zhuang, Q., Wilkins, S.E., Eaton, C.D., Abboud, M., Katz, M.J., McNeil, H.E., Leśniak, R., Hall, C., Struwe, W.B., Konietzny, R., Davis, S., Yang, M., Ge, W., Benesch, J., Kessler, B., Ratcliffe, P., Cockman, M., Fischer, R., Wappner, P., Chowdhury, R., Coleman, M., Schofield, C.J.
Nat. Chem. Biol. (2018), 14, 688-695
77
Lipid binding attenuates channel closure of the outer membrane protein OmpF
Liko, I., Degiacomi, M.T., Lee, S., Newport, T.D., Gault, J., Reading, E., Hopper, J.T.S., Housden, N.G., White, P., Colledge, M., Sula, A., Wallace, B.A., Kleanthous, C., Stansfeld, P.J., Bayley, H., Benesch, J.L.P., Allison, T.M., and Robinson, C.V.
PNAS (2018), 115 (26), 6691-6696
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Liko, I., Degiacomi, M.T., Lee, S., Newport, T.D., Gault, J., Reading, E., Hopper, J.T.S., Housden, N.G., White, P., Colledge, M., Sula, A., Wallace, B.A., Kleanthous, C., Stansfeld, P.J., Bayley, H., Benesch, J.L.P., Allison, T.M., and Robinson, C.V.
PNAS (2018), 115 (26), 6691-6696
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76
Identifying key membrane protein lipid interactions using mass spectrometry.
Gupta K, Li J, Liko I, Gault J, Bechara C, Wu D, Hopper JTS, Giles K, Benesch JLP, Robinson CV.
Nat. Protoc. (2018) 13 (5), 1106-1120
Gupta K, Li J, Liko I, Gault J, Bechara C, Wu D, Hopper JTS, Giles K, Benesch JLP, Robinson CV.
Nat. Protoc. (2018) 13 (5), 1106-1120
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75
Quantitative mass imaging of single biological macromolecules
Young, G., Hundt, N., Cole, D., Fineberg, A., Andrecka, J., Tyler, A., Olerinyova, A., Ansari, A., Marklund, E.G., Collier, M.P., Chandler, S.A., Tkachenko, O., Allen, J., Crispin, M., Billington, N., Takagi, Y., Sellers, J.R., Eichmann, C., Selenko, P., Frey, L., Riek, R., Galpin, M.R., Struwe, W.B., Benesch, J.L.P., Kukura, P.
Science (2018) 360 (6387), 423-427
Young, G., Hundt, N., Cole, D., Fineberg, A., Andrecka, J., Tyler, A., Olerinyova, A., Ansari, A., Marklund, E.G., Collier, M.P., Chandler, S.A., Tkachenko, O., Allen, J., Crispin, M., Billington, N., Takagi, Y., Sellers, J.R., Eichmann, C., Selenko, P., Frey, L., Riek, R., Galpin, M.R., Struwe, W.B., Benesch, J.L.P., Kukura, P.
Science (2018) 360 (6387), 423-427
74
The influence of the N-terminal region proximal to the core domain on the assembly and chaperone activity of αB-crystallin
Jovcevski, B., Andrew Aquilina, J., Benesch, J.L.P., Ecroyd, H.
Cell Stress Chaperones (2018) doi:10.1007/s12192-018-0889-y
Jovcevski, B., Andrew Aquilina, J., Benesch, J.L.P., Ecroyd, H.
Cell Stress Chaperones (2018) doi:10.1007/s12192-018-0889-y
73
Structural and functional aspects of the interaction partners of the small heat-shock protein in Synechocystis.
Marklund, E.G., Zhang, Y., Basha, E., Benesch, J.L.P., Vierling, E.
Cell Stress and Chaperones (2018) doi:10.1007/s12192-018-0884-3
Marklund, E.G., Zhang, Y., Basha, E., Benesch, J.L.P., Vierling, E.
Cell Stress and Chaperones (2018) doi:10.1007/s12192-018-0884-3
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72
Structural principles that enable oligomeric small heat-shock protein paralogs to evolve distinct functions
Hochberg, G.K.A., Shepherd, D.A., Marklund, E.G., Santhanagoplan, I., Degiacomi, M.T., Laganowsky, A., Allison, T.M., Basha, E., Marty, M.T., Galpin, M.R., Struwe, W.B., Baldwin, A.J., Vierling, E., Benesch, J.L.P.
