Literature DB >> 12923782

Proteomics application exercise of the Swiss Proteomics Society: report of the SPS'02 session.

Pierre-Alain Binz1, Fadi Abdi, Michael Affolter, Laure Allard, Jachen Barblan, Sanjeev Bhardwaj, Willy V Bienvenut, Philippe Bulet, Jennifer Burgess, Odile Carrette, Garry Corthals, François Delalande, Hélène Diemer, Philippe Favreau, Elia Giuliano, Yannick Gueguen, Elisabeth Guillaume, Stephanie Hahner, Petr Man, Sophie Michalet, Dario Neri, Dimitrios Noukakis, Patricia Palagi, Pierre Paroutaud, Daniel Carvalho Pimenta, Manfredo Quadroni, Anja Resemann, Sophie Richert, Jascha Rybak, Jean-Charles Sanchez, Alexander Scherl, Simone Scheurer, Ulrike Schweiger Hufnagel, Christoph Siethoff, Detlev Suckau, Alain van Dorsselaer, Winfried Wagner Redeker, Nadia Walter, Reto Stöcklin.   

Abstract

After the success of the mass spectrometry (MS) round table that was held at the first Swiss Proteomics Society congress (SPS'01) in Geneva, the SPS has organized a proteomics application exercise and allocated a full session at the SPS'02 congress. The main objective was to encourage the exchange of expertise in protein identification, with a focus on the use of mass spectrometry, and to create a bridge between the users' questions and the instrument providers' solutions. Two samples were sent to fifteen interested labs, including academic groups and MS hardware providers. Participants were asked to identify and partially characterize the samples. They consisted of a complex mixture of peptide/proteins (sample A) and an almost pure recombinant peptide carrying post-translational modifications (sample B). Sample A was an extract of snake venom from the species Bothrops jararaca. Sample B was a recombinant and modified peptide derived from the shrimp Penaeus vannamei penaeidin 3a. The eight labs that returned results reported the use of a wide range of MS instrumentation and techniques. They mentioned a variety of time and manpower allocations. The origin of sample A was generally identified together with a number of database protein entries. The difficulty of the sample identification lay in the incomplete knowledge of the Bothrops species genome sequence and is discussed. Sample B was generally and correctly identified as penaeidin. However, only one group reported the full primary structure. Interestingly, the approaches were again varied and are discussed in the text.

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Year:  2003        PMID: 12923782     DOI: 10.1002/pmic.200300458

Source DB:  PubMed          Journal:  Proteomics        ISSN: 1615-9853            Impact factor:   3.984


  2 in total

1.  Proteomic characterization of two snake venoms: Naja naja atra and Agkistrodon halys.

Authors:  Shuting Li; Jingqiang Wang; Xumin Zhang; Yan Ren; Ning Wang; Kang Zhao; Xishu Chen; Caifeng Zhao; Xiaolei Li; Jianmin Shao; Jianning Yin; Matthew B West; Ningzhi Xu; Siqi Liu
Journal:  Biochem J       Date:  2004-11-15       Impact factor: 3.857

Review 2.  Diversity in penaeidin antimicrobial peptide form and function.

Authors:  Brandon J Cuthbertson; Leesa J Deterding; Jason G Williams; Kenneth B Tomer; Kizee Etienne; Perry J Blackshear; Erika E Büllesbach; Paul S Gross
Journal:  Dev Comp Immunol       Date:  2007-08-03       Impact factor: 3.636

  2 in total

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