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1
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0024289037
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Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltons
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Karas M, Hillenkamp F. Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltons. Anal Chem. 60:1988;2299-2301.
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Anal Chem
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Karas, M.1
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2
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0029331042
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Mass resolution improvement by incorporation of pulsed ion extraction in a matrix-assisted laser desorption/ionization linear time-of-flight mass spectrometer
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Brown RS, Lennon JJ. Mass resolution improvement by incorporation of pulsed ion extraction in a matrix-assisted laser desorption/ionization linear time-of-flight mass spectrometer. Anal Chem. 67:1995;1998-2003.
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Anal Chem
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Brown, R.S.1
Lennon, J.J.2
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3
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0030041205
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Developments in matrix-assisted laser desorption/ionization peptide mass spectrometry
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Mann M, Talbo G. Developments in matrix-assisted laser desorption/ionization peptide mass spectrometry. Curr Opin Biotechnol. 7:1996;11-19.
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(1996)
Curr Opin Biotechnol
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Mann, M.1
Talbo, G.2
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4
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0030712449
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Delayed extraction time-of-flight MALDI mass spectrometry of proteins above 25,000 Da
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Bahr U, Stahl-Zeng J, Gleitsmann E, Karas M. Delayed extraction time-of-flight MALDI mass spectrometry of proteins above 25,000 Da. J Mass Spectrometry. 32:1997;1111-1116.
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J Mass Spectrometry
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Bahr, U.1
Stahl-Zeng, J.2
Gleitsmann, E.3
Karas, M.4
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5
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21544444186
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Functional wave time-lag focusing matrix-assisted laser desorption/ionization in a linear time-of-flight mass spectrometer: Improved mass accuracy
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Whittal RM, Russon LM, Weinberger SR, Li L. Functional wave time-lag focusing matrix-assisted laser desorption/ionization in a linear time-of-flight mass spectrometer: improved mass accuracy. Anal Chem. 69:1997;2147-2153.
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(1997)
Anal Chem
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, pp. 2147-2153
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Whittal, R.M.1
Russon, L.M.2
Weinberger, S.R.3
Li, L.4
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6
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0024438708
-
Electrospray ionization for mass spectrometry of large biomolecules
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Fenn JB, Mann M, Meng CK, Wong SF, Whitehouse CM. Electrospray ionization for mass spectrometry of large biomolecules. Science. 246:1989;64-71.
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(1989)
Science
, vol.246
, pp. 64-71
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Fenn, J.B.1
Mann, M.2
Meng, C.K.3
Wong, S.F.4
Whitehouse, C.M.5
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7
-
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0030026070
-
Femtomole sequencing of proteins from polyacrylamide gels by nano-electrospray mass spectrometry
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Wilm M, Shevchenko A, Houthaeve T, Breit S, Schweigerer L, Fotsis T, Mann M. Femtomole sequencing of proteins from polyacrylamide gels by nano-electrospray mass spectrometry. Nature. 379:1996;466-469.
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(1996)
Nature
, vol.379
, pp. 466-469
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-
Wilm, M.1
Shevchenko, A.2
Houthaeve, T.3
Breit, S.4
Schweigerer, L.5
Fotsis, T.6
Mann, M.7
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8
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0029685702
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Analytical properties of the nanoelectrospray ion source
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Wilm M, Mann M. Analytical properties of the nanoelectrospray ion source. Anal Chem. 68:1996;1-8.
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(1996)
Anal Chem
, vol.68
, pp. 1-8
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Wilm, M.1
Mann, M.2
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9
-
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0031081353
-
Multichannel microchip electrospray mass spectrometry
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of special interest. Multiple small electrospray ion sources were produced as p parallel etoned channels on a microchip. The device typically afforded flow rates of 100-200 nl/min and mass spectra of standard proteins were obtained at concentrations as low as 60 femtomole/μl. The parallel design avoids cross-contamination of samples and holds the potential of increased throughput compared to conventional microelectrospray sources.
-
Xue Q, Foret F, Dunayevskiy YM, Zavracky PM, McGruer NE, Karger BL. Multichannel microchip electrospray mass spectrometry. of special interest Anal Chem. 69:1997;426-430 Multiple small electrospray ion sources were produced as p parallel etoned channels on a microchip. The device typically afforded flow rates of 100-200 nl/min and mass spectra of standard proteins were obtained at concentrations as low as 60 femtomole/μl. The parallel design avoids cross-contamination of samples and holds the potential of increased throughput compared to conventional microelectrospray sources.
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(1997)
Anal Chem
, vol.69
, pp. 426-430
-
-
Xue, Q.1
Foret, F.2
Dunayevskiy, Y.M.3
Zavracky, P.M.4
McGruer, N.E.5
Karger, B.L.6
-
10
-
-
0031206748
-
A microfabricated device for rapid protein identification by microelectrospray ion trap mass spectrometry
-
of special interest. A similar idea to the one discussed in [9] was realized in this paper as multiple sample wells on a microchip connected to a microelectrospray capillary. Liquid flow (100 nl/min) from individual wells was generated by electro-osmotic pumping using a long capillary. Detection of standard peptide mixtures in the low femtomole range was achieved. Since the same spraying capillaries were used for all samples, cross-contamination might hamper high sensitivity applications.
-
Figeys D, Ning Y, Aebersold R. A microfabricated device for rapid protein identification by microelectrospray ion trap mass spectrometry. of special interest Anal Chem. 69:1997;3153-3160 A similar idea to the one discussed in [9] was realized in this paper as multiple sample wells on a microchip connected to a microelectrospray capillary. Liquid flow (100 nl/min) from individual wells was generated by electro-osmotic pumping using a long capillary. Detection of standard peptide mixtures in the low femtomole range was achieved. Since the same spraying capillaries were used for all samples, cross-contamination might hamper high sensitivity applications.