Science (2018), 359 (6378), 930-935
Hochberg, G.K.A., Shepherd, D.A., Marklund, E.G., Santhanagoplan, I., Degiacomi, M.T., Laganowsky, A., Allison, T.M., Basha, E., Marty, M.T., Galpin, M.R., Struwe, W.B., Baldwin, A.J., Vierling, E., Benesch, J.L.P.
Science (2018), 359 (6378), 930-935
71
Real-Time Intrinsic Fluorescence Visualization and Sizing of Proteins and Protein Complexes in Microfluidic Devices.
Challa, P.K., Peter, Q., Wright, M.A., Zhang, Y., Saar, K.L., Carozza, J.A., Benesch, J.L.P., Knowles, T.P.J.
Anal. Chem. (2018), 90 (6), 3849-3855
Challa, P.K., Peter, Q., Wright, M.A., Zhang, Y., Saar, K.L., Carozza, J.A., Benesch, J.L.P., Knowles, T.P.J.
Anal. Chem. (2018), 90 (6), 3849-3855
70
Mass spectrometry beyond the native state
Chandler, S.A., Benesch, J.L.P.
Curr. Opin. Chem. Biol. (2017), 42, 130-137
Chandler, S.A., Benesch, J.L.P.
Curr. Opin. Chem. Biol. (2017), 42, 130-137
69
Evaluating the Effect of Phosphorylation on the Structure and Dynamics of Hsp27 Dimers by Means of Ion Mobility Mass Spectrometry
Jovcevski, B., Kelly, M.A., Aquilina, J.A., Benesch, J.L.P., Ecroyd, H
Anal. Chem. (2017), 89 (24), 13275-13282
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Jovcevski, B., Kelly, M.A., Aquilina, J.A., Benesch, J.L.P., Ecroyd, H
Anal. Chem. (2017), 89 (24), 13275-13282
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68
Discovery of a Highly Selective Cell-Active Inhibitor of the Histone Lysine Demethylases KDM2/7
Gerken, P.A., Wolstenhulme, J.R., Tumber, A., Hatch, S.B., Zhang, Y., Müller, S., Chandler, S.A., Mair, B., Li, F., Nijman, S.M.B., Konietzny, R., Szommer, T., Yapp, C., Fedorov, O., Benesch, J.L.P., Vedadi, M., Kessler, B.M., Kawamura, A., Brennan, P.E., Smith, M.D.
Angew. Chem. (International ed. in English) (2017), 56 (49), 15555-15559
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Gerken, P.A., Wolstenhulme, J.R., Tumber, A., Hatch, S.B., Zhang, Y., Müller, S., Chandler, S.A., Mair, B., Li, F., Nijman, S.M.B., Konietzny, R., Szommer, T., Yapp, C., Fedorov, O., Benesch, J.L.P., Vedadi, M., Kessler, B.M., Kawamura, A., Brennan, P.E., Smith, M.D.
Angew. Chem. (International ed. in English) (2017), 56 (49), 15555-15559
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67
Adenosine Monophosphate Binding Stabilizes the KTN Domain of the Shewanella denitrificans Kef Potassium Efflux System.
Pliotas, C., Grayer, S.C., Ekkerman, S., Chan, A.K.N., Healy, J., Marius, P., Bartlett, W., Khan, A., Cortopassi, W.A., Chandler, S.A., Rasmussen, T., Benesch, J.L.P., Paton, R.S., Claridge, T.D.W., Miller, S., Booth, I.R., Naismith, J.H., Conway, S.J.
Biochemistry (2017), 56 (32), 4219-4234
Pliotas, C., Grayer, S.C., Ekkerman, S., Chan, A.K.N., Healy, J., Marius, P., Bartlett, W., Khan, A., Cortopassi, W.A., Chandler, S.A., Rasmussen, T., Benesch, J.L.P., Paton, R.S., Claridge, T.D.W., Miller, S., Booth, I.R., Naismith, J.H., Conway, S.J.
Biochemistry (2017), 56 (32), 4219-4234
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66
Accommodating protein dynamics in the modeling of chemical crosslinks
Degiacomi, MT, Schmidt, C, Baldwin, AJ, Benesch, JLP
Structure, (2017), 25, 1-7
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Degiacomi, MT, Schmidt, C, Baldwin, AJ, Benesch, JLP
Structure, (2017), 25, 1-7
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65
Controlling Protein Orientation in Vacuum Using Electric Fields
Marklund E.G., Ekeberg T., Moog M., Benesch J.L.P., Caleman C.
J. Phys. Chem. Lett., (2017), 8 (18), 4540-4544
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Marklund E.G., Ekeberg T., Moog M., Benesch J.L.P., Caleman C.
