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0032530724
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Mass spectral and thermodynamic evidence for water molecules in SH2 binding sites
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Chung EW, Henriques D, Renzoni DA, Waksman G, Robinson CV, Ladbury JE Mass spectral and thermodynamic evidence for water molecules in SH2 binding sites. Structure. 36:1998;1141-1151.
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Chung, E.W.1
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Ladbury, J.E.6
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4
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0032555738
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Protein subunit interactions and structural integrity of amyloidogenic transthyretins - evidence from electrospray mass spectrometry
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This paper explores the relationship between mass spectrometry conditions and solution data. Using a range of conditions to effectively calibrate the mass spectrometer, the stabilities of amyloidgenic variants of transthyretin in solution are proposed.
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Nettleton E, Sunde M, Lai V, Kelly J, Dobson C, Robinson C Protein subunit interactions and structural integrity of amyloidogenic transthyretins - evidence from electrospray mass spectrometry. J Mol Biol. 281:1998;553-564. This paper explores the relationship between mass spectrometry conditions and solution data. Using a range of conditions to effectively calibrate the mass spectrometer, the stabilities of amyloidgenic variants of transthyretin in solution are proposed.
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J Mol Biol
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Nettleton, E.1
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Kelly, J.4
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5
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0024289037
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Laser desorption ionization of protein with molecular masses exceeding 10,000 daltons
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Karas M, Hillenkamp F Laser desorption ionization of protein with molecular masses exceeding 10,000 daltons. Anal Chem. 60:1988;2299-2301.
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Karas, M.1
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Orthogonal-acceleration time-of-flight mass spectrometer
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Dawson, J.H.J.1
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7
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0028064214
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A reflecting time of flight mass spectrometer with an electrospray ion source and orthogonal extraction
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Verentchikov A, Ens W, Standing K A reflecting time of flight mass spectrometer with an electrospray ion source and orthogonal extraction. Anal Chem. 66:1994;126-133.
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Verentchikov, A.1
Ens, W.2
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8
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0028670568
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Conformation of GroEL-bound α-lactalbumin probed by mass spectrometry
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Robinson CV, Groß M, Eyles SJ, Ewbank JJ, Mayhew M, Hartl FU, Dobson CM, Radford SE Conformation of GroEL-bound α-lactalbumin probed by mass spectrometry. Nature. 372:1994;646-651.
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Robinson, C.V.1
Groß, M.2
Eyles, S.J.3
Ewbank, J.J.4
Mayhew, M.5
Hartl, F.U.6
Dobson, C.M.7
Radford, S.E.8
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9
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0029861712
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β-Lactamase binds to GroEL in a conformation highly protected against hydrogen/deuterium exchange
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Gervasoni P, Staudenman W, James P, Gehrig P, Pluckthun A β-Lactamase binds to GroEL in a conformation highly protected against hydrogen/deuterium exchange. Proc Natl Acad Sci USA. 93:1996;12189-12194.
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Gervasoni, P.1
Staudenman, W.2
James, P.3
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Pluckthun, A.5
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10
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0030451744
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Significant hydrogen exchange protection in GroEL-bound DHFR is maintained during iterative rounds of substrate cycling
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Groß M, Robinson CV, Mayhew M, Hartl FU, Radford SE Significant hydrogen exchange protection in GroEL-bound DHFR is maintained during iterative rounds of substrate cycling. Protein Sci. 5:1996;2506-2513.
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Groß, M.1
Robinson, C.V.2
Mayhew, M.3
Hartl, F.U.4
Radford, S.E.5
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11
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0031920206
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Probing conformations of GroEL-bound substrate proteins by mass spectrometry
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Robinson CV, Groß M, Radford SE Probing conformations of GroEL-bound substrate proteins by mass spectrometry. Methods Enzymol. 290:1998;296-313.
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Methods Enzymol
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Robinson, C.V.1
Groß, M.2
Radford, S.E.3
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12
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0032560474
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Protein-protein interactions in intact ribosomes probed by mass spectrometry
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The MS analysis of intact ribosomes shows that the pattern of dissociation correlates strongly with known structural features of the ribosome.
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Benjamin DR, Robinson CV, Hendrick JP, Hartl FU, Dobson CM Protein-protein interactions in intact ribosomes probed by mass spectrometry. Proc Natl Acad Sci USA. 93:1998;7391-7395. The MS analysis of intact ribosomes shows that the pattern of dissociation correlates strongly with known structural features of the ribosome.
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Proc Natl Acad Sci USA
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Benjamin, D.R.1
Robinson, C.V.2
Hendrick, J.P.3
Hartl, F.U.4
Dobson, C.M.5
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13
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0029794153
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Probing the nature of non-covalent interactions by mass spectrometry. A study of protein-CoA ligand binding and assembly
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Robinson CV, Chung EW, Kragelund BB, Knudsen J, Aplin RT, Poulsen FM, Dobson CM Probing the nature of non-covalent interactions by mass spectrometry. A study of protein-CoA ligand binding and assembly. J Am Chem Soc. 118:1996;8646-8653.