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(1997)
Anal Chem
, vol.69
, pp. 3153-3160
-
-
Figeys, D.1
Ning, Y.2
Aebersold, R.3
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11
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0031014649
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The quadrupole ion trap mass spectrometer - A small solution to a big challenge
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Jonscher KR, Yates JR. The quadrupole ion trap mass spectrometer - a small solution to a big challenge. Anal Biochem. 244:1997;1-15.
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(1997)
Anal Biochem
, vol.244
, pp. 1-15
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Jonscher, K.R.1
Yates, J.R.2
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13
-
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0029717657
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High-sensitivity collisionally-activated decomposition tandem mass spectrometry on a novel quadrupole/orthogonal-acceleration time-of-flight mass spectrometer
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Morris H, Paxton T, Dell A, Langhorne J, Berg M, Bordoli RS, Hoyes J, Batemar RH. High-sensitivity collisionally-activated decomposition tandem mass spectrometry on a novel quadrupole/orthogonal-acceleration time-of-flight mass spectrometer. Rapid Commun Mass Spectrom. 10:1996;889-896.
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(1996)
Rapid Commun Mass Spectrom
, vol.10
, pp. 889-896
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Morris, H.1
Paxton, T.2
Dell, A.3
Langhorne, J.4
Berg, M.5
Bordoli, R.S.6
Hoyes, J.7
Batemar, R.H.8
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14
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0030960366
-
Rapid 'de novo' peptide sequencing by a combination of nanoelectrospray, isotopic labeling and a quadrupole/time-of-flight mass spectrometer
-
8O-labelling and a novel quadrupole TOF mass spectrometer. The increased resolution and mass accuracy obtained greatly facilitated data interpretation and enhanced the specificity of 'peptide sequence tag' database searches. Cloning strategies based upon peptide sequencing in particular will become more generally applicable as a result of the high data quality afforded by this instrumental design.
-
8O-labelling and a novel quadrupole TOF mass spectrometer. The increased resolution and mass accuracy obtained greatly facilitated data interpretation and enhanced the specificity of 'peptide sequence tag' database searches. Cloning strategies based upon peptide sequencing in particular will become more generally applicable as a result of the high data quality afforded by this instrumental design.
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(1997)
Rapid Commun Mass Spectrom
, vol.11
, pp. 1015-1024
-
-
Shevchenko, A.1
Chernushevich, I.2
Ens, W.3
Standing, K.G.4
Thomson, B.5
Wilm, M.6
Mann, M.7
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15
-
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0027198862
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Identifying proteins from two-dimensional gels by molecular mass searching of peptide fragments in protein sequence databases
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Henzel WJ, Billec TM, Stults JT, Wong SC, Grimley C, Watanabe C. Identifying proteins from two-dimensional gels by molecular mass searching of peptide fragments in protein sequence databases. Proc Natl Acad Sci USA. 90:1993;5011-5015.
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(1993)
Proc Natl Acad Sci USA
, vol.90
, pp. 5011-5015
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Henzel, W.J.1
Billec, T.M.2
Stults, J.T.3
Wong, S.C.4
Grimley, C.5
Watanabe, C.6
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16
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0027608882
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Use of mass spectrometric molecular weight information to identify proteins in sequence databases
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Mann M, Hojrup P, Roepstorff P. Use of mass spectrometric molecular weight information to identify proteins in sequence databases. Biol Mass Spectrom. 22:1993;338-345.
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(1993)
Biol Mass Spectrom
, vol.22
, pp. 338-345
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Mann, M.1
Hojrup, P.2
Roepstorff, P.3
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17
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12944269065
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Rapid identification of proteins by peptide mass finger printing
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Pappin D, Højrup P, Bleasby AJ. Rapid identification of proteins by peptide mass finger printing. Curr Biol. 3:1993;327-332.
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(1993)
Curr Biol
, vol.3
, pp. 327-332
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Pappin, D.1
Højrup, P.2
Bleasby, A.J.3
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19
-
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0027375364
-
Peptide mass maps: A highly informative approach to protein identification
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Yates JR, Speicher S, Griffin PR, Hunkapiller T. Peptide mass maps: a highly informative approach to protein identification. Anal Biochem. 214:1993;397-408.
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(1993)
Anal Biochem
, vol.214
, pp. 397-408
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Yates, J.R.1
Speicher, S.2
Griffin, P.R.3
Hunkapiller, T.4
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20
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0031298696
-
Identification of the components of simple protein mixtures by high-accuracy peptide mass mapping and database searching
-
of special interest. It was shown that state of the art MALDI MS affords sufficiently high mass accuracy (<30 ppm) to enable the identification of components of simple protein mixtures using MALDI mass mapping and an iterative database search routine. Such mixtures are often encountered when proteins from 1D polyacrylamide gels are investigated. The ability to analyze mixtures will further reduce the need for sequencing of proteins that are already represented in databases.
-
Jensen ON, Podtelejnikov AV, Mann M. Identification of the components of simple protein mixtures by high-accuracy peptide mass mapping and database searching. of special interest Anal Chem. 69:1997;4741-4750 It was shown that state of the art MALDI MS affords sufficiently high mass accuracy (<30 ppm) to enable the identification of components of simple protein mixtures using MALDI mass mapping and an iterative database search routine. Such mixtures are often encountered when proteins from 1D polyacrylamide gels are investigated. The ability to analyze mixtures will further reduce the need for sequencing of proteins that are already represented in databases.
-
(1997)
Anal Chem
, vol.69
, pp. 4741-4750
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Jensen, O.N.1
Podtelejnikov, A.V.2
Mann, M.3
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21
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0030951591
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Sensitivity and mass accuracy for proteins analyzed directly from polyacrylamide gels: Implications for proteome mapping
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of special interest. MALDI mass spectra were obtained for low picomole amounts of intact proteins desorbed directly from isoelectric focusing gels. Intact molecular weight information is not sufficient for the identification of proteins by database searching, although it is nevertheless of value for the characterization of endogenous forms of mature proteins. The decrease in sensitivity at higher mass and a generally low mass accuracy might, however, still limit the application of the method in practice.