J. Phys. Chem. Lett., (2017), 8 (18), 4540-4544
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64
Proline isomerization in the C-terminal region of HSP27
Alderson, T.R., Benesch, J.L., Baldwin, A.J.
Cell Stress Chaperones (2017), 22, 639-651
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Alderson, T.R., Benesch, J.L., Baldwin, A.J.
Cell Stress Chaperones (2017), 22, 639-651
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63
The growing world of small heat shock proteins: from structure to functions
Carra, S., Alberti, S., Arrigo, P.A., Benesch, J.L., Benjamin, I.J., Boelens, W., Bartelt-Kirbach, B., Brundel, B.J., Buchner, J., Bukau, B., Carver, J.A., Ecroyd, H., Emanuelsson, C., Finet, S., Golenhofen, N., Goloubinoff, P., Gusev, N., Haslbeck, M., Hightower, L.E., Kampinga, H.H., Klevit, R.E., Liberek, K., Mchaourab, H.S., McMenimen, K.A., Poletti, A., Quinlan, R., Strelkov, S.V., Toth, M.E., Vierling, E., Tanguay, R.M.
Cell Stress Chaperones (2017), 22 (4), 601-611
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Carra, S., Alberti, S., Arrigo, P.A., Benesch, J.L., Benjamin, I.J., Boelens, W., Bartelt-Kirbach, B., Brundel, B.J., Buchner, J., Bukau, B., Carver, J.A., Ecroyd, H., Emanuelsson, C., Finet, S., Golenhofen, N., Goloubinoff, P., Gusev, N., Haslbeck, M., Hightower, L.E., Kampinga, H.H., Klevit, R.E., Liberek, K., Mchaourab, H.S., McMenimen, K.A., Poletti, A., Quinlan, R., Strelkov, S.V., Toth, M.E., Vierling, E., Tanguay, R.M.
Cell Stress Chaperones (2017), 22 (4), 601-611
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62
The Tetrameric Plant Lectin BanLec Neutralizes HIV through Bidentate Binding to Specific Viral Glycans.
Hopper, J.T.S., Ambrose. S., Grant, O.C., Krumm, S.A., Allison, T.M., Degiacomi, M.T., Tully, M.D., Pritchard, L.K., Ozorowski, G., Ward, A.B., Crispin, M., Doores, K.J., Woods, R.J., Benesch, J.L.P., Robinson, C.V., Struwe, W.B.
Structure (2017), 25 (5), 773-782.e5
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Hopper, J.T.S., Ambrose. S., Grant, O.C., Krumm, S.A., Allison, T.M., Degiacomi, M.T., Tully, M.D., Pritchard, L.K., Ozorowski, G., Ward, A.B., Crispin, M., Doores, K.J., Woods, R.J., Benesch, J.L.P., Robinson, C.V., Struwe, W.B.
Structure (2017), 25 (5), 773-782.e5
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61
Integrating mass spectrometry with MD simulations reveals the role of lipids in Na+/H+ antiporters
Landreh, M., Marklund, E.G., Uzdavinys, P., Degiacomi, M.T., Coincon, M., Gault, J., Gupta, K., Liko, I., Benesch, J.L.P., Drew, D., Robinson, C.V.
Nat. Commun. (2017), 13993
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Landreh, M., Marklund, E.G., Uzdavinys, P., Degiacomi, M.T., Coincon, M., Gault, J., Gupta, K., Liko, I., Benesch, J.L.P., Drew, D., Robinson, C.V.
Nat. Commun. (2017), 13993
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60
Protein aggregate-ligand binding assays based on microfluidic diffusional separation
Zhang, Y., Buell, A.K., Müller, T., Benesch, J.L.P., Dobson, C.M., Knowles, T.P.J.
ChemBioChem (2016), 17 (20), 1920–1924
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Zhang, Y., Buell, A.K., Müller, T., Benesch, J.L.P., Dobson, C.M., Knowles, T.P.J.
ChemBioChem (2016), 17 (20), 1920–1924
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59
Infrared laser activation of soluble and membrane protein assemblies in the gas phase
Mikhailov, V.A., Liko, I., Mize, T.H., Bush, M.F., Benesch, J.L.P., Robinson, C.V.
Anal. Chem. (2016), 88(14), 7060-7
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Mikhailov, V.A., Liko, I., Mize, T.H., Bush, M.F., Benesch, J.L.P., Robinson, C.V.
