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Analysis of cross-link on Tranaldolase

ABSTRACT: analysis of cross link on tranaldolase using mass spectrometry

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Neisseria Gonorrhoeae

SUBMITTER: Pan Fang

LAB HEAD: henning urlaub

PROVIDER: PXD020302 | Pride | 2021-05-26

REPOSITORIES: pride

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Dataset's files

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			Action	DRS
	C38S_1mMDTT_1.raw	Raw
	C38S_1mMDTT_2.raw	Raw
	C38S_5mMDTT_1.raw	Raw
	C38S_5mMDTT_2.raw	Raw
	C38S_nativ_1.raw	Raw

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1 - 5 of 19

Publications

A lysine-cysteine redox switch with an NOS bridge regulates enzyme function.

Wensien Marie M von Pappenheim Fabian Rabe FR Funk Lisa-Marie LM Kloskowski Patrick P Curth Ute U Diederichsen Ulf U Uranga Jon J Ye Jin J Fang Pan P Pan Kuan-Ting KT Urlaub Henning H Mata Ricardo A RA Sautner Viktor V Tittmann Kai K

Nature 20210505 7859

Disulfide bonds between cysteine residues are important post-translational modifications in proteins that have critical roles for protein structure and stability, as redox-active catalytic groups in enzymes or allosteric redox switches that govern protein function<sup>1-4</sup>. In addition to forming disulfide bridges, cysteine residues are susceptible to oxidation by reactive oxygen species, and are thus central not only to the scavenging of these but also to cellular signalling and communicat ...[more]

PMID: 33953398

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