-
Ogorzalek Loo RR, Mitchell C, Stevenson TI, Martin SA, Hines WM, Juhasz P, Patterson DH, Peltier JM, Loo JA, Andrews PC. Sensitivity and mass accuracy for proteins analyzed directly from polyacrylamide gels: implications for proteome mapping. of special interest Electrophoresis. 18:1997;382-390 MALDI mass spectra were obtained for low picomole amounts of intact proteins desorbed directly from isoelectric focusing gels. Intact molecular weight information is not sufficient for the identification of proteins by database searching, although it is nevertheless of value for the characterization of endogenous forms of mature proteins. The decrease in sensitivity at higher mass and a generally low mass accuracy might, however, still limit the application of the method in practice.
-
(1997)
Electrophoresis
, vol.18
, pp. 382-390
-
-
Ogorzalek Loo, R.R.1
Mitchell, C.2
Stevenson, T.I.3
Martin, S.A.4
Hines, W.M.5
Juhasz, P.6
Patterson, D.H.7
Peltier, J.M.8
Loo, J.A.9
Andrews, P.C.10
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22
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0031202984
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Analysis of proteins by direct-scanning infrared-MALDI mass spectrometry after 2D-PAGE separation and electroblotting
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of special interest. MALDI mass spectra were obtained for intact proteins that were desorped directly from blots following 2D gel electrophoresis. See [21] for comments.
-
Eckerskorn C, Strupat K, Schleuder D, Hochstrasser D, Sanchez JC, Lottspeich F, Hillenkamp F. Analysis of proteins by direct-scanning infrared-MALDI mass spectrometry after 2D-PAGE separation and electroblotting. of special interest Anal Chem. 69:1997;2888-2892 MALDI mass spectra were obtained for intact proteins that were desorped directly from blots following 2D gel electrophoresis. See [21] for comments.
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(1997)
Anal Chem
, vol.69
, pp. 2888-2892
-
-
Eckerskorn, C.1
Strupat, K.2
Schleuder, D.3
Hochstrasser, D.4
Sanchez, J.C.5
Lottspeich, F.6
Hillenkamp, F.7
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23
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0031148680
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Mass spectrometry of whole proteins eluted from sodium dodecyl sulfate- polyacrylamide gel electrophoresis gels
-
of special interest. MALDI mass spectra were obtained for low picomole amounts of intact proteins that were extracted from negatively stained SDS-PAGE gels. In principle, the method does not suffer from the low mass accuracies associated with the techniques used in [21] and [22] but the extraction procedure might impose limits on the attainable mass range.
-
Cohen SL, Chait BT. Mass spectrometry of whole proteins eluted from sodium dodecyl sulfate- polyacrylamide gel electrophoresis gels. of special interest Anal Biochem. 247:1997;257-267 MALDI mass spectra were obtained for low picomole amounts of intact proteins that were extracted from negatively stained SDS-PAGE gels. In principle, the method does not suffer from the low mass accuracies associated with the techniques used in [21] and [22] but the extraction procedure might impose limits on the attainable mass range.
-
(1997)
Anal Biochem
, vol.247
, pp. 257-267
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-
Cohen, S.L.1
Chait, B.T.2
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24
-
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0028575316
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Error-tolerant identification of peptides in sequence databases by peptide sequence tags
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Mann M, Wilm M. Error-tolerant identification of peptides in sequence databases by peptide sequence tags. Anal Chem. 66:1994;4390-4399.
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(1994)
Anal Chem
, vol.66
, pp. 4390-4399
-
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Mann, M.1
Wilm, M.2
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25
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0000857494
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An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
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Eng J, McCorrmack AL, Yates JR. An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. J Am Soc Mass Spectrom. 5:1994;976-989.
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(1994)
J Am Soc Mass Spectrom
, vol.5
, pp. 976-989
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-
Eng, J.1
McCorrMacK, A.L.2
Yates, J.R.3
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26
-
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0030176044
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Protein identification by capillary zone electrophoresis/microelectrospray ionization-tandem mass spectrometry at the subfemtomole level
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Figeys D, van Oostveen I, Ducret A, Aebersold R. Protein identification by capillary zone electrophoresis/microelectrospray ionization-tandem mass spectrometry at the subfemtomole level. Anal Chem. 68:1996;1822-1828.
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(1996)
Anal Chem
, vol.68
, pp. 1822-1828
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-
Figeys, D.1
Van Oostveen, I.2
Ducret, A.3
Aebersold, R.4
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27
-
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0031588703
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Identification of proteins by capillary electrophoresis-tandem mass spectrometry. Evaluation of an on-line solid-phase extraction device
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of special interest. The sensitivity of on line CE/MS analysis of protein digests was shown to be increased by the use of an on line solid-phase extraction (SPE) step prior to CE/MS. The efficient sample concentration and purification afforded by the SPE device allowed the detection of low femtomole amounts of standard protein digests, as well as the identification of yeast proteins separated by 2D electrophoresis.
-
Figeys D, Ducret A, Aebersold R. Identification of proteins by capillary electrophoresis-tandem mass spectrometry. Evaluation of an on-line solid-phase extraction device. of special interest J Chromatogr A. 763:1997;295-306 The sensitivity of on line CE/MS analysis of protein digests was shown to be increased by the use of an on line solid-phase extraction (SPE) step prior to CE/MS. The efficient sample concentration and purification afforded by the SPE device allowed the detection of low femtomole amounts of standard protein digests, as well as the identification of yeast proteins separated by 2D electrophoresis.
