Comparative crosslinking and mass spectrometry of an intact F-type ATPase suggest a role for phosphorylation in regulating subunit interactions and nucleotide occupancy

Carla Schmidt; Hazel Marriott; Min Zhou; Nina Morgner; Argyris Politis; Carol Robinson

doi:10.1038/ncomms2985

Comparative crosslinking and mass spectrometry of an intact F-type ATPase suggest a role for phosphorylation in regulating subunit interactions and nucleotide occupancy

Carla Schmidt, Hazel Marriott, Min Zhou, Nina Morgner, Argyris Politis, Carol Robinson

Biomedical Sciences Research

Research output: Contribution to journal › Article › peer-review

117 Citations (Scopus)

Original language	English
Journal	Nature Communications
Volume	1985
DOIs	https://doi.org/10.1038/ncomms2985
Publication status	Published (in print/issue) - 12 Jun 2013

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10.1038/ncomms2985

http://uir.ulster.ac.uk/28543/1/ncomms2985.pdf

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title = "Comparative crosslinking and mass spectrometry of an intact F-type ATPase suggest a role for phosphorylation in regulating subunit interactions and nucleotide occupancy",

author = "Carla Schmidt and Hazel Marriott and Min Zhou and Nina Morgner and Argyris Politis and Carol Robinson",

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T1 - Comparative crosslinking and mass spectrometry of an intact F-type ATPase suggest a role for phosphorylation in regulating subunit interactions and nucleotide occupancy

AU - Schmidt, Carla

AU - Marriott, Hazel

AU - Zhou, Min

AU - Morgner, Nina

AU - Politis, Argyris

AU - Robinson, Carol

PY - 2013/6/12

Y1 - 2013/6/12

UR - https://www.scopus.com/pages/publications/84879967659

U2 - 10.1038/ncomms2985

DO - 10.1038/ncomms2985

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SN - 2041-1723

VL - 1985

JO - Nature Communications

JF - Nature Communications

ER -

Comparative crosslinking and mass spectrometry of an intact F-type ATPase suggest a role for phosphorylation in regulating subunit interactions and nucleotide occupancy

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