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Robinson, C.V.1
Chung, E.W.2
Kragelund, B.B.3
Knudsen, J.4
Aplin, R.T.5
Poulsen, F.M.6
Dobson, C.M.7
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14
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0031018564
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Carbonic anhydrase-inhibitor binding: From solution to the gas phase
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Wu Q-Y, Gao J-M, Joseph-McCarthy D, Sigal GB, Bruce JE, Whitesides GM, Smith RD Carbonic anhydrase-inhibitor binding: from solution to the gas phase. J Am Chem Soc. 119:1997;1157-1158.
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J Am Chem Soc
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Wu, Q.-Y.1
Gao, J.-M.2
Joseph-Mccarthy, D.3
Sigal, G.B.4
Bruce, J.E.5
Whitesides, G.M.6
Smith, R.D.7
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15
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33846278908
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New mass spectrometric methods for the study of non-covalent associations of biopolymers
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This review covers important considerations for protein-ligand complexes in the gas phase. The nature of the interactions and the use of competitive binding experiments for libraries of ligands is discussed, together with the limitations and the promise of the MS method.
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Smith RD, Bruce JE, Wu Q, Lei QP New mass spectrometric methods for the study of non-covalent associations of biopolymers. Chem Soc Rev. 26:1997;191-202. This review covers important considerations for protein-ligand complexes in the gas phase. The nature of the interactions and the use of competitive binding experiments for libraries of ligands is discussed, together with the limitations and the promise of the MS method.
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Chem Soc Rev
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Smith, R.D.1
Bruce, J.E.2
Wu, Q.3
Lei, Q.P.4
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16
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0031777368
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Study of a noncovalent trp repressor: DNA operator complex by electrospray time-of-flight mass spectrometry
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Potier N, Donald LJ, Chernushevich I, Ayed A, Ens W, Arrowsmith CH, Standing KG, Duckworth HW Study of a noncovalent trp repressor: DNA operator complex by electrospray time-of-flight mass spectrometry. Protein Sci. 7:1998;1388-1395.
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Protein Sci
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Potier, N.1
Donald, L.J.2
Chernushevich, I.3
Ayed, A.4
Ens, W.5
Arrowsmith, C.H.6
Standing, K.G.7
Duckworth, H.W.8
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17
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0032125821
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Detection of a monomeric intermediate associated with dimerization of protein HU by mass spectrometry
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Vis H, Heinemann U, Dobson CM, Robinson CV Detection of a monomeric intermediate associated with dimerization of protein HU by mass spectrometry. J Am Chem Soc. 120:1998;6427-6428.
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J Am Chem Soc
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Vis, H.1
Heinemann, U.2
Dobson, C.M.3
Robinson, C.V.4
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18
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0032246514
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Application of electrospray ionization mass spectrometry for studying human immunodeficiency virus protein complexes
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Loo JA, Holler TP, Foltin SK, McConnell P, Banotai CA, Horne NM, Mueller WT, Stevenson TI, Mack DP Application of electrospray ionization mass spectrometry for studying human immunodeficiency virus protein complexes. Proteins. 2 (suppl):1998;28-37.
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Proteins
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Loo, J.A.1
Holler, T.P.2
Foltin, S.K.3
McConnell, P.4
Banotai, C.A.5
Horne, N.M.6
Mueller, W.T.7
Stevenson, T.I.8
Mack, D.P.9
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19
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0031573676
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HIV-1 Tat peptide binding to TAR RNA by electrospray mass spectrometry
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Sannes-Lowery KA, Hu P, Mack DP, Mei H-Y, Loo JA HIV-1 Tat peptide binding to TAR RNA by electrospray mass spectrometry. Anal Chem. 69:1997;5130-5135.
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Anal Chem
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Sannes-Lowery, K.A.1
Hu, P.2
Mack, D.P.3
Mei, H.-Y.4
Loo, J.A.5
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20
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0011275132
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Direct observation of a ternary complex between the dimeric enzyme HIV-1 protease and a substrate-based inhibitor
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Baca M, Kent SB Direct observation of a ternary complex between the dimeric enzyme HIV-1 protease and a substrate-based inhibitor. J Am Chem Soc. 114:1992;3992-3993.
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Water: Now you see it, now you don't
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Levitt M, Park BH Water: now you see it, now you don't. Structure. 1:1993;223-226.