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(1997)
J Chromatogr a
, vol.763
, pp. 295-306
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-
Figeys, D.1
Ducret, A.2
Aebersold, R.3
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28
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0030884713
-
Emerging tandem-mass-spectrometry techniques for the rapid identification of proteins
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Dongre AR, Eng JK, Yates JR. Emerging tandem-mass-spectrometry techniques for the rapid identification of proteins. Trends Biotechnol. 15:1997;418-425.
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(1997)
Trends Biotechnol
, vol.15
, pp. 418-425
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Dongre, A.R.1
Eng, J.K.2
Yates, J.R.3
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29
-
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0031568420
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Direct analysis and identification of proteins in mixtures by LC/MS/MS and database searching at the low-femtomole level
-
of special interest. This paper describes an interesting approach to the identification of interacting proteins without prior separation of the mixture by SDS-PAGE. Instead, the proteins were cleaved with a protease in solution to yield a large collection of peptides. This peptide mixture was then analyzed by liquid chromatography (LC)/MS/MS, in conjunction with database searching, to reveal the constituent proteins. Circumventing the need for gels would make mixture analysis less tedious but LC separation of very heterogeneous peptide mixtures might not be able to cope with larger numbers of interacting proteins and also might not offer a dynamic range comparable to SDS-PAGE.
-
McCormack AL, Schieltz DM, Goode B, Yang S, Barnes G, Drubin D, Yates JR. Direct analysis and identification of proteins in mixtures by LC/MS/MS and database searching at the low-femtomole level. of special interest Anal Chem. 69:1997;767-776 This paper describes an interesting approach to the identification of interacting proteins without prior separation of the mixture by SDS-PAGE. Instead, the proteins were cleaved with a protease in solution to yield a large collection of peptides. This peptide mixture was then analyzed by liquid chromatography (LC)/MS/MS, in conjunction with database searching, to reveal the constituent proteins. Circumventing the need for gels would make mixture analysis less tedious but LC separation of very heterogeneous peptide mixtures might not be able to cope with larger numbers of interacting proteins and also might not offer a dynamic range comparable to SDS-PAGE.
-
(1997)
Anal Chem
, vol.69
, pp. 767-776
-
-
McCorMacK, A.L.1
Schieltz, D.M.2
Goode, B.3
Yang, S.4
Barnes, G.5
Drubin, D.6
Yates, J.R.7
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30
-
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0031242798
-
A strategy for rapid, high-confidence protein identification
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of special interest. A strategy for the identification of proteins based upon MALDI ion trap MS/MS is presented. The approach combines the advantageous features of MALDI (low sample consumption and facile data interpretation) with the high information content of tandem MS. Empirical observations, such as preferential fragmentation at acidic residues, provided specific search criteria for subsequent database searches.
-
Qin J, Fenyo D, Zhao Y, Hail WW, Chao DM, Wilson CJ, Young RA, Chait BT. A strategy for rapid, high-confidence protein identification. of special interest Anal Chem. 69:1997;3995-4001 A strategy for the identification of proteins based upon MALDI ion trap MS/MS is presented. The approach combines the advantageous features of MALDI (low sample consumption and facile data interpretation) with the high information content of tandem MS. Empirical observations, such as preferential fragmentation at acidic residues, provided specific search criteria for subsequent database searches.
-
(1997)
Anal Chem
, vol.69
, pp. 3995-4001
-
-
Qin, J.1
Fenyo, D.2
Zhao, Y.3
Hail, W.W.4
Chao, D.M.5
Wilson, C.J.6
Young, R.A.7
Chait, B.T.8
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31
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0030772963
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MRNA silencing in erythroid differentiation: HnRNP K and hnRNP E1 regulate 15-lipoxygenase translation from the 3′ end
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Ostareck DH, Ostareck-Lederer A, Wilm M, Thiele BJ, Mann M, Hentze MW. mRNA silencing in erythroid differentiation: hnRNP K and hnRNP E1 regulate 15-lipoxygenase translation from the 3′ end. Cell. 89:1997;597-606.
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(1997)
Cell
, vol.89
, pp. 597-606
-
-
Ostareck, D.H.1
Ostareck-Lederer, A.2
Wilm, M.3
Thiele, B.J.4
Mann, M.5
Hentze, M.W.6
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32
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0030943857
-
Calmodulin modulates the interaction between IQGAP1 and Cdc42. Identification of IQGAP1 by nanoelectrospray tandem mass spectrometry
-
Joyal JL, Annan RS, Ho YD, Huddleston ME, Carr SA, Hart MJ, Sacks DB. Calmodulin modulates the interaction between IQGAP1 and Cdc42. Identification of IQGAP1 by nanoelectrospray tandem mass spectrometry. J Biol Chem. 272:1997;15419-15425.
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(1997)
J Biol Chem
, vol.272
, pp. 15419-15425
-
-
Joyal, J.L.1
Annan, R.S.2
Ho, Y.D.3
Huddleston, M.E.4
Carr, S.A.5
Hart, M.J.6
Sacks, D.B.7
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33
-
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0030743386
-
Activity of DNA ligase IV stimulated by complex formation with XRCC4 protein in mammalian cells
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Grawunder U, Wilm M, Wu X, Kulesza P, Wilson TE, Mann M, Lieber MR. Activity of DNA ligase IV stimulated by complex formation with XRCC4 protein in mammalian cells. Nature. 388:1997;492-495.
