Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Claudia C. Bicho"'
Autor:
Boris Macek, Kenneth E. Sawin, André Koch, Alejandro Carpy, Silke Hauf, Claudia C. Bicho, Weronika E. Borek
Publikováno v:
Cold Spring Harbor protocols. 2017(6)
Shotgun proteomics combined with stable isotope labeling by amino acids in cell culture (SILAC) is a powerful approach to quantify proteins and posttranslational modifications across the entire proteome. SILAC technology in Schizosaccharomyces pombe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::15b05695e52e66de2c3d1f78001c8fc2
https://pubmed.ncbi.nlm.nih.gov/28572211
https://pubmed.ncbi.nlm.nih.gov/28572211
Autor:
Weronika E. Borek, Kenneth E. Sawin, Boris Macek, Claudia C. Bicho, Alejandro Carpy, André Koch, Silke Hauf
Publikováno v:
Cold Spring Harbor Protocols. 2017:pdb.prot091686
Modern mass spectrometry (MS)-based approaches are capable of identifying and quantifying thousands of proteins and phosphorylation events in a single biological experiment. Here we present a (phospho)proteomic workflow based on in-solution proteome
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a003018ce50542dac3353d096e6417b8
https://doi.org/10.1101/pdb.prot091686
https://doi.org/10.1101/pdb.prot091686
Autor:
André Koch, Kenneth E. Sawin, Silke Hauf, Alejandro Carpy, Boris Macek, Weronika E. Borek, Claudia C. Bicho
Publikováno v:
Cold Spring Harbor Protocols. 2017:pdb.prot091678
Stable isotope labeling by amino acids in cell culture (SILAC) enables the relative quantification of protein amounts and posttranslational modifications in complex biological samples through the use of stable heavy isotope–labeled amino acids. Her
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c3438521e29f362e045ff990c297f952
https://doi.org/10.1101/pdb.prot091678
https://doi.org/10.1101/pdb.prot091678
Autor:
Sergio A. Rincón, Weronika E. Borek, Kenneth E. Sawin, Flavia de Lima Alves, Vincent Fraisier, Mercè Guzman-Vendrell, Anne Paoletti, Sophie G. Martin, Damarys Loew, Payal Bhatia, Claudia C. Bicho, Juri Rappsilber, Florent Dingli
Publikováno v:
Rincon, S A, Bhatia, P, Bicho, C, Guzman-Vendrell, M, Fraisier, V, Borek, W E, Alves, F D L, Dingli, F, Loew, D, Rappsilber, J, Sawin, K E, Martin, S G & Paoletti, A 2014, ' Pom1 regulates the assembly of Cdr2-Mid1 cortical nodes for robust spatial control of cytokinesis ', Journal of Cell Biology, vol. 206, no. 1, pp. 61-77 . https://doi.org/10.1083/jcb.201311097
Journal of Cell Biology, vol. 206, no. 1, pp. 61-77
The Journal of Cell Biology
Journal of Cell Biology, vol. 206, no. 1, pp. 61-77
The Journal of Cell Biology
Pom1 regulation of Cdr2 membrane association and interaction with Mid1 prevents Cdr2 assembly into stable nodes in the cell tip region, which ensures proper positioning of cytokinetic ring precursors and accurate division plane positioning in fission
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7ea9d32419d3b299622f325a46f79bfe
https://www.pure.ed.ac.uk/ws/files/17409894/61.full.pdf
https://www.pure.ed.ac.uk/ws/files/17409894/61.full.pdf
Publikováno v:
Molecular & Cellular Proteomics : MCP
Bicho, C C, Alves, F D L, Chen, Z A, Rappsilber, J & Sawin, K E 2010, ' A Genetic Engineering Solution to the “Arginine Conversion Problem” in Stable Isotope Labeling by Amino Acids in Cell Culture (SILAC) ', Molecular and Cellular Proteomics, vol. 9, no. 7, pp. 1567-1577 . https://doi.org/10.1074/mcp.M110.000208
Bicho, C C, Alves, F D L, Chen, Z A, Rappsilber, J & Sawin, K E 2010, ' A Genetic Engineering Solution to the “Arginine Conversion Problem” in Stable Isotope Labeling by Amino Acids in Cell Culture (SILAC) ', Molecular and Cellular Proteomics, vol. 9, no. 7, pp. 1567-1577 . https://doi.org/10.1074/mcp.M110.000208
Stable isotope labeling by amino acids in cell culture (SILAC) provides a straightforward tool for quantitation in proteomics. However, one problem associated with SILAC is the in vivo conversion of labeled arginine to other amino acids, typically pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cbf3e3543cb5ec4cc188d1d6e298bd12
https://pubmed.ncbi.nlm.nih.gov/20460254
https://pubmed.ncbi.nlm.nih.gov/20460254
Publikováno v:
Current Biology
Bicho, C C, Kelly, D A, Snaith, H A, Goryachev, A B & Sawin, K E 2010, ' A Catalytic Role for Mod5 in the Formation of the Tea1 Cell Polarity Landmark ', Current Biology, vol. 20, no. 19, pp. 1752-1757 . https://doi.org/10.1016/j.cub.2010.08.035
Bicho, C C, Kelly, D A, Snaith, H A, Goryachev, A B & Sawin, K E 2010, ' A Catalytic Role for Mod5 in the Formation of the Tea1 Cell Polarity Landmark ', Current Biology, vol. 20, no. 19, pp. 1752-1757 . https://doi.org/10.1016/j.cub.2010.08.035
Summary Many systems regulating cell polarity involve stable landmarks defined by internal cues [1–5]. In the rod-shaped fission yeast Schizosaccharomyces pombe, microtubules regulate polarized vegetative growth via a landmark involving the protein
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::443dfa6778da6e0615ee2df179755aa2
https://pubmed.ncbi.nlm.nih.gov/20850323
https://pubmed.ncbi.nlm.nih.gov/20850323
Publikováno v:
Analytical Biochemistry
Immunoglobulin G (IgG)–Sepharose is often used for purification of protein A- and tandem affinity purification (TAP)-tagged proteins from eukaryotic cells, but because it is based on an agarose matrix, it is not always optimal for all proteins. Syn
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c34d7cbd628ea4cc84a4de8baafb3d98