ReviewFrontiers in plant science2016
The Use of Advanced Mass Spectrometry to Dissect the Life-Cycle of Photosystem II.
Review in Frontiers in plant science, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
9 citing papers in PubMed.
- High-Light-Induced Degradation of Photosystem II Subunits' Involvement in the Albino Phenotype in Tea Plants.International journal of molecular sciences · 2022Article
- Advances in the Understanding of the Lifecycle of Photosystem II.Microorganisms · 2022Review
- High-resolution cryo-electron microscopy structure of photosystem II from the mesophilic cyanobacterium,Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Structural insights into photosystem II assembly.Nature plants · 2021Article
- Mass Spectrometry-Based Protein Footprinting for Higher-Order Structure Analysis: Fundamentals and Applications.Chemical reviews · 2020Review
- A novel chlorophyll protein complex in the repair cycle of photosystem II.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Reactive oxygen species leave a damage trail that reveals water channels in Photosystem II.Science advances · 2017Article
- The proteolysis adaptor, NblA, binds to the N-terminus of β-phycocyanin: Implications for the mechanism of phycobilisome degradation.Photosynthesis research · 2017Article
- Mass spectrometry-based cross-linking study shows that the Psb28 protein binds to cytochromeProceedings of the National Academy of Sciences of the United States of America · 2017Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Photosystem II (PSII) is a photosynthetic membrane-protein complex that undergoes an intricate, tightly regulated cycle of assembly, damage, and repair. The available crystal structures of cyanobacterial PSII are an essential foundation for understanding PSII function, but nonetheless provide a snapshot only of the active complex. To study aspects of the entire PSII life-cycle, mass spectrometry (MS) has emerged as a powerful tool that can be used in conjunction with biochemical techniques. In this article, we present the MS-based approaches that are used to study PSII composition, dynamics, and structure, and review the information about the PSII life-cycle that has been gained by these methods. This information includes the composition of PSII subcomplexes, discovery of accessory PSII proteins, identification of post-translational modifications and quantification of their changes under various conditions, determination of the binding site of proteins not observed in PSII crystal structures, conformational changes that underlie PSII functions, and identification of water and oxygen channels within PSII. We conclude with an outlook for the opportunity of future MS contributions to PSII research.
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Registered trials
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