-
(1997)
Nature
, vol.388
, pp. 492-495
-
-
Grawunder, U.1
Wilm, M.2
Wu, X.3
Kulesza, P.4
Wilson, T.E.5
Mann, M.6
Lieber, M.R.7
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34
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0030836588
-
Rapid protein sequencing by tandem mass spectrometry and cDNA cloning of p20-CGGBP. A novel protein that binds to the unstable triplet repeat 5′-d(CGG)n-3′ in the human FMR1 gene
-
of special interest. This study illustrates that mass spectrometric peptide sequencing can provide a short cut to interesting genes. Searching of EST databases using peptide sequence tags identified a clone containing the full-length coding sequence of a hitherto unknown protein. This allowed the rapid cloning of the cognate gene. Given the tremendous growth of EST databases, this strategy is expected to become more generally applicable in the future.
-
Deissler H, Wilm M, Gene B, Schmitz B, Ternes T, Naumann F, Mann M, Doerfler W. Rapid protein sequencing by tandem mass spectrometry and cDNA cloning of p20-CGGBP. A novel protein that binds to the unstable triplet repeat 5′-d(CGG)n-3′ in the human FMR1 gene. of special interest J Biol Chem. 272:1997;16761-16768 This study illustrates that mass spectrometric peptide sequencing can provide a short cut to interesting genes. Searching of EST databases using peptide sequence tags identified a clone containing the full-length coding sequence of a hitherto unknown protein. This allowed the rapid cloning of the cognate gene. Given the tremendous growth of EST databases, this strategy is expected to become more generally applicable in the future.
-
(1997)
J Biol Chem
, vol.272
, pp. 16761-16768
-
-
Deissler, H.1
Wilm, M.2
Gene, B.3
Schmitz, B.4
Ternes, T.5
Naumann, F.6
Mann, M.7
Doerfler, W.8
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35
-
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0030938901
-
Reverse transcriptase motifs in the catalytic subunit of telomerase
-
of outstanding interest. Tandem mass spectrometric de novo sequencing of multiple peptides of low picomole amounts of the catalytic subunit of telomerase allowed the generation of degenerate oligonucleotide primers for the subsequent cloning of the corresponding gene. More than 150 amino acids were represented in respective MS/MS spectra. Detailed sequence analysis of the cloned gene revealed that telomerase contains reverse transcriptase motifs that were found to be essential for chromosome replication. This paper represents the first instance of the cloning of a novel protein of major biological significance using MS data from sample amounts too low for traditional sequencing strategies.
-
Lingner J, Hughes TR, Shevchenko A, Mann M, Lundblad V, Cech TR. Reverse transcriptase motifs in the catalytic subunit of telomerase. of outstanding interest Science. 276:1997;561-567 Tandem mass spectrometric de novo sequencing of multiple peptides of low picomole amounts of the catalytic subunit of telomerase allowed the generation of degenerate oligonucleotide primers for the subsequent cloning of the corresponding gene. More than 150 amino acids were represented in respective MS/MS spectra. Detailed sequence analysis of the cloned gene revealed that telomerase contains reverse transcriptase motifs that were found to be essential for chromosome replication. This paper represents the first instance of the cloning of a novel protein of major biological significance using MS data from sample amounts too low for traditional sequencing strategies.
-
(1997)
Science
, vol.276
, pp. 561-567
-
-
Lingner, J.1
Hughes, T.R.2
Shevchenko, A.3
Mann, M.4
Lundblad, V.5
Cech, T.R.6
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36
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0030807903
-
SH2 signaling in a lower eukaryote: A STAT protein that regulates stalk cell differentiation in dictyostelium
-
Kawata T, Shevchenko A, Fukuzawa M, Jermyn KA, Totty NF, Zhukovskaya NV, Sterling AE, Mann M, Williams JG. SH2 signaling in a lower eukaryote: a STAT protein that regulates stalk cell differentiation in dictyostelium. Cell. 89:1997;909-916.
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(1997)
Cell
, vol.89
, pp. 909-916
-
-
Kawata, T.1
Shevchenko, A.2
Fukuzawa, M.3
Jermyn, K.A.4
Totty, N.F.5
Zhukovskaya, N.V.6
Sterling, A.E.7
Mann, M.8
Williams, J.G.9
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37
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0030790695
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P47 is a cofactor for p97-mediated membrane fusion
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Kondo H, Rabouille C, Newman R, Levine TP, Pappin D, Freemont P, Warren G. p47 is a cofactor for p97-mediated membrane fusion. Nature. 388:1997;75-78.
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Nature
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Kondo, H.1
Rabouille, C.2
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Levine, T.P.4
Pappin, D.5
Freemont, P.6
Warren, G.7
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38
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17344377424
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A novel Rab5 GDP/GTP exchange factor complexed to Rabaptin-5 links nucleotide exchange to effector recruitment and function
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Horiuchi H, Lippe R, McBride HM, Rubino M, Woodman P, Stenmark H, Rybin V, Wilm M, Ashman K, Mann M, Zerial M. A novel Rab5 GDP/GTP exchange factor complexed to Rabaptin-5 links nucleotide exchange to effector recruitment and function. Cell. 90:1997;1149-1159.
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Horiuchi, H.1
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McBride, H.M.3
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Woodman, P.5
Stenmark, H.6
Rybin, V.7
Wilm, M.8
Ashman, K.9
Mann, M.10
Zerial, M.11
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39
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0031029388
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Identification of the proteins of the yeast U1 small nuclear ribonucleoprotein complex by mass spectrometry
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of special interest. This study represents the first report on the identification of members of an entire multiprotein complex by mass spectrometry. All previously known members of the complex were identified by peptide sequence tags following immunoaffinity chromatography and SDS-PAGE. Four additional proteins were identified and subsequently shown to play a role within the protein complex.
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Neubauer G, Gottschalk A, Fabrizio P, Seraphin B, Luhrmann R, Mann M. Identification of the proteins of the yeast U1 small nuclear ribonucleoprotein complex by mass spectrometry. of special interest Proc Natl Acad Sci. 94:1997;385-390 This study represents the first report on the identification of members of an entire multiprotein complex by mass spectrometry. All previously known members of the complex were identified by peptide sequence tags following immunoaffinity chromatography and SDS-PAGE. Four additional proteins were identified and subsequently shown to play a role within the protein complex.
