Pages that link to "Q33632317"
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The following pages link to Protein modification: docking sites for kinases (Q33632317):
Displayed 50 items.
- Phosphoproteomic Analysis of the Mouse Brain Cytosol Reveals a Predominance of Protein Phosphorylation in Regions of Intrinsic Sequence Disorder (Q22061729) (← links)
- ERK5 is targeted to myocyte enhancer factor 2A (MEF2A) through a MAPK docking motif (Q24292700) (← links)
- Bidirectional signals transduced by DAPK-ERK interaction promote the apoptotic effect of DAPK (Q24336428) (← links)
- Identification of a docking groove on ERK and p38 MAP kinases that regulates the specificity of docking interactions (Q24536356) (← links)
- Nuclear entry of the circadian regulator mPER1 is controlled by mammalian casein kinase I epsilon (Q24553133) (← links)
- Identification of a pocket in the PDK1 kinase domain that interacts with PIF and the C-terminal residues of PKA (Q24600810) (← links)
- Crystal structures of MAP kinase p38 complexed to the docking sites on its nuclear substrate MEF2A and activator MKK3b (Q27639263) (← links)
- A 3-phosphoinositide-dependent protein kinase-1 (PDK1) docking site is required for the phosphorylation of protein kinase Czeta (PKCzeta ) and PKC-related kinase 2 by PDK1 (Q28141738) (← links)
- Hydrophobic as well as charged residues in both MEK1 and ERK2 are important for their proper docking (Q28188989) (← links)
- The AP-1 repressor, JDP2, is a bona fide substrate for the c-Jun N-terminal kinase (Q28198705) (← links)
- Identification of novel point mutations in ERK2 that selectively disrupt binding to MEK1 (Q28217158) (← links)
- A conserved docking site in MEKs mediates high-affinity binding to MAP kinases and cooperates with a scaffold protein to enhance signal transmission (Q28345384) (← links)
- The PIF-binding pocket in PDK1 is essential for activation of S6K and SGK, but not PKB. (Q28345841) (← links)
- Computational prediction and experimental verification of new MAP kinase docking sites and substrates including Gli transcription factors (Q28475319) (← links)
- The N-terminal ERK-binding site of MEK1 is required for efficient feedback phosphorylation by ERK2 in vitro and ERK activation in vivo (Q28609067) (← links)
- Docking interactions in the mitogen-activated protein kinase cascades (Q28679130) (← links)
- Signaling--2000 and beyond (Q29617413) (← links)
- Mechanisms of specificity in protein phosphorylation (Q29617541) (← links)
- A conserved docking motif in MAP kinases common to substrates, activators and regulators (Q29619999) (← links)
- Reengineering the signaling properties of a Src family kinase (Q30157090) (← links)
- Glyceraldehyde-3-Phosphate Dehydrogenase (GAPDH) Protein-Protein Interaction Inhibitor Reveals a Non-catalytic Role for GAPDH Oligomerization in Cell Death (Q30387486) (← links)
- PPSP: prediction of PK-specific phosphorylation site with Bayesian decision theory (Q33237091) (← links)
- GPS 2.0, a tool to predict kinase-specific phosphorylation sites in hierarchy (Q33332411) (← links)
- Substrate and docking interactions in serine/threonine protein kinases (Q33576177) (← links)
- Inhibition of p38 MAP kinase as a therapeutic strategy (Q33957191) (← links)
- Docking domains and substrate-specificity determination for MAP kinases (Q34023280) (← links)
- Docking sites on mitogen-activated protein kinase (MAPK) kinases, MAPK phosphatases and the Elk-1 transcription factor compete for MAPK binding and are crucial for enzymic activity (Q34170648) (← links)
- ERK-dependent phosphorylation of the transcription initiation factor TIF-IA is required for RNA polymerase I transcription and cell growth. (Q34181707) (← links)
- The protein kinase activity modulation sites: mechanisms for cellular regulation - targets for therapeutic intervention (Q34268736) (← links)
- Specificity in signal transduction: from phosphotyrosine-SH2 domain interactions to complex cellular systems (Q34292599) (← links)
- Structural basis for the selective inhibition of JNK1 by the scaffolding protein JIP1 and SP600125. (Q34348280) (← links)
- p38 MAP kinase: molecular target for the inhibition of pro-inflammatory cytokines. (Q34483284) (← links)
- Understanding the specificity of a docking interaction between JNK1 and the scaffolding protein JIP1. (Q34588321) (← links)
- Structural basis of docking interactions between ERK2 and MAP kinase phosphatase 3. (Q34600125) (← links)
- An ERK2 docking site in the Pointed domain distinguishes a subset of ETS transcription factors (Q35004774) (← links)
- Recruitment interactions can override catalytic interactions in determining the functional identity of a protein kinase (Q35049203) (← links)
- Molecular recognitions in the MAP kinase cascades (Q35086083) (← links)
- Ternary complex factors: prime nuclear targets for mitogen-activated protein kinases (Q35131700) (← links)
- CKI isoforms α and ε regulate Star-PAP target messages by controlling Star-PAP poly(A) polymerase activity and phosphoinositide stimulation (Q35259346) (← links)
- Arabidopsis kinome: after the casting. (Q35636774) (← links)
- Targeting diverse signaling interaction sites allows the rapid generation of bivalent kinase inhibitors (Q35836458) (← links)
- The many paths to p38 mitogen-activated protein kinase activation in the immune system (Q36518938) (← links)
- The mitogen-activated protein (MAP) kinase ERK induces tRNA synthesis by phosphorylating TFIIIB. (Q39756106) (← links)
- A TNF- and c-Cbl-dependent FLIP(S)-degradation pathway and its function in Mycobacterium tuberculosis-induced macrophage apoptosis (Q39825680) (← links)
- In vivo role of the PIF-binding docking site of PDK1 defined by knock-in mutation (Q39831998) (← links)
- Determinants that control the specific interactions between TAB1 and p38alpha (Q40285664) (← links)
- Molecular determinants that mediate selective activation of p38 MAP kinase isoforms (Q40387373) (← links)
- Extracellular signal-regulated kinases 1/2 are serum-stimulated "Bim(EL) kinases" that bind to the BH3-only protein Bim(EL) causing its phosphorylation and turnover (Q40606380) (← links)
- Differential phosphorylation of c-Jun and JunD in response to the epidermal growth factor is determined by the structure of MAPK targeting sequences (Q40607333) (← links)
- Specificity determinants in MAPK signaling to transcription factors (Q40757743) (← links)