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ALICE Commissioning: Getting Ready for Physics
Lippmann, C
arXiv.org, May 11, 2009
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Title: ALICE Commissioning: Getting Ready for Physics
Author: Lippmann, C
Contributor: Lippmann, C (pacrepositoryorg)
Subject: Commissioning ; Large Hadron Collider ; Ion Detectors ; Subsystems
Description: ALICE is a general-purpose heavy-ion detector at the CERN LHC. We describe the commissioning activities in the years 2007-2009 and the status of the different subsystems at the time of this conference.
Is part of: arXiv.org, May 11, 2009
Identifier: 2331-8422 (E-ISSN)

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ALICE Commissioning: Getting Ready for Physics
Lippmann, C.
Cornell University

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Title: ALICE Commissioning: Getting Ready for Physics
Author: Lippmann, C.
Subject: Nuclear Experiment
Description: ALICE is a general-purpose heavy-ion detector at the CERN LHC. We describe the commissioning activities in the years 2007-2009 and the status of the different subsystems at the time of this conference. Comment: Proceedings for the Rencontres de Moriond (2009 QCD session). 4 pages, 3 figures
Identifier: 0905.1565 (ARXIV ID)

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The Time Projection Chamber for the ALICE Experiment
Lippmann, C
arXiv.org, Oct 6, 2008
© ProQuest LLC All rights reserved, Engineering Database, Publicly Available Content Database, ProQuest Engineering Collection, ProQuest Technology Collection, ProQuest SciTech Collection, Materials Science & Engineering Database, ProQuest Central (new), ProQuest Central Korea, SciTech Premium Collection, Technology Collection, ProQuest Central Essentials, ProQuest One Academic, Engineering Collection (ProQuest)

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Title: The Time Projection Chamber for the ALICE Experiment
Author: Lippmann, C
Contributor: Lippmann, C (pacrepositoryorg)
Subject: Cosmic Rays ; Krypton ; Radiation Counters ; Signal Processing ; Large Hadron Collider ; Cosmic Rays ; Ultraviolet Lasers ; Energy Dissipation ; Krypton Isotopes
Description: The Time Projection Chamber of the ALICE Experiment has been installed in the experimental setup in the underground area at the Large Hadron Collider at CERN in Geneva. The Alice TPC ReadOut (ALTRO) chip implements intelligent signal processing on the Front-End-Electronics. During the years of 2007 and 2008 commissioning and calibration of the TPC have been carried out with cosmic rays, radioactive Krypton isotopes and with tracks produced by a UV laser system. In addition to these in this publication we present first results on energy loss measurements and on the momentum resolution.
Is part of: arXiv.org, Oct 6, 2008
Identifier: 2331-8422 (E-ISSN)

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Phosphorylation of elongation factor Tu prevents ternary complex formation
Alexander, C, Bilgin, N, Lindschau, C, Mesters, J R, Kraal, B, Hilgenfeld, R, Erdmann, V A, Lippmann, C
The Journal of biological chemistry, 16 June 1995, Vol.270(24), pp.14541-7 [Peer Reviewed Journal]

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RCU2-The ALICE TPC readout electronics consolidation for Run2
Alme, J., Alt, T., Bratrud, L., Christiansen, Peter, Costa, F., David, E., Gunji, T., Kiss, T., Langoy, R., Lien, J., Lippmann, C., Oskarsson, Anders, Rehman, A. Ur, Roed, K., Rohrich, D., Tarantola, A., Torgersen, C., Torsvik, I. Nikolai, Ullaland, K., Velure
Journal of Instrumentation, 2013, Vol.8 [Peer Reviewed Journal]
SwePub (National Library of Sweden)