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Proc Natl Acad Sci
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Neubauer, G.1
Gottschalk, A.2
Fabrizio, P.3
Seraphin, B.4
Luhrmann, R.5
Mann, M.6
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40
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0030839857
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Chromatin-remodelling factor CHRAC contains the ATPases ISWI and topoisomerase II
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Varga-Weisz PD, Wilm M, Bonte E, Dumas K, Mann M, Becker PB. Chromatin-remodelling factor CHRAC contains the ATPases ISWI and topoisomerase II. Nature. 388:1997;598-602.
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(1997)
Nature
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Varga-Weisz, P.D.1
Wilm, M.2
Bonte, E.3
Dumas, K.4
Mann, M.5
Becker, P.B.6
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41
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0030685825
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IKK-1 and IKK-2: Cytokine-activated IkappaB kinases essential for NF- kappaB activation
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Mercurio F, Zhu H, Murray BW, Shevchenko A, Bennett BL, Li J, Young DB, Barbosa M, Mann M, Manning A, Rao A. IKK-1 and IKK-2: cytokine-activated IkappaB kinases essential for NF- kappaB activation. Science. 278:1997;860-866.
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Science
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Mercurio, F.1
Zhu, H.2
Murray, B.W.3
Shevchenko, A.4
Bennett, B.L.5
Li, J.6
Young, D.B.7
Barbosa, M.8
Mann, M.9
Manning, A.10
Rao, A.11
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42
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0030702085
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The exosome: A conserved eukaryotic RNA processing complex containing multiple 3′→5′ exoribonucleases
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Mitchell P, Petfalski E, Shevchenko A, Mann M, Tollervey D. The exosome: a conserved eukaryotic RNA processing complex containing multiple 3′→5′ exoribonucleases. Cell. 91:1997;457-466.
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Cell
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Mitchell, P.1
Petfalski, E.2
Shevchenko, A.3
Mann, M.4
Tollervey, D.5
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43
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0032549115
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Mass spectrometric analysis of the anaphase-promoting complex from yeast: Identification of a subunit related to cullins
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Zachariae W, Shevchenko A, Andrews PD, Ciosk R, Galova M, Stark MJR, Mann M, Nasmyth K. Mass spectrometric analysis of the anaphase-promoting complex from yeast: identification of a subunit related to cullins. Science. 279:1998;1216-1219.
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Science
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Zachariae, W.1
Shevchenko, A.2
Andrews, P.D.3
Ciosk, R.4
Galova, M.5
Stark, M.J.R.6
Mann, M.7
Nasmyth, K.8
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44
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0029033175
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Progress with gene-product mapping of the Mollicutes: Mycoplasma genitalium
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Wasinger VC, Cordwell SJ, Cerpa-Poljak A, Yan JX, Gooley AA, Wilkins MR, Duncan MW, Harris R, Williams KL, Humphrey-Smith I. Progress with gene-product mapping of the Mollicutes: Mycoplasma genitalium. Electrophoresis. 16:1995;1090-1094.
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Wasinger, V.C.1
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Cerpa-Poljak, A.3
Yan, J.X.4
Gooley, A.A.5
Wilkins, M.R.6
Duncan, M.W.7
Harris, R.8
Williams, K.L.9
Humphrey-Smith, I.10
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45
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13344269000
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From proteins to proteosomes: Large scale protein identification by two-dimensional electrophoresis and amino acid analysis
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Wilkins MR, Pasquali C, Appel RD, Ou K, Golaz O, Sanchez JC, Yan JX, Gooley AA, Hughes G, Humphery-Smith I, et al. From proteins to proteosomes: large scale protein identification by two-dimensional electrophoresis and amino acid analysis. Biotechnology. 14:1996;61-65.
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Wilkins, M.R.1
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Ou, K.4
Golaz, O.5
Sanchez, J.C.6
Yan, J.X.7
Gooley, A.A.8
Hughes, G.9
Humphery-Smith, I.10
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46
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0030751010
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Proteome research: Complementarity and limitations with respect to the RNA and DNA worlds
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Humphery-Smith I, Cordwell SJ, Blackstock WP. Proteome research: complementarity and limitations with respect to the RNA and DNA worlds. Electrophoresis. 18:1997;1217-1242.
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Electrophoresis
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Humphery-Smith, I.1
Cordwell, S.J.2
Blackstock, W.P.3
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47
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0031133487
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Automation of matrix-assisted laser desorption/ionization mass spectrometry using fuzzy logic feedback control
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of special interest. An automated, high throughput protein identification strategy was devised based upon MALDI peptide mapping. A key element was the use of fuzzy logic feedback control to adjust the laser fluence during spectra acquisition in order to ensure high data quality. Integration of this control element with software tools for automatic mass calibration, peak labeling and database searching allowed the unattended analysis of 78 samples within four hours.
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Jensen ON, Mortensen P, Vorm O, Mann M. Automation of matrix-assisted laser desorption/ionization mass spectrometry using fuzzy logic feedback control. of special interest Anal Chem. 69:1997;1706-1714 An automated, high throughput protein identification strategy was devised based upon MALDI peptide mapping. A key element was the use of fuzzy logic feedback control to adjust the laser fluence during spectra acquisition in order to ensure high data quality. Integration of this control element with software tools for automatic mass calibration, peak labeling and database searching allowed the unattended analysis of 78 samples within four hours.
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Anal Chem
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Jensen, O.N.1
Mortensen, P.2
Vorm, O.3
Mann, M.4
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48
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10544244161
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Linking genome and proteome by mass spectrometry: Large-scale identification of yeast proteins from two dimensional gels
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Shevchenko A, Jensen ON, Podtelejnikov AV, Sagliocco F, Wilm M, Vorm O, Mortensen P, Shevchenko A, Boucherie H, Mann M. Linking genome and proteome by mass spectrometry: large-scale identification of yeast proteins from two dimensional gels. Proc Natl Acad Sci USA. 93:1996;14440-14445.