Anal. Chem. (2016), 88(14), 7060-7
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58
The human 343delT HSPB5 chaperone associated with early-onset skeletal myopathy causes defects in protein solubility
Mitzelfelt, K.A., Limphong, P., Choi, M.J., Kondrat, F.D., Lai, S., Kolander, K.D., Kwok, W.M., Dai, Q., Grzybowski, M.N., Zhang, H., Taylor, G.M., Lui, Q., Thao, M.T., Hudson, J.A., Barresi, R., Bushby, K., Jungbluth, H., Wraige, E., Geurts, A.M., Benesch, J.L.P., Riedel, M., Christians, E.S., Minella, A.C., Benjamin, I.J.
J. Biol. Chem. (2016), 291(29), 14939-53
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Mitzelfelt, K.A., Limphong, P., Choi, M.J., Kondrat, F.D., Lai, S., Kolander, K.D., Kwok, W.M., Dai, Q., Grzybowski, M.N., Zhang, H., Taylor, G.M., Lui, Q., Thao, M.T., Hudson, J.A., Barresi, R., Bushby, K., Jungbluth, H., Wraige, E., Geurts, A.M., Benesch, J.L.P., Riedel, M., Christians, E.S., Minella, A.C., Benjamin, I.J.
J. Biol. Chem. (2016), 291(29), 14939-53
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57
Low charge and reduced mobility of membrane protein complexes has implications for calibration of collision cross section measurements
Allison, T.M., Landreh, M., Benesch, J.L.P, Robinson, C.V.
Anal. Chem. (2016), 88(11), 5879-84
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Allison, T.M., Landreh, M., Benesch, J.L.P, Robinson, C.V.
Anal. Chem. (2016), 88(11), 5879-84
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56
Negative ions enhance survival of membrane protein complexes
Liko, I, Hopper. J.T., Allison. T.M., Benesch, J.L.P., Robinson, C.V.
J. Am. Soc. Mass Spectrom. (2016), 27(6), 1099-104
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Liko, I, Hopper. J.T., Allison. T.M., Benesch, J.L.P., Robinson, C.V.
J. Am. Soc. Mass Spectrom. (2016), 27(6), 1099-104
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55
Characterisation of Shigella Spa33 and Thermotoga FliM/N reveals a new model for C-ring assembly in T3SS
McDowell, M.A., Marcoux, J., McVicker, G., Johnson, S., Fong, Y.H., Stevens, R., Bowman, L.A., Degiacomi, M.T., Yan, J., Wise, A., Friede, M., Benesch, J.L.P., Deane, J.E., Tang, C.M., Robinson, C.V., Lea, S.M.
Mol. Micro. (2016), 99, 759-66
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McDowell, M.A., Marcoux, J., McVicker, G., Johnson, S., Fong, Y.H., Stevens, R., Bowman, L.A., Degiacomi, M.T., Yan, J., Wise, A., Friede, M., Benesch, J.L.P., Deane, J.E., Tang, C.M., Robinson, C.V., Lea, S.M.
Mol. Micro. (2016), 99, 759-66
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53
Optimal synthetic glycosylation of a therapeutic antibody
Parsons, T.B., Struwe, W.B., Gault, J., Yamamoto, K., Taylor, T.A., Raj, R., Wals, K., Mohammed, S., Robinson, C.V., Benesch, J.L.P., Davis, B.G.
Angew. Chem. Int. Ed. (2016), 55, 2361-7
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Parsons, T.B., Struwe, W.B., Gault, J., Yamamoto, K., Taylor, T.A., Raj, R., Wals, K., Mohammed, S., Robinson, C.V., Benesch, J.L.P., Davis, B.G.
Angew. Chem. Int. Ed. (2016), 55, 2361-7
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51
A novel mechano-enzymatic cleavage mechanism underlies transthyretin amyloidogenesis
Marcoux, J., Mangione, P.P., Porcari, R., Degiacomi, M.T., Verona, G., Taylor, G.W., Giorgetti, S., Raimondi, S., Sanglier-Cianférani, S., Benesch, J.L.P., Cecconi, C., Naqvi, M.M., Gillmore, J.D., Hawkins, P.N., Stoppini, M., Robinson, C.V., Pepys, M.B., Bellotti, V.
EMBO Mol. Med. (2015), 7, 1337-49
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video
Marcoux, J., Mangione, P.P., Porcari, R., Degiacomi, M.T., Verona, G., Taylor, G.W., Giorgetti, S., Raimondi, S., Sanglier-Cianférani, S., Benesch, J.L.P., Cecconi, C., Naqvi, M.M., Gillmore, J.D., Hawkins, P.N., Stoppini, M., Robinson, C.V., Pepys, M.B., Bellotti, V.
EMBO Mol. Med. (2015), 7, 1337-49
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50
Collision cross sections of high-mannose N-glycans in commonly observed adduct states - identification of gas-phase conformers unique to [M-H]- ions
Struwe, W.B., Benesch, J.L.P., Harvey, D.J., Pagel, K.
Analyst (2015), 140, 6799-803
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Struwe, W.B., Benesch, J.L.P., Harvey, D.J., Pagel, K.
Analyst (2015), 140, 6799-803
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46
The role of the detergent micelle in preserving the structure of membrane proteins in the gas phase
Reading, E., Liko, I., Allison, T.M., Benesch, J.L.P., Laganowsky, A., & Robinson, C.V.
Angew. Chem. Int. Ed. (2015), 54, 4577-81
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Reading, E., Liko, I., Allison, T.M., Benesch, J.L.P., Laganowsky, A., & Robinson, C.V.
Angew. Chem. Int. Ed. (2015), 54, 4577-81
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45
Combining tandem mass spectrometry with ion mobility separation to determine the architecture of polydisperse proteins
Shepherd, D.A., Marty, M.T., Giles, K., Baldwin, A.J., & Benesch, J.L.P.
Int. J. Mass Spectrom. (2015), 377, 663-71
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Shepherd, D.A., Marty, M.T., Giles, K., Baldwin, A.J., & Benesch, J.L.P.
Int. J. Mass Spectrom. (2015), 377, 663-71
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44
Studying the active-site loop movement of the São Paolo metallo-β-lactamase-1
Brem, J., Struwe, W.B., Rydzik, A.M., Tarhonskaya, H., Pfeffer, I., Flashman, E., van Berkel, S.S., Spencer, J., Claridge, T.D.W., McDonough, M.A., Benesch, J.L.P., & Schofield, C.J.
Chem. Sci. (2015), 6, 956-63
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Brem, J., Struwe, W.B., Rydzik, A.M., Tarhonskaya, H., Pfeffer, I., Flashman, E., van Berkel, S.S., Spencer, J., Claridge, T.D.W., McDonough, M.A., Benesch, J.L.P., & Schofield, C.J.
Chem. Sci. (2015), 6, 956-63
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43
Phosphomimics destabilise HSP27 oligomeric assemblies and enhance chaperone activity
Jovcevski, B., Kelly, M.A., Rote, A.P., Berg, T., Gastall, H.Y., Benesch, J.L.P., Aquilina, J.A. & Ecroyd, H.
Chem. Biol. (2015), 22, 186-95
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Jovcevski, B., Kelly, M.A., Rote, A.P., Berg, T., Gastall, H.Y., Benesch, J.L.P., Aquilina, J.A. & Ecroyd, H.
Chem. Biol. (2015), 22, 186-95
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41
Ejection of structural zinc leads to inhibition of γ-butyrobetaine hydroxylase
Rydzik, A.M., Brem, J., Struwe, W.B., Kochan, G.T., Benesch, J.L.P., & Schofield C.J.
Bioorg. Med. Chem. Lett. (2014), 24, 4954-7
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Rydzik, A.M., Brem, J., Struwe, W.B., Kochan, G.T., Benesch, J.L.P., & Schofield C.J.
Bioorg. Med. Chem. Lett. (2014), 24, 4954-7
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40
Mass-selective soft-landing of protein assemblies with controlled landing energies
Mikhailov, V.A., Mize, T.H., Benesch, J.L.P., & Robinson, C.V.
Anal. Chem. (2014), 86, 8321-8
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Mikhailov, V.A., Mize, T.H., Benesch, J.L.P., & Robinson, C.V.
Anal. Chem. (2014), 86, 8321-8
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38
The structured core domain of αB-crystallin can prevent amyloid fibrillation and associated toxicity
Hochberg, G.K.A, Ecroyd, H., Liu, C., Cox, D., Cascio, D., Sawaya, M.R., Collier, M.P., Stroud, J., Carver, J.A., Baldwin, A.J., Robinson, C.V., Eisenberg, D.S., Benesch, J.L.P. & Laganowsky, A.
Proc. Natl. Acad. Sci. U.S.A. (2014), 111, E1562-70
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commentary
Hochberg, G.K.A, Ecroyd, H., Liu, C., Cox, D., Cascio, D., Sawaya, M.R., Collier, M.P., Stroud, J., Carver, J.A., Baldwin, A.J., Robinson, C.V., Eisenberg, D.S., Benesch, J.L.P. & Laganowsky, A.
Proc. Natl. Acad. Sci. U.S.A. (2014), 111, E1562-70
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commentary
37
Hopper, J.T., Yu, Y.T., Li, D., Raymond, A., Bostock, M., Liko, I., Mikhailov, V., Laganowsky, A., Benesch, J.L.P., Caffrey, M., Nietlispach, D., & Robinson, C.V.
Nat. Methods (2013), 10, 1206-8
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36
HSP70 oligomerization is mediated by an interaction between the interdomain linker and the substrate binding domain
Aprile, F.A., Dhulesia, A., Stengel, F., Roodveldt, C., Benesch, J.L.P., Tortora, P., Robinson, C.V., Salvatella, X., Dobson, C.M., & Cremades, N.
PLOS One (2013), 8, e6796
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Aprile, F.A., Dhulesia, A., Stengel, F., Roodveldt, C., Benesch, J.L.P., Tortora, P., Robinson, C.V., Salvatella, X., Dobson, C.M., & Cremades, N.
PLOS One (2013), 8, e6796
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35
C-terminal interactions mediate the quaternary dynamics of αB-crystallin
Hilton, G.R., Hochberg, G.K.A., Laganowsky, A., McGinnigle, S.I., Baldwin, A.J., & Benesch, J.L.P.
Phil. Trans. Roy. Soc. B (2013), 368, 20110405
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Hilton, G.R., Hochberg, G.K.A., Laganowsky, A., McGinnigle, S.I., Baldwin, A.J., & Benesch, J.L.P.
Phil. Trans. Roy. Soc. B (2013), 368, 20110405
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34
Probing dynamic conformations of the high molecular weight αB-crystallin heat shock protein ensemble by NMR spectroscopy
Baldwin, A.J., Walsh, P., Hansen, D.F., Hilton, G.R., Benesch, J.L.P., Sharpe, S., & Kay, L.E.
J. Am. Chem. Soc. (2012), 134, 15343-50
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Baldwin, A.J., Walsh, P., Hansen, D.F., Hilton, G.R., Benesch, J.L.P., Sharpe, S., & Kay, L.E.
J. Am. Chem. Soc. (2012), 134, 15343-50
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33
The unusual mycobacterial chaperonins: Evidence for in vivo oligomerization and specialization of function
Fan, M., Rao, T., Zacco, E., Ahmed, M.T., Shukla, A., Ojha, A., Freeke, J., Robinson, C.V., Benesch, J.L.P., & Lund, P.A..
Mol. Micro. (2012), 85, 934-33
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Fan, M., Rao, T., Zacco, E., Ahmed, M.T., Shukla, A., Ojha, A., Freeke, J., Robinson, C.V., Benesch, J.L.P., & Lund, P.A..
Mol. Micro. (2012), 85, 934-33
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32
Dissecting heterogeneous molecular chaperone complexes using a mass spectrum deconvolution approach
Stengel, F., Baldwin, A.J., Bush, M.F., Hilton, G.R., Lioe, H., Basha, E., Jaya, N., Vierling, E. & Benesch, J.L.P.
Chem & Biol. (2012), 19, 599-607
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commentary
Stengel, F., Baldwin, A.J., Bush, M.F., Hilton, G.R., Lioe, H., Basha, E., Jaya, N., Vierling, E. & Benesch, J.L.P.
Chem & Biol. (2012), 19, 599-607
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commentary
29
The polydispersity of αB-crystallin is rationalised by an interconverting polyhedral architecture
Baldwin A.J., Lioe, H., Hilton, G.R., Baker, L.A., Rubinstein, J.L., Kay, L.E. & Benesch, J.L.P.
Structure (2011), 19, 1855-63
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Baldwin A.J., Lioe, H., Hilton, G.R., Baker, L.A., Rubinstein, J.L., Kay, L.E. & Benesch, J.L.P.
Structure (2011), 19, 1855-63
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27
Baldwin A.J., Hilton, G.R., Lioe, H., Bagnéris, C., Benesch, J.L.P. & Kay, L.E.
J. Mol. Biol. (2011), 413, 310-20
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commentary
26
Baldwin A.J., Lioe, H., Robinson, C.V., Kay, L.E. & Benesch, J.L.P.
J. Mol. Biol. (2011), 413, 297-309
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cover
commentary
25
The quaternary organization and dynamics of the molecular chaperone HSP26 are thermally regulated
Benesch, J.L.P., Aquilina, J.A., Baldwin, A.J., Rekas, A., Stengel, F., Lindner, R., Basha, E., Devlin, G., Horwitz, J., Vierling, E., Carver, J.A. & Robinson, C.V.
