Ultrasensitivity in the mitogen-activated protein kinase cascade - Wikidata - awgldk - TriplyDB

Ultrasensitivity in the mitogen-activated protein kinase cascade

Ultrasensitivity in the mitogen-activated protein kinase cascade

http://www.wikidata.org/entity/Q24597665

about

Condor-COPASI: high-throughput computing for biochemical networks Robust network topologies for generating switch-like cellular responses Raf family kinases: old dogs have learned new tricks Computational modelling of the receptor-tyrosine-kinase-activated MAPK pathway The Bacillus subtilis sin operon: an evolvable network motif Biphasic activation of Aurora-A kinase during the meiosis I- meiosis II transition in Xenopus oocytes Robust spindle alignment in Drosophila neuroblasts by ultrasensitive activation of pins Open cascades as simple solutions to providing ultrasensitivity and adaptation in cellular signaling MAPK signaling in equations and embryos An ultrasensitive sorting mechanism for EGF receptor endocytosis Galphai generates multiple Pins activation states to link cortical polarity and spindle orientation in Drosophila neuroblasts Signaling switches and bistability arising from multisite phosphorylation in protein kinase cascades A calculus of purpose Systems biology approaches in cell signaling research Development of ERK Activity Sensor, an in vitro, FRET-based sensor of Extracellular Regulated Kinase activity.Modeling T cell antigen discrimination based on feedback control of digital ERK responses PI3K-AKT-mTOR-signaling and beyond: the complex network in gastroenteropancreatic neuroendocrine neoplasms Molecular signaling network motifs provide a mechanistic basis for cellular threshold responses Ultrasensitivity part III: cascades, bistable switches, and oscillators Novel Reporter for Faithful Monitoring of ERK2 Dynamics in Living Cells and Model Organisms.An Ultrasensitive Mechanism Regulates Influenza Virus-Induced Inflammation Quantitative and logic modelling of molecular and gene networks Abiotic stress signal transduction in plants: Molecular and genetic perspectives Mixed lineage kinase-dependent JNK activation is governed by interactions of scaffold protein JIP with MAPK module components.In vivo robustness analysis of cell division cycle genes in Saccharomyces cerevisiae Funneled landscape leads to robustness of cell networks: yeast cell cycle Dose response relationship in anti-stress gene regulatory networks Membrane recruitment of scaffold proteins drives specific signaling Optimal signal processing in small stochastic biochemical networks Operating regimes of signaling cycles: statics, dynamics, and noise filtering A hidden feedback in signaling cascades is revealed The signaling petri net-based simulator: a non-parametric strategy for characterizing the dynamics of cell-specific signaling networks Large-scale analysis of network bistability for human cancers Training signaling pathway maps to biochemical data with constrained fuzzy logic: quantitative analysis of liver cell responses to inflammatory stimuli Computational investigation of the changing patterns of subtype specific NMDA receptor activation during physiological glutamatergic neurotransmission Retroactive signaling in short signaling pathways Noise propagation in two-step series MAPK cascade Modeling of tumor progression in NSCLC and intrinsic resistance to TKI in loss of PTEN expression A characterization of scale invariant responses in enzymatic networks Characterizing the relationship between steady state and response using analytical expressions for the steady states of mass action models

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P2860

Ultrasensitivity in the mitogen-activated protein kinase cascade

http://www.wikidata.org/entity/Q24597665

description

1996 nî lūn-bûn

@nan

1996 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

1996 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

1996年の論文

@ja

1996年論文

@yue

1996年論文

@zh-hant

1996年論文

@zh-hk

1996年論文

@zh-mo

1996年論文

@zh-tw

1996年论文

@wuu

name

Ultrasensitivity in the mitogen-activated protein kinase cascade

@ast

Ultrasensitivity in the mitogen-activated protein kinase cascade

@en

Ultrasensitivity in the mitogen-activated protein kinase cascade

@nl

type

label

Ultrasensitivity in the mitogen-activated protein kinase cascade

@ast

Ultrasensitivity in the mitogen-activated protein kinase cascade

@en

Ultrasensitivity in the mitogen-activated protein kinase cascade

@nl

prefLabel

Ultrasensitivity in the mitogen-activated protein kinase cascade

@ast

Ultrasensitivity in the mitogen-activated protein kinase cascade

@en

Ultrasensitivity in the mitogen-activated protein kinase cascade

@nl

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Ultrasensitivity in the mitogen-activated protein kinase cascade

@en

P2093

C Y Huang

http://www.w3.org/2001/XMLSchema#string

J E Ferrell

http://www.w3.org/2001/XMLSchema#string

P2860

Identification of the sites in MAP kinase kinase-1 phosphorylated by p74raf-1

An amplified sensitivity arising from covalent modification in biological systems

Signaling in the yeast pheromone response pathway: specific and high-affinity interaction of the mitogen-activated protein (MAP) kinases Kss1 and Fus3 with the upstream MAP kinase kinase Ste7.

How MAP kinases are regulated

Comparison of experimental binding data and theoretical models in proteins containing subunits

Identification of the regulatory phosphorylation sites in pp42/mitogen-activated protein kinase (MAP kinase).

Requirement for integration of signals from two distinct phosphorylation pathways for activation of MAP kinase.

Xenopus MAP kinase activator: identification and function as a key intermediate in the phosphorylation cascade

Ultrasensitivity in biochemical systems controlled by covalent modification. Interplay between zero-order and multistep effects.

The c-mos proto-oncogene protein kinase turns on and maintains the activity of MAP kinase, but not MPF, in cell-free extracts of Xenopus oocytes and eggs

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10078-83

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scholarly article

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942986

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10.1073/PNAS.93.19.10078

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19

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