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Proc Natl Acad Sci USA
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Shevchenko, A.1
Jensen, O.N.2
Podtelejnikov, A.V.3
Sagliocco, F.4
Wilm, M.5
Vorm, O.6
Mortensen, P.7
Shevchenko, A.8
Boucherie, H.9
Mann, M.10
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49
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0030805824
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Two-dimensional map of Haemophilus influenzae following protein enrichment by heparin chromatography
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of special interest. MALDI peptide mapping was used as the primary tool for the dentification of proteins from Haemophilus influenzae that were separated by 2D gels. Low copy number gene products were enriched by heparin chromatography, which has an affinity for growth and protein biosynthesis factors. Out of 160 protein spots analyzed, 110 corresponded to newly identified proteins. See also [50].
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Fountoulakis M, Langen H, Evers S, Gray C, Takacs B. Two-dimensional map of Haemophilus influenzae following protein enrichment by heparin chromatography. of special interest Electrophoresis. 18:1997;1193-1202 MALDI peptide mapping was used as the primary tool for the dentification of proteins from Haemophilus influenzae that were separated by 2D gels. Low copy number gene products were enriched by heparin chromatography, which has an affinity for growth and protein biosynthesis factors. Out of 160 protein spots analyzed, 110 corresponded to newly identified proteins. See also [50].
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Electrophoresis
, vol.18
, pp. 1193-1202
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Fountoulakis, M.1
Langen, H.2
Evers, S.3
Gray, C.4
Takacs, B.5
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50
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0030751012
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Identifying the major proteome components of Haemophilus influenzae type-strain NCTC 8143
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of special interest. LC/MS/MS was used as the exclusive tool for the identification of proteins from Haemophilus influenzae that were separated by 2D gels. Automatic LC/MS/MS enabled the analysis of 300 out of a total of 400 protein spots, at a rate of 22 proteins per day. Several proteins that were not annotated in the genomic sequence were identified in this study. See also [49].
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Link AJ, Hays LG, Carmack EB, Yates JR. Identifying the major proteome components of Haemophilus influenzae type-strain NCTC 8143. of special interest Electrophoresis. 18:1997;1314-1334 LC/MS/MS was used as the exclusive tool for the identification of proteins from Haemophilus influenzae that were separated by 2D gels. Automatic LC/MS/MS enabled the analysis of 300 out of a total of 400 protein spots, at a rate of 22 proteins per day. Several proteins that were not annotated in the genomic sequence were identified in this study. See also [49].
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(1997)
Electrophoresis
, vol.18
, pp. 1314-1334
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Link, A.J.1
Hays, L.G.2
CarMacK, E.B.3
Yates, J.R.4
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51
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0001900596
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Identification of common post-translational modifications
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Creighton T. edn 2 New York: Oxford University Press
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Krishna R, Wod F. Identification of common post-translational modifications. Creighton T. edn 2 Protein Structure - A Practical Approach. 1997;91-116 Oxford University Press, New York.
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Protein Structure - a Practical Approach
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Krishna, R.1
Wod, F.2
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52
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53249113519
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The essential role of mass spectrometry in characterizing protein structure: Mapping posttranslational modifications
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Annan RS, Carr SA. The essential role of mass spectrometry in characterizing protein structure: mapping posttranslational modifications. J Protein Chem. 16:1997;391-402.
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J Protein Chem
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Annan, R.S.1
Carr, S.A.2
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53
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0030612012
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Phosphorylation of Sic1p by G1 Cdk required for its degradation and entry into S phase
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1 to the S phase in the cell cycle. Phosphorylated peptides were identified by LC/MS and individual phosphorylation sites were identified by nanoelectrospray tandem mass spectrometry.
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1 to the S phase in the cell cycle. Phosphorylated peptides were identified by LC/MS and individual phosphorylation sites were identified by nanoelectrospray tandem mass spectrometry.
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(1997)
Science
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, pp. 455-460
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Verma, R.1
Annan, R.S.2
Huddleston, M.J.3
Carr, S.A.4
Reynard, G.5
Deshaies, R.J.6
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54
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0031081363
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Detection of modified peptides in enzymatic digests by capillary liquid chromatography/electrospray mass spectrometry and a programmable skimmer CID acquisition routine
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of special interest. In an extension to a previously established LC/MS technique for the detection of modified peptides [52], a programmable CID acquisition routine allowed the detection of multiple peptide modifications in a single LC/MS experiment. Mixtures of phosphorylated, glycosylated, sulfated and acrylamidated peptides derived from digests of model proteins could be analyzed in the subpicomole range.
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Jedrzejewski PT, Lehmann WD. Detection of modified peptides in enzymatic digests by capillary liquid chromatography/electrospray mass spectrometry and a programmable skimmer CID acquisition routine. of special interest Anal Chem. 69:1997;294-301 In an extension to a previously established LC/MS technique for the detection of modified peptides [52], a programmable CID acquisition routine allowed the detection of multiple peptide modifications in a single LC/MS experiment. Mixtures of phosphorylated, glycosylated, sulfated and acrylamidated peptides derived from digests of model proteins could be analyzed in the subpicomole range.
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Anal Chem
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Jedrzejewski, P.T.1
Lehmann, W.D.2
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55
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0030033198
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Parent ion scans of unseparated peptide mixtures
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Wilm M, Neubauer G, Mann M. Parent ion scans of unseparated peptide mixtures. Anal Chem. 68:1996;527-533.