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Title: RCU2-The ALICE TPC readout electronics consolidation for Run2
Author: Alme, J.; Alt, T.; Bratrud, L.; Christiansen, Peter; Costa, F.; David, E.; Gunji, T.; Kiss, T.; Langoy, R.; Lien, J.; Lippmann, C.; Oskarsson, Anders; Rehman, A. Ur; Roed, K.; Rohrich, D.; Tarantola, A.; Torgersen, C.; Torsvik, I. Nikolai; Ullaland, K.; Velure
Subject: Electronics For Detector Readout ; Liquid) ; Electronic Detector Readout Concepts (Gas ; Front-End ; Data Acquisition Concepts ; Digital ; Electronic Circuits ; Naturvetenskap ; Fysik ; Acceleratorfysik Och Instrumentering ; Natural Sciences ; Physical Sciences ; Accelerator Physics And Instrumentation
Description: This paper presents the solution for optimization of the ALICE TPC readout for running at full energy in the Run2 period after 2014. For the data taking with heavy ion beams an event readout rate of 400 Hz with a low dead time is envisaged for the ALICE central barrel detectors during these three years. A new component, the Readout Control Unit 2 (RCU2), is being designed to increase the present readout rate by a factor of up to 2.6. The immunity to radiation induced errors will also be significantly improved by the new design.
Is part of: Journal of Instrumentation, 2013, Vol.8
Identifier: 1748-0221 (ISSN); 1748-0221 (ISSN); 10.1088/1748-0221/8/12/C12032 (DOI)

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Identification of the phosphorylation sites of the murine small heat shock protein hsp25
Gaestel, M, Schröder, W, Benndorf, R, Lippmann, C, Buchner, K, Hucho, F, Erdmann, V A, Bielka, H
The Journal of biological chemistry, 05 August 1991, Vol.266(22), pp.14721-4 [Peer Reviewed Journal]
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Title: Identification of the phosphorylation sites of the murine small heat shock protein hsp25
Author: Gaestel, M; Schröder, W; Benndorf, R; Lippmann, C; Buchner, K; Hucho, F; Erdmann, V A; Bielka, H
Subject: Heat-Shock Proteins -- Metabolism
Description: Native phosphorylated mouse small heat shock protein hsp25 from Ehrlich ascites tumor cells was isolated and the in vivo phosphorylation sites of the protein were determined. Furthermore, native hsp25 was phosphorylated by the endogenous kinase(s) in a cell-free system as well as recombinant hsp25 was phosphorylated in vitro by protein kinase C and catalytic subunit of cAMP-dependent protein kinase. The two major phosphorylation sites of native and recombinant hsp25 were determined as Ser-15 and Ser-86. There are no differences in the hsp25 phosphorylation sites phosphorylated by the protein kinase C, the catalytic subunit of cAMP-dependent protein kinase and the unknown intracellular kinase(s). The serine residues identified exist in all known small mammalian stress proteins and are located in the conserved kinase recognition sequence Arg-X-X-Ser.
Is part of: The Journal of biological chemistry, 05 August 1991, Vol.266(22), pp.14721-4
Identifier: 0021-9258 (ISSN); 1860870 Version (PMID)

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Prokaryotic elongation factor Tu is phosphorylated in vivo
Lippmann, C, Lindschau, C, Vijgenboom, E, Schröder, W, Bosch, L, Erdmann, V A
The Journal of biological chemistry, 05 January 1993, Vol.268(1), pp.601-7 [Peer Reviewed Journal]
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Title: Prokaryotic elongation factor Tu is phosphorylated in vivo
Author: Lippmann, C; Lindschau, C; Vijgenboom, E; Schröder, W; Bosch, L; Erdmann, V A
Subject: Escherichia Coli -- Metabolism ; Peptide Elongation Factor Tu -- Metabolism ; Thermus Thermophilus -- Metabolism
Description: Covalent modification of proteins by phosphate transfer reactions constitutes a major mechanism of regulation in higher eukaryotes. Recently, phosphorylation of eukaryotic elongation factors has been described. Analysis of Escherichia coli proteins revealed several of them to be phosphorylated. Various lines of evidence lead us to conclude that one of these proteins is identical to elongation factor (EF) Tu, which can be phosphorylated in vivo at one of its threonine residues. Structural analysis showed that one fragment of the phosphorylated EF-Tu is highly resistant to tryptic digestion. Phosphorylation of eubacterial EF-Tu is not restricted to the E. coli factor but could also be demonstrated for Thermus thermophilus HB8 EF-Tu. Overexpression of tufA did not increase the number of EF-Tu molecules to be phosphorylated. This may indicate that a constant but limited amount of EF-Tu is modified, possibly for a specific function. Phosphorylation of EF-Tu could also be demonstrated in vitro....
Is part of: The Journal of biological chemistry, 05 January 1993, Vol.268(1), pp.601-7
Identifier: 0021-9258 (ISSN); 8416965 Version (PMID)

