(Q51838104)

English

Top-down structural analysis of posttranslationally modified proteins by Fourier transform ion cyclotron resonance-MS with hydrogen/deuterium exchange and electron capture dissociation.

scientific article published on 15 February 2013

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

13 April 2018

http://europepmc.org/abstract/MED/23319428

Top-down structural analysis of posttranslationally modified proteins by Fourier transform ion cyclotron resonance-MS with hydrogen/deuterium exchange and electron capture dissociation. (English)

1 reference

Europe PubMed Central

PubMed publication ID

13 April 2018

http://europepmc.org/abstract/MED/23319428

author name string

Jingxi Pan

1

1 reference

Europe PubMed Central

PubMed publication ID

13 April 2018

http://europepmc.org/abstract/MED/23319428

Christoph H Borchers

2

1 reference

Europe PubMed Central

PubMed publication ID

13 April 2018

http://europepmc.org/abstract/MED/23319428

publication date

15 February 2013

1 reference

Europe PubMed Central

PubMed publication ID

13 April 2018

http://europepmc.org/abstract/MED/23319428

1 reference

Europe PubMed Central

PubMed publication ID

13 April 2018

http://europepmc.org/abstract/MED/23319428

13

1 reference

Europe PubMed Central

PubMed publication ID

13 April 2018

http://europepmc.org/abstract/MED/23319428

6

1 reference

Europe PubMed Central

PubMed publication ID

13 April 2018

http://europepmc.org/abstract/MED/23319428

974-981

1 reference

Europe PubMed Central

PubMed publication ID

13 April 2018

http://europepmc.org/abstract/MED/23319428

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Electron transfer dissociation facilitates the measurement of deuterium incorporation into selectively labeled peptides with single residue resolution

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Protein conformations can be probed in top-down HDX MS experiments utilizing electron transfer dissociation of protein ions without hydrogen scrambling.

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Tertiary structural rearrangements upon oxidation of Methionine145 in calmodulin promotes targeted proteasomal degradation

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An altered mode of calcium coordination in methionine-oxidized calmodulin

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Structural uncoupling between opposing domains of oxidized calmodulin underlies the enhanced binding affinity and inhibition of the plasma membrane Ca-ATPase

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Oxidation of Met144 and Met145 in calmodulin blocks calmodulin dependent activation of the plasma membrane Ca-ATPase

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Electron Capture Dissociation of Multiply Charged Protein Cations. A Nonergodic Process

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Semi-automated data processing of hydrogen exchange mass spectra using HX-Express

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Cation binding mode of fully oxidised calmodulin explained by the unfolding of the apostate.

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Electron capture dissociation proceeds with a low degree of intramolecular migration of peptide amide hydrogens

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Solution structure of calcium-free calmodulin

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Post-translational modifications differentially affect IgG1 conformation and receptor binding.

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Site-specific methionine oxidation in calmodulin affects structural integrity and interaction with Ca2+/calmodulin-dependent protein kinase II

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Identifiers

10.1002/PMIC.201200246

1 reference

Europe PubMed Central

PubMed publication ID

13 April 2018

http://europepmc.org/abstract/MED/23319428

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

13 April 2018

http://europepmc.org/abstract/MED/23319428

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