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(1996)
Anal Chem
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Wilm, M.1
Neubauer, G.2
Mann, M.3
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56
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0031013632
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Parent ion scans of large molecules
-
of special interest. In this study, the use of precursor ion scans for the selective detection of peptides and post-translational modifications was extended to the analysis of proteins and oligonucleotides. Phospho- and glycoproteins could be distinguished from nonmodified proteins by monitoring fragment ions specific to the respective modification. The technique was found to be of particular value when high levels of chemical noise hamper the direct detection of proteins and oligonucleotides.
-
Neubauer G, Mann M. Parent ion scans of large molecules. of special interest J Mass Spectrometry. 32:1997;94-98 In this study, the use of precursor ion scans for the selective detection of peptides and post-translational modifications was extended to the analysis of proteins and oligonucleotides. Phospho- and glycoproteins could be distinguished from nonmodified proteins by monitoring fragment ions specific to the respective modification. The technique was found to be of particular value when high levels of chemical noise hamper the direct detection of proteins and oligonucleotides.
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(1997)
J Mass Spectrometry
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Neubauer, G.1
Mann, M.2
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57
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0030914528
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Identification of phosphorylation sites on neurofilament proteins by nanoelectrospray mass spectrometry
-
of special interest. Phosphorylation sites on neurofilament protein subunits were identified by nanoelectrospray parent ion scanning following SDS-PAGE and purification by immobilized metal affinity chromatography. The analysis showed that some phosphorylation sites are only transiently occupied, which suggests a role in filament assembly.
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Betts JC, Blackstock WP, Ward MA, Anderton BH. Identification of phosphorylation sites on neurofilament proteins by nanoelectrospray mass spectrometry. of special interest J Biol Chem. 272:1997;12922-12927 Phosphorylation sites on neurofilament protein subunits were identified by nanoelectrospray parent ion scanning following SDS-PAGE and purification by immobilized metal affinity chromatography. The analysis showed that some phosphorylation sites are only transiently occupied, which suggests a role in filament assembly.
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J Biol Chem
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Betts, J.C.1
Blackstock, W.P.2
Ward, M.A.3
Anderton, B.H.4
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58
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0031241394
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Identification and characterization of posttranslational modifications of proteins by MALDI ion trap mass spectrometry
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of special interest. This study demonstrates the use of MALDI ion trap MS for the analysis of a number of post-translational peptide modifications, including phophorylation, glycosylation and disulfide bond formation. The identification of modified peptides within a mixture was not as straightforward as the use of electrospray on scanning instruments, although 'signatures' of modified peptides, such as the loss of 98 Da from phosphopeptides, were apparent from MS/MS spectra.
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Qin J, Chait BT. Identification and characterization of posttranslational modifications of proteins by MALDI ion trap mass spectrometry. of special interest Anal Chem. 69:1997;4002-4009 This study demonstrates the use of MALDI ion trap MS for the analysis of a number of post-translational peptide modifications, including phophorylation, glycosylation and disulfide bond formation. The identification of modified peptides within a mixture was not as straightforward as the use of electrospray on scanning instruments, although 'signatures' of modified peptides, such as the loss of 98 Da from phosphopeptides, were apparent from MS/MS spectra.
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Anal Chem
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Qin, J.1
Chait, B.T.2
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59
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0031028207
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Matrix-assisted laser desorption ionization/quadrupole ion trap mass spectrometry of peptides. Application to the localization of phosphorylation sites on the P protein from Sendai virus
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Jonscher KR, Yates JR. Matrix-assisted laser desorption ionization/quadrupole ion trap mass spectrometry of peptides. Application to the localization of phosphorylation sites on the P protein from Sendai virus. J Biol Chem. 272:1997;1735-1741.
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J Biol Chem
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Jonscher, K.R.1
Yates, J.R.2
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60
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0030048495
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Mass spectrometric characterization of glycosylated interferon-gamma variants separated by gel electrophoresis
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Mortz E, Sareneva T, Haebel S, Julkunen I, Roepstorff P. Mass spectrometric characterization of glycosylated interferon-gamma variants separated by gel electrophoresis. Electrophoresis. 17:1996;925-931.
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Mortz, E.1
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Haebel, S.3
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Roepstorff, P.5
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61
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0031571138
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Sequencing of N-linked oligosaccharides directly from protein gels: In-gel deglycosylation followed by matrix-assisted laser desorption/ionization mass spectrometry and normal-phase high-performance liquid chromatography
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of special interest. In-gel deglycosylation, using peptide-N-glycosidase F in conjunction with MALDI MS, was shown to allow the analysis of the global glycosylation pattern of gel-separated proteins at the 50 picomole level. Deglycosylated proteins were amenable to identification by MALDI peptide mapping and the released oligosaccharides could be sequenced by arrays of exoglycosidases.
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Kuster B, Wheeler SF, Hunter AP, Dwek RA, Harvey DJ. Sequencing of N-linked oligosaccharides directly from protein gels: in-gel deglycosylation followed by matrix-assisted laser desorption/ionization mass spectrometry and normal-phase high-performance liquid chromatography. of special interest Anal Biochem. 250:1997;82-101 In-gel deglycosylation, using peptide-N-glycosidase F in conjunction with MALDI MS, was shown to allow the analysis of the global glycosylation pattern of gel-separated proteins at the 50 picomole level. Deglycosylated proteins were amenable to identification by MALDI peptide mapping and the released oligosaccharides could be sequenced by arrays of exoglycosidases.
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(1997)
Anal Biochem
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, pp. 82-101
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Kuster, B.1
Wheeler, S.F.2
Hunter, A.P.3
Dwek, R.A.4
Harvey, D.J.5
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62
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Oligosaccharide sequencing technology
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Nature
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Rudd, P.M.1
Guile, G.R.2
Kuster, B.3
Harvey, D.J.4
Opdenakker, G.5
Dwek, R.A.6
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63
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