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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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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64

Proline isomerization in the C-terminal region of HSP27
Alderson, T.R., Benesch, J.L., Baldwin, A.J.
Cell Stress and 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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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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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.
Nature Communications 8 (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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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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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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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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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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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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54

GlycoMob: an ion mobility-mass spectrometry collision cross section database for glycomics
Struwe, W.B., Pagel, K., Benesch, J.L.P., Harvey, D.J., Campbell, M.P.
Glycoconj. J. (2016), 33, 399-404
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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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52

EMIM: software for relating ion mobility mass spectrometry and electron microscopy data
Degiacomi, M.T., Benesch, J.L.P.
Analyst (2016), 141, 70-5
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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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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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49

Dynamics-function relationships of the small heat-shock proteins
Hochberg, G.K.A. & Benesch, J.L.P.
Heat Shock Proteins (2015), 8, 87-100
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48

Bayesian deconvolution of mass and ion mobility spectra: from binary interactions to polydisperse ensembles
Marty, M.T., Baldwin, A.J., Marklund, E.G., Hochberg, G.K.A., Benesch, J.L.P., & Robinson, C.V.
Anal. Chem. (2015), 87, 4370-6
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video
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47

Collision cross sections for structural proteomics
Marklund, E.G., Degiacomi, M.T., Robinson, C.V., Baldwin, A.J., & Benesch, J.L.P.
Structure (2015), 23, 791-9
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software

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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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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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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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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42

Native mass spectrometry: towards high-throughput structural proteomics
Kondrat, F.D., Struwe, W.B., & Benesch, J.L.P.
Methods Mol. Biol. (2014), 1261, 349-71
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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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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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39

Dynamical structure of αB-crystallin
Hochberg, G.K.A. & Benesch, J.L.P.
Prog. Biophys. Mol. Biol. (2014), 115, 11-20
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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

37

2013 Detergent-Free Mass Spectrometry of Membrane Protein Complexes - Cover
Detergent-free mass spectrometry of membrane protein complexes
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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cover

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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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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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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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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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

31

Small heat-shock proteins: paramedics of the cell
Hilton, G.R., Lioe, H., Stengel, F., Baldwin, A.J. & Benesch, J.L.P.
Top. Curr. Chem. (2012), 328, 69-98
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30

Two decades of studying non-covalent biomolecular assemblies by means of electrospray ionisation mass spectrometry
Hilton, G.R. & Benesch, J.L.P.
J. R. Soc. Interface (2012), 9, 801-16
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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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28

Mass spectrometry: come of age for structural and dynamical biology
Benesch, J.L.P. & Ruotolo, B.T.
Curr. Op. Struc. Biol. (2011), 21, 641-9
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27

Quaternary dynamics of αB-crystallin as a direct consequence of localised tertiary fluctuations in the C-terminus
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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cover
commentary

26

αB-crystallin polydispersity is a consequence of unbiased quaternary dynamics
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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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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23

Crystal structures of truncated αA and αB crystallins reveals structural mechanisms of polydispersity important for eye lens function
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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cover

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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21

Dehydrated but unharmed
Benesch, J.L.P. & Robinson, C.V.
Nature (2009), 462, 576-7
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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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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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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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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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16

Collisional activation of protein complexes: picking up the pieces
Benesch, J.L.P.
J. Am. Soc. Mass. Spectrom. (2009), 20, 341-8
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cover

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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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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13

Ion mobility mass spectrometry analysis of large protein complexes
Ruotolo, B.T., Benesch, J.L.P., Sandercock, A.M., Hyung, S.-J. & Robinson, C.V.
Nat. Prot. (2008), 3, 1139-52
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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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11

Protein complexes in the gas phase: technology for structural genomics and proteomics
Benesch, J.L.P., Ruotolo, B.T., Simmons, D.A. & Robinson, C.V.
Chem. Rev. (2007), 107, 3544-67
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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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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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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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7

Mass spectrometry of macromolecular assemblies: preservation and dissociation
Benesch, J.L.P. & Robinson, C.V.
Curr. Op. Struc. Biol. (2006), 16, 245-51
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6

Dodecameric structure of the small heat shock protein Acr1 from Mycobacterium tuberculosis
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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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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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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2

Thermal dissociation of multimeric protein complexes by using nanoelectrospray mass spectrometry
Benesch, J.L.P., Sobott, F. & Robinson, C.V.
Anal. Chem. (2003), 75, 2208-14
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commentary
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1

Subunit exchange of multimeric protein complexes: real-time monitoring of subunit exchange between small heat shock proteins by using electrospray mass spectrometry
Sobott, F., Benesch, J.L.P., Vierling, E. & Robinson, C.V.
J. Biol. Chem. (2002), 277, 38921-9
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