The combination of hydrogen/deuterium exchange or chemical cross-linking techniques with mass spectrometry: mapping of human 14-3-3ζ homodimer interface.
about
The crystal structure of Giardia duodenalis 14-3-3 in the apo form: when protein post-translational modifications make the differenceThe application of an emerging technique for protein-protein interaction interface mapping: the combination of photo-initiated cross-linking protein nanoprobes with mass spectrometry.Chemical cross-linking/mass spectrometry targeting acidic residues in proteins and protein complexesApplications of hydrogen/deuterium exchange MS from 2012 to 2014.Probing structures of large protein complexes using zero-length cross-linking.Oligomeric structure of 14-3-3 protein: what do we know about monomers?Conformational effects in protein electrospray-ionization mass spectrometry.Role of salt bridges in the dimer interface of 14-3-3ζ in dimer dynamics, N-terminal α-helical order, and molecular chaperone activity.
P2860
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P2860
The combination of hydrogen/deuterium exchange or chemical cross-linking techniques with mass spectrometry: mapping of human 14-3-3ζ homodimer interface.
description
2012 nî lūn-bûn
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2012年の論文
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2012年学术文章
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2012年学术文章
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name
The combination of hydrogen/de ...... n 14-3-3ζ homodimer interface.
@en
The combination of hydrogen/de ...... n 14-3-3ζ homodimer interface.
@nl
type
label
The combination of hydrogen/de ...... n 14-3-3ζ homodimer interface.
@en
The combination of hydrogen/de ...... n 14-3-3ζ homodimer interface.
@nl
prefLabel
The combination of hydrogen/de ...... n 14-3-3ζ homodimer interface.
@en
The combination of hydrogen/de ...... n 14-3-3ζ homodimer interface.
@nl
P2093
P50
P1476
The combination of hydrogen/de ...... n 14-3-3ζ homodimer interface.
@en
P2093
Hynek Mrázek
Kateřina Haladová
Petr Halada
Petr Novák
Tomáš Ječmen
Tomáš Obšil
P356
10.1016/J.JSB.2012.04.016
P577
2012-05-02T00:00:00Z