Murine cerebellar neurons express a novel gene encoding a protein related to cell cycle control and cell fate determination proteins

Taoka, Masato; Isobe, Toshiaki; Okuyama, T; Watanabe, Mutsufusa; Kondo, Hisatake; Yamakawa, Yoshio; Ozawa, Fumiko; Hishinuma, Fumio; Kubota, Misae; Minegishi, Atsuko

doi:10.1016/s0021-9258(17)36974-0

Cited by 39 publications

(2 citation statements)

References 38 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Almost two decades ago, we presented an automated two-dimensional high-performance liquid chromatography (2DLC) technique for the systematic separation of very complex protein or peptide mixtures − and applied this system for the sequence analysis of very large proteins and protein genetic variants − and for profiling the proteins expressed in the developing rat cerebella. − This technique has currently been refined for a more sophisticated approach by incorporating new MS technology, e.g., replacing the conventional UV detector by MS with an electrospray ionization (ESI) source . Accordingly, the analytical columns were downsized to reduce the LC flow rate, and a small reversed-phase “trap” column was inserted between the two analytical columns to remove the salts from the peptides and proteins eluted from the first ion-exchange column before the MS step.…”

Section: Introductionmentioning

confidence: 99%

Large-Scale Identification of Caenorhabditis elegans Proteins by Multidimensional Liquid Chromatography−Tandem Mass Spectrometry

et al. 2002

View full text Add to dashboard Cite

A proteome of a model organism, Caenorhabditis elegans, was analyzed by an integrated liquid chromatography (LC)-based protein identification system, which was constructed by microscale two-dimensional liquid chromatography (2DLC) coupled with electrospray ionization (ESI) tandem mass spectrometry (MS/MS) on a high-resolution hybrid mass spectrometer with an automated data analysis system. Soluble and insoluble protein fractions were prepared from a mixed growth phase culture of the worm C. elegans, digested with trypsin, and fractionated separately on the 2DLC system. The separated peptides were directly analyzed by on-line ESI-MS/MS in a data-dependent mode, and the resultant spectral data were automatically processed to search a genome sequence database, wormpep 66, for protein identification. The total number of proteins of the composite proteome identified in this method was 1,616, including 110 secreted/targeted proteins and 242 transmembrane proteins. The codon adaptation indices of the identified proteins suggested that the system could identify proteins of relatively low abundance, which are difficult to identify by conventional 2D-gel electrophoresis (GE) followed by an offline mass spectrometric analysis such as peptide mass fingerprinting. Among the approximately 5,400 peptides assigned in this study, many peptides with post-translational modifications, such as N-terminal acetylation and phosphorylation, were detected. This expression profile of C. elegans, containing 571 hypothetical gene products, will serve as the basic data of a major proteome set expressed in the worm.

show abstract

Section: Introductionmentioning

confidence: 99%

Large-Scale Identification of Caenorhabditis elegans Proteins by Multidimensional Liquid Chromatography−Tandem Mass Spectrometry

et al. 2002

View full text Add to dashboard Cite

show abstract

“…The model has been applied to describe the folding of many proteins [12][13][14][15][16][17][18][19][20] , and also to the study of force-induced denaturation of proteins and RNA [21][22][23][24][25] . We apply the WSME model to the study of Myotrophin, a 118 residues protein, ubiquitously expressed in all mammalian tissues [26][27][28][29] , made up of four ankyrin repeats. Its equilibrium has been characterized experimentally as two-state by Peng and coworkers 30 with thermal and chemical denaturation experiments, and later confirmed as such, at least as far as chemical denaturations is concerned, by Lowe and Itzhaki 31 , that also studied the kinetics 31,32 .…”

Section: Introductionmentioning

confidence: 99%

Analysis of the equilibrium and kinetics of the ankyrin repeat protein myotrophin

Faccin

Bruscolini

Pelizzola

2011

The Journal of Chemical Physics

View full text Add to dashboard Cite

We apply the Wako-Saito-Muñoz-Eaton model to the study of Myotrophin, a small ankyrin repeat protein, whose folding equilibrium and kinetics have been recently characterized experimentally. The model, which is a native-centric with binary variables, provides a finer microscopic detail than the Ising model, that has been recently applied to some different repeat proteins, while being still amenable for an exact solution. In partial agreement with the experiments, our results reveal a weakly three-state equilibrium and a two-state-like kinetics of the wild type protein despite the presence of a non-trivial free-energy profile. These features appears to be related to a careful "design" of the free-energy landscape, so that mutations can alter this picture, stabilizing some intermediates and changing the position of the rate-limiting step. Also the experimental findings of two alternative pathways, an N-terminal and a C-terminal one, are qualitatively confirmed, even if the variations in the rates upon the experimental mutations cannot be quantitatively reproduced. Interestingly, folding and unfolding pathway appear to be different, even if closely related: a property that is not generally considered in the phenomenological interpretation of the experimental data.

show abstract

Profiling ofCaenorhabditis elegans proteins using two-dimensional gel electrophoresis and matrix assisted laser desorption/ionization-time of flight-mass spectrometry

et al. 2000

View full text Add to dashboard Cite

Murine cerebellar neurons express a novel gene encoding a protein related to cell cycle control and cell fate determination proteins

Cited by 39 publications

References 38 publications

Large-Scale Identification of Caenorhabditis elegans Proteins by Multidimensional Liquid Chromatography−Tandem Mass Spectrometry

Large-Scale Identification of Caenorhabditis elegans Proteins by Multidimensional Liquid Chromatography−Tandem Mass Spectrometry

Analysis of the equilibrium and kinetics of the ankyrin repeat protein myotrophin

Profiling ofCaenorhabditis elegans proteins using two-dimensional gel electrophoresis and matrix assisted laser desorption/ionization-time of flight-mass spectrometry

Contact Info

Product

Resources

About