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Crystallization and preliminary X-ray diffraction studies of intact EF-Tu from Thermus aquaticus YT-1
Lippmann, C, Betzel, C, Dauter, Z, Wilson, K, Erdmann, V A
FEBS letters, 21 November 1988, Vol.240(1-2), pp.139-42 [Peer Reviewed Journal]
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Title: Crystallization and preliminary X-ray diffraction studies of intact EF-Tu from Thermus aquaticus YT-1
Author: Lippmann, C; Betzel, C; Dauter, Z; Wilson, K; Erdmann, V A
Subject: Peptide Elongation Factor Tu ; Thermus -- Enzymology
Description: Many attempts have been made to elucidate the three-dimensional structure from elongation factor Tu, but so far the only crystals suitable for X-ray crystallography contained a partially degraded protein. Here, we report the crystallization of a fully active, intact EF-Tu from thermus aquaticus. The crystals belong to hexagonal space group P6(3)(22) and diffract up to 2.6 A. The cell dimensions are a = b = 178 A, c = 238 A and 6 molecules are contained per asymmetric unit.
Is part of: FEBS letters, 21 November 1988, Vol.240(1-2), pp.139-42
Identifier: 0014-5793 (ISSN); 3142792 Version (PMID)

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First performance results of the ALICE TPC Readout Control Unit 2
Zhao, Chengxin, Alme, Johan, Alt, Torsten, Appelshäuser, Harald, Bratrud, Lars Karlot Stubberud, Castro, Andrew, Costa, Filippo, David, Ernö, Gunji, T, Kirsch, S, Kiss, Tivadar, Langøy, Rune, Lien, Jørgen, Lippmann, C, Oskarsson, Anders, Rehman, Attiq Ur, Røed, Ketil, Røhrich, Dieter, Sekiguchi, Yoko, Stuart, Meghan, Ullaland, Kjetil, Velure, Arild, Yang, Shiming, Österman, Lennart
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Title: First performance results of the ALICE TPC Readout Control Unit 2
Author: Zhao, Chengxin; Alme, Johan; Alt, Torsten; Appelshäuser, Harald; Bratrud, Lars Karlot Stubberud; Castro, Andrew; Costa, Filippo; David, Ernö; Gunji, T; Kirsch, S; Kiss, Tivadar; Langøy, Rune; Lien, Jørgen; Lippmann, C; Oskarsson, Anders; Rehman, Attiq Ur; Røed, Ketil; Røhrich, Dieter; Sekiguchi, Yoko; Stuart, Meghan; Ullaland, Kjetil; Velure, Arild; Yang, Shiming; Österman, Lennart
Date: 2016
Description: -
This paper presents the first performance results of the ALICE TPC Readout Control Unit 2 (RCU2). With the upgraded hardware typology and the new readout scheme in FPGA design, the RCU2 is designed to achieve twice the readout speed of the present Readout Control Unit. Design choices such as using the flash-based Microsemi Smartfusion2 FPGA and applying mitigation techniques in interfaces and FPGA design ensure a high degree of radiation tolerance. This paper presents the system level irradiation test results as well as the first commissioning results of the RCU2. Furthermore, it will be concluded with a discussion of the planned updates in firmware.

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The Time Projection Chamber for the ALICE Experiment
Lippmann, C., Collaboration, The Alice Tpc
Cornell University

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Title: The Time Projection Chamber for the ALICE Experiment
Author: Lippmann, C.; Collaboration, The Alice Tpc
Subject: Nuclear Experiment
Description: The Time Projection Chamber of the ALICE Experiment has been installed in the experimental setup in the underground area at the Large Hadron Collider at CERN in Geneva. The Alice TPC ReadOut (ALTRO) chip implements intelligent signal processing on the Front-End-Electronics. During the years of 2007 and 2008 commissioning and calibration of the TPC have been carried out with cosmic rays, radioactive Krypton isotopes and with tracks produced by a UV laser system. In addition to these in this publication we present first results on energy loss measurements and on the momentum resolution. Comment: ICHEP08
Identifier: 0809.5133 (ARXIV ID)

Phosphorylation of elongation factor Tu prevents ternary complex formation