Cited by 1,600Protein Kinase Regulation and GTPase SignalingMelanoma and MAPK PathwaysProtein Tyrosine Phosphatases

The DOI matches its Crossref record; 144 of the 144 references it cites were found in a registry or an index.

Mitogen-Activated Protein Kinases: Specific Messages from Ubiquitous Messengers

Open access

Schaeffer, Hans J., Weber, Michael J.·1999·Molecular and Cellular Biology

Open this paper in CoChat — free account

Abstract

Signal transduction networks allow cells to perceive changes in the extracellular environment and to mount an appropriate response. Mitogen-activated protein kinase (MAPK) cascades are among the most thoroughly studied of signal transduction systems and have been shown to participate in a diverse array of cellