Docking Motif Interactions in MAP Kinases Revealed by Hydrogen Exchange Mass Spectrometry-Reference-Cited by-同舟云学术

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Docking Motif Interactions in MAP Kinases Revealed by Hydrogen Exchange Mass Spectrometry

Published:2004-04 Issue:1 Volume:14 Page:43-55
ISSN:1097-2765
Container-title:Molecular Cell
language:en
Short-container-title:Molecular Cell

Author:

Lee Thomas,Hoofnagle Andrew N,Kabuyama Yukihito,Stroud James,Min Xiaoshan,Goldsmith Elizabeth J,Chen Lin,Resing Katheryn A,Ahn Natalie G

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology

Reference34 articles.

1. Two co-existing mechanisms for nuclear import of MAP kinase;Adachi;EMBO J.,1999

2. A conserved motif at the amino termini of MEK5 might mediate high affinity interaction with the cognate MAPKs;Bardwell;Trends Biochem. Sci.,1996

3. Specificity determinants in MAPK signaling to transcription factors;Barsyte-Lovejoy;J. Biol. Chem.,2002

4. The structure of phosphorylated p38gamma is monomeric and reveals a conserved activation-loop conformation;Bellon;Structure Fold. Des.,1999

5. Crystallography & NMR system;Brunger;Acta Crystallogr. D Biol. Crystallogr.,1998

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