Literature DB >> 24825726

Phosphoproteomics in photosynthetic organisms.

William O Slade1, Emily G Werth, Alex Chao, Leslie M Hicks.   

Abstract

As primarily sessile organisms, photosynthetic species survive in dynamic environments by using elegant signaling pathways to manifest molecular responses to extracellular cues. These pathways exploit phosphorylation of specific amino acids (e.g. serine, threonine, tyrosine), which impact protein structure, function, and localization. Despite substantial progress in implementation of phosphoproteomics to understand photosynthetic organisms, researchers still struggle to translate a biological question into an experimental strategy and vice versa. This review evaluates the current status of phosphoproteomics in photosynthetic organisms and concludes with recommendations based on current knowledge.
© 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

Entities:  

Keywords:  Phosphoproteomics; Photosynthetic; Post-translational modifications; Proteomics

Mesh:

Substances:

Year:  2014        PMID: 24825726     DOI: 10.1002/elps.201400154

Source DB:  PubMed          Journal:  Electrophoresis        ISSN: 0173-0835            Impact factor:   3.535


  1 in total

1.  Sample preparation for phosphoproteomic analysis of circadian time series in Arabidopsis thaliana.

Authors:  Johanna Krahmer; Matthew M Hindle; Sarah F Martin; Thierry Le Bihan; Andrew J Millar
Journal:  Methods Enzymol       Date:  2014-12-26       Impact factor: 1.600

  1 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.