Chem. Biol. (2010), 17, 1008-17
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Benesch, J.L.P., Aquilina, J.A., Baldwin, A.J., Rekas, A., Stengel, F., Lindner, R., Basha, E., Devlin, G., Horwitz, J., Vierling, E., Carver, J.A. & Robinson, C.V.
Chem. Biol. (2010), 17, 1008-17
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24
Separating and visualising protein assemblies by means of preparative mass spectrometry and microscopy
Benesch, J.L.P., Ruotolo, B.T., Simmons, D.A., Barrera, N.P., Morgner, N., Wang, L., Saibil, H.R. & Robinson, C.V..
J. Struct. Biol. (2010), 172, 161-8
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Benesch, J.L.P., Ruotolo, B.T., Simmons, D.A., Barrera, N.P., Morgner, N., Wang, L., Saibil, H.R. & Robinson, C.V..
J. Struct. Biol. (2010), 172, 161-8
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23
Laganowsky, A., Benesch, J.L.P., Landau, M., Ding, L., Sawaya, M.R., Cascio, D. Huang, Q., Robinson, C.V., Horwitz, J. & Eisenberg, D.
Protein Sci. (2010), 19, 1031-43
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22
Quaternary dynamics and plasticity underlie small heat shock protein chaperone function
Stengel, F., Baldwin, A.J., Painter, A.J., Jaya, N., Basha, E., Kay, L.E., Vierling, E., Robinson, C.V. & Benesch, J.L.P.
Proc. Natl. Acad. Sci. U.S.A. (2010), 107, 2007-12
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Stengel, F., Baldwin, A.J., Painter, A.J., Jaya, N., Basha, E., Kay, L.E., Vierling, E., Robinson, C.V. & Benesch, J.L.P.
Proc. Natl. Acad. Sci. U.S.A. (2010), 107, 2007-12
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20
The small heat-shock proteins HSPB2 and HSPB3 form well-defined heterooligomers in a unique 3 to 1 subunit ratio
den Engelsman, J., Boros, S., Dankers, P.Y., Kamps, B., Vree Egberts, W.T., Bode, C.S., Lane, L.A., Aquilina, J.A., Benesch, J.L.P., Robinson, C.V., de Jong, W.W. & Boelens, W.C.
J. Mol. Biol. (2009), 393, 1022-32
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den Engelsman, J., Boros, S., Dankers, P.Y., Kamps, B., Vree Egberts, W.T., Bode, C.S., Lane, L.A., Aquilina, J.A., Benesch, J.L.P., Robinson, C.V., de Jong, W.W. & Boelens, W.C.
J. Mol. Biol. (2009), 393, 1022-32
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19
Defining the structural basis of human plasminogen binding by streptococcal surface enolase
Cork, A.J., Jergic, S., Hammerschmidt, S., Kobe, B., Pancholi, V., Benesch, J.L.P., Robinson, C.V., Dixon, N.E., Aquilina, J.A. & Walker, M.J.
J. Biol. Chem. (2009), 284, 17129-37
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Cork, A.J., Jergic, S., Hammerschmidt, S., Kobe, B., Pancholi, V., Benesch, J.L.P., Robinson, C.V., Dixon, N.E., Aquilina, J.A. & Walker, M.J.
J. Biol. Chem. (2009), 284, 17129-37
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18
Coupling microdroplet microreactors with mass spectrometry: reading the contents of single droplets online
Fidalgo, L.M., Whyte, G., Ruotolo, B.T., Benesch, J.L.P., Stengel, F., Abell, C., Robinson, C.V. & Huck, W.T.
Angew. Chem. Int. Ed. (2009), 48, 3665-8
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commentary
Fidalgo, L.M., Whyte, G., Ruotolo, B.T., Benesch, J.L.P., Stengel, F., Abell, C., Robinson, C.V. & Huck, W.T.
Angew. Chem. Int. Ed. (2009), 48, 3665-8
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17
A Monte-Carlo approach for assessing the specificity of protein oligomers observed in nano-electrospray mass spectra
Lane, L.A., Ruotolo, B.T., Robinson, C.V., Favrin, G. & Benesch, J.L.P.
Int. J. Mass Spectrom. (2009), 283, 169-77
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Lane, L.A., Ruotolo, B.T., Robinson, C.V., Favrin, G. & Benesch, J.L.P.
Int. J. Mass Spectrom. (2009), 283, 169-77
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15
Quadrupole-time-of-flight mass spectrometer modified for higher-energy dissociation reduced protein assemblies to peptide fragments
Benesch, J.L.P., Ruotolo, B.T., Sobott, F., Wildgoose, J., Gilbert, A., Bateman, R. & Robinson, C.V. & Aquilina, J.A.
