scholarly article | Q13442814 |
P2093 | author name string | Attila Reményi | |
Anita Alexa | |||
Gergő Gógl | |||
Gábor Glatz | |||
P2860 | cites work | Evolutionary history of the vertebrate mitogen activated protein kinases family | Q21134977 |
ERK5 is targeted to myocyte enhancer factor 2A (MEF2A) through a MAPK docking motif | Q24292700 | ||
Components of a new human protein kinase signal transduction pathway | Q24319086 | ||
BMK1/ERK5 regulates serum-induced early gene expression through transcription factor MEF2C | Q24532869 | ||
Erk5 null mice display multiple extraembryonic vascular and embryonic cardiovascular defects | Q24534817 | ||
Specificity of linear motifs that bind to a common mitogen-activated protein kinase docking groove | Q24610682 | ||
Scaffolds: interaction platforms for cellular signalling circuits. | Q34774526 | ||
Solution NMR insights into docking interactions involving inactive ERK2 | Q35012791 | ||
Recruitment interactions can override catalytic interactions in determining the functional identity of a protein kinase | Q35049203 | ||
ERK5 activation of MEF2-mediated gene expression plays a critical role in BDNF-promoted survival of developing but not mature cortical neurons | Q35168574 | ||
Multiple docking sites on substrate proteins form a modular system that mediates recognition by ERK MAP kinase | Q35186927 | ||
Regulation of cellular functions by the ERK5 signalling pathway | Q36352695 | ||
Domains, motifs, and scaffolds: the role of modular interactions in the evolution and wiring of cell signaling circuits. | Q36498348 | ||
MAPK signalling: ERK5 versus ERK1/2. | Q36553050 | ||
Cell signaling and function organized by PB1 domain interactions. | Q36584065 | ||
Docking of PRAK/MK5 to the atypical MAPKs ERK3 and ERK4 defines a novel MAPK interaction motif | Q37339291 | ||
Targeted deletion of BMK1/ERK5 in adult mice perturbs vascular integrity and leads to endothelial failure. | Q37370471 | ||
The beta-arrestin-2 scaffold protein promotes c-Jun N-terminal kinase-3 activation by binding to its nonconserved N terminus. | Q40446331 | ||
The unique C-terminal tail of the mitogen-activated protein kinase ERK5 regulates its activation and nuclear shuttling. | Q40490843 | ||
PB1 domain-dependent signaling complex is required for extracellular signal-regulated kinase 5 activation | Q41766614 | ||
Two adjacent docking sites in the yeast Hog1 mitogen-activated protein (MAP) kinase differentially interact with the Pbs2 MAP kinase kinase and the Ptp2 protein tyrosine phosphatase | Q41772137 | ||
Noncanonical function of MEKK2 and MEK5 PB1 domains for coordinated extracellular signal-regulated kinase 5 and c-Jun N-terminal kinase signaling | Q41775036 | ||
Regulation of nuclear translocation of extracellular signal-regulated kinase 5 by active nuclear import and export mechanisms. | Q42006830 | ||
The MAP kinase ERK5 binds to and phosphorylates p90 RSK. | Q50335553 | ||
Docking interactions induce exposure of activation loop in the MAP kinase ERK2 | Q83964224 | ||
MolProbity: all-atom structure validation for macromolecular crystallography | Q24649111 | ||
Selectivity of docking sites in MAPK kinases | Q24651580 | ||
PHENIX: a comprehensive Python-based system for macromolecular structure solution | Q24654617 | ||
MEK5/ERK5 pathway: the first fifteen years | Q26866383 | ||
Crystal structures of MAP kinase p38 complexed to the docking sites on its nuclear substrate MEF2A and activator MKK3b | Q27639263 | ||
Insight into the binding properties of MEKK3 PB1 to MEK5 PB1 from its solution structure | Q27648968 | ||
Phosphorylation of DCC by ERK2 is facilitated by direct docking of the receptor P1 domain to the kinase | Q27665837 | ||
Protein–peptide complex crystallization: a case study on the ERK2 mitogen-activated protein kinase | Q27676946 | ||
Atomic structure of the MAP kinase ERK2 at 2.3 A resolution | Q27730946 | ||
XDS | Q27860472 | ||
Overview of the CCP4 suite and current developments | Q27860782 | ||
Phasercrystallographic software | Q27860930 | ||
Features and development of Coot | Q27861079 | ||
The Ste5 scaffold allosterically modulates signaling output of the yeast mating pathway. | Q27935451 | ||
Optimization of specificity in a cellular protein interaction network by negative selection | Q27940190 | ||
ERK5 and ERK2 cooperate to regulate NF-kappaB and cell transformation | Q28140491 | ||
PB1 domains of MEKK2 and MEKK3 interact with the MEK5 PB1 domain for activation of the ERK5 pathway | Q28200957 | ||
MEF2: a central regulator of diverse developmental programs | Q28254625 | ||
Atypical mitogen-activated protein kinases: structure, regulation and functions | Q28278354 | ||
Bmk1/Erk5 is required for cell proliferation induced by epidermal growth factor | Q28286729 | ||
Differential regulation and properties of MAPKs | Q28301932 | ||
Transcription factor ATF2 regulation by the JNK signal transduction pathway | Q28305631 | ||
ERK5 MAPK regulates embryonic angiogenesis and acts as a hypoxia-sensitive repressor of vascular endothelial growth factor expression | Q28591302 | ||
A conserved docking motif in MAP kinases common to substrates, activators and regulators | Q29619999 | ||
Spatial exclusivity combined with positive and negative selection of phosphorylation motifs is the basis for context-dependent mitotic signaling | Q30414432 | ||
Differential regulation of mitogen-activated protein kinases ERK1/2 and ERK5 by neurotrophins, neuronal activity, and cAMP in neurons. | Q31840769 | ||
Systematic analysis of human kinase genes: a large number of genes and alternative splicing events result in functional and structural diversity | Q33229366 | ||
The evolution of the MAP kinase pathways: coduplication of interacting proteins leads to new signaling cascades | Q33879366 | ||
Docking domains and substrate-specificity determination for MAP kinases | Q34023280 | ||
Neurotrophins use the Erk5 pathway to mediate a retrograde survival response. | Q34090264 | ||
The role of docking interactions in mediating signaling input, output, and discrimination in the yeast MAPK network | Q34477973 | ||
Structural basis of docking interactions between ERK2 and MAP kinase phosphatase 3. | Q34600125 | ||
Extracellular signal-regulated kinase (ERK) 5 is necessary and sufficient to specify cortical neuronal fate | Q34687169 | ||
P433 | issue | 12 | |
P407 | language of work or name | English | Q1860 |
P921 | main subject | cell biology | Q7141 |
P304 | page(s) | 8596-609 | |
P577 | publication date | 2013-03-22 | |
P1433 | published in | Journal of Biological Chemistry | Q867727 |
P1476 | title | Structural mechanism for the specific assembly and activation of the extracellular signal regulated kinase 5 (ERK5) module | |
P478 | volume | 288 |
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