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Structure
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Levitt, M.1
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0032544931
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Freeze-dried biomolecules: FT-ICR studies of the specific solvation of functional groups and clatherate formation observed by the slow evaporation of water from hydrated peptides and model compounds in the gas phase
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Lee SW, Freivogel P, Schlindler T, Beauchamp JL Freeze-dried biomolecules: FT-ICR studies of the specific solvation of functional groups and clatherate formation observed by the slow evaporation of water from hydrated peptides and model compounds in the gas phase. J Am Chem Soc. 120:1998;11758-11765.
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J Am Chem Soc
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Lee, S.W.1
Freivogel, P.2
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Beauchamp, J.L.4
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24
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0001663318
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Hydration of folded and unfolded gas-phase proteins: Saturation of cytochrome c and apomyoglobin
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The authors show that in the gas phase, folded conformations of both cytochrome c and apomyoglobin are more hydrated than their unfolded counterparts.
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Fye JL, Woenckhaus J, Jarrold MF Hydration of folded and unfolded gas-phase proteins: saturation of cytochrome c and apomyoglobin. J Am Chem Soc. 120:1998;1327-1328. The authors show that in the gas phase, folded conformations of both cytochrome c and apomyoglobin are more hydrated than their unfolded counterparts.
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J Am Chem Soc
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Fye, J.L.1
Woenckhaus, J.2
Jarrold, M.F.3
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25
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0032247077
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Dissection of multi-protein complexes using mass spectrometry - Subunit interactions in transthyretin and retinol-binding protein complexes
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This paper examines the interactions between transthyretin and retinol-binding protein and shows that the stoichiometry and interactions in this multiprotein complex can be defined by MS.
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Rostom AA, Sunde M, Richardson SJ, Schreiber G, Jarvis S, Bateman R, Dobson CM, Robinson CV Dissection of multi-protein complexes using mass spectrometry - subunit interactions in transthyretin and retinol-binding protein complexes. Proteins. 2 (suppl):1998;3-11. This paper examines the interactions between transthyretin and retinol-binding protein and shows that the stoichiometry and interactions in this multiprotein complex can be defined by MS.
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Proteins
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Rostom, A.A.1
Sunde, M.2
Richardson, S.J.3
Schreiber, G.4
Jarvis, S.5
Bateman, R.6
Dobson, C.M.7
Robinson, C.V.8
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26
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0031956947
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Quantitative evaluation of protein-protein and ligand-protein equilibria of a large allosteric enzyme by electrospray ionization time-of-flight mass spectrometry
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The first demonstration of high mass homo-oligomeric protein-protein interactions by electrospray time-of-flight MS.
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Ayed A, Krutchinsky AN, Ens W, Standing KG, Duckworth HW Quantitative evaluation of protein-protein and ligand-protein equilibria of a large allosteric enzyme by electrospray ionization time-of-flight mass spectrometry. Rapid Commun Mass Spectrom. 12:1998;339-344. The first demonstration of high mass homo-oligomeric protein-protein interactions by electrospray time-of-flight MS.
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Rapid Commun Mass Spectrom
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Ayed, A.1
Krutchinsky, A.N.2
Ens, W.3
Standing, K.G.4
Duckworth, H.W.5
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27
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0032067782
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Electrospray mass spectrometry studies of non-heme iron containing proteins
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Lei QP, Cui X Jr., Kurtz DM, Amster IJ, Chernushevich IV, Standing KG Electrospray mass spectrometry studies of non-heme iron containing proteins. Anal Chem. 70:1998;1838-1846.
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Anal Chem
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Lei, Q.P.1
Cui X., Jr.2
Kurtz, D.M.3
Amster, I.J.4
Chernushevich, I.V.5
Standing, K.G.6
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28
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0031734169
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The interaction between the chaperone Sec B and its ligands: Evidence for multiple subsites for binding
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Randall LL, Hardy SJS, Topping TB, Smith VF, Bruce JE, Smith RD The interaction between the chaperone Sec B and its ligands: evidence for multiple subsites for binding. Protein Sci. 7:1998;2384-2390.
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Protein Sci
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Randall, L.L.1
Hardy, S.J.S.2
Topping, T.B.3
Smith, V.F.4
Bruce, J.E.5
Smith, R.D.6
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29
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0031835583
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The observation of chaperone-ligand noncovalent complexes with electrospray ionization mass spectrometry
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The detection of this intact chaperone by Fourier transform MS demonstrated the binding stoichiometry of one Sec B tetramer and one OppA protein ligand.
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Bruce JE, Smith VF, Liu C, Randall LL, Smith RD The observation of chaperone-ligand noncovalent complexes with electrospray ionization mass spectrometry. Protein Sci. 7:1998;1180-1185. The detection of this intact chaperone by Fourier transform MS demonstrated the binding stoichiometry of one Sec B tetramer and one OppA protein ligand.
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Protein Sci
, vol.7
, pp. 1180-1185
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Bruce, J.E.1
Smith, V.F.2
Liu, C.3
Randall, L.L.4
Smith, R.D.5
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