Anal. Chem. (2009), 81, 1270-4
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Benesch, J.L.P., Ruotolo, B.T., Sobott, F., Wildgoose, J., Gilbert, A., Bateman, R. & Robinson, C.V. & Aquilina, J.A.
Anal. Chem. (2009), 81, 1270-4
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14
Small heat shock protein activity is regulated by variable oligomeric substructure
Benesch, J.L.P., Ayoub, M., Robinson, C.V. & Aquilina, J.A.
J. Biol. Chem. (2008), 283, 28513-7
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Benesch, J.L.P., Ayoub, M., Robinson, C.V. & Aquilina, J.A.
J. Biol. Chem. (2008), 283, 28513-7
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12
Real-time monitoring of protein complexes reveals their quaternary organization and dynamics
Painter, A.J., Jaya, N., Basha, E., Vierling, E., Robinson, C.V. & Benesch, J.L.P.
Chem. Biol. (2008), 15, 246-53
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commentary
Painter, A.J., Jaya, N., Basha, E., Vierling, E., Robinson, C.V. & Benesch, J.L.P.
Chem. Biol. (2008), 15, 246-53
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commentary
10
Mimicking phosphorylation of αB-crystallin affects its chaperone activity
Ecroyd, H., Meehan, S., Horwitz, J., Aquilina, J.A., Benesch, J.L.P., Robinson, C.V., MacPhee, C.E. & Carver, J.A.
Biochemical J. (2007), 401, 129-41
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Ecroyd, H., Meehan, S., Horwitz, J., Aquilina, J.A., Benesch, J.L.P., Robinson, C.V., MacPhee, C.E. & Carver, J.A.
Biochemical J. (2007), 401, 129-41
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9
Tandem mass spectrometry reveals the quaternary organization of macromolecular assemblies
Benesch, J.L.P., Aquilina, J.A., Ruotolo, B.T., Sobott, F. & Robinson, C.V.
Chem. Biol. (2006), 13, 597-605
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Benesch, J.L.P., Aquilina, J.A., Ruotolo, B.T., Sobott, F. & Robinson, C.V.
Chem. Biol. (2006), 13, 597-605
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8
All three chaperonin genes in the archaeon Haloferax volcanii are individually dispensable
Kapatai, G., Large, A., Benesch, J.L.P., Robinson, C.V., Carrascosa, J.L., Valpuesta, J.M., Gowrinathan, P. & Lund, P.A.
Mol. Micro. (2006), 61, 1583-97
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Kapatai, G., Large, A., Benesch, J.L.P., Robinson, C.V., Carrascosa, J.L., Valpuesta, J.M., Gowrinathan, P. & Lund, P.A.
Mol. Micro. (2006), 61, 1583-97
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6
Kennaway, C., Benesch, J.L.P., Gohlke, U., Wang, L., Robinson, C.V., Orlova, E.V., Saibil, H.R. & Keep, N.H.
J. Biol. Chem. (2005), 280, 33419-35
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5
Subunit exchange of polydisperse proteins: mass spectrometry reveals consequences of αA-crystallin truncation
Aquilina, J.A., Benesch, J.L.P., Ding, L.L., Yaron, O., Horwitz, J. & Robinson, C.V.
J. Biol. Chem. (2005), 280, 14485-91
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Aquilina, J.A., Benesch, J.L.P., Ding, L.L., Yaron, O., Horwitz, J. & Robinson, C.V.
J. Biol. Chem. (2005), 280, 14485-91
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4
Phosphorylation of αB-crystallin alters chaperone function through loss of dimeric substructure
Aquilina, J.A., Benesch, J.L.P., Ding, L.L., Yaron, O., Horwitz, J. & Robinson, C.V.
J. Biol. Chem. (2004), 279, 28675-80
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Aquilina, J.A., Benesch, J.L.P., Ding, L.L., Yaron, O., Horwitz, J. & Robinson, C.V.
J. Biol. Chem. (2004), 279, 28675-80
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3
Polydispersity of a mammalian chaperone: mass spectrometry reveals the population of oligomers in αB-crystallin
Aquilina, J.A., Benesch, J.L.P., Bateman, O.A., Slingsby, C. & Robinson, C.V.
Proc. Natl. Acad. Sci. U.S.A. (2003), 100, 10611-6
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Aquilina, J.A., Benesch, J.L.P., Bateman, O.A., Slingsby, C. & Robinson, C.V.
Proc. Natl. Acad. Sci. U.S.A. (2003), 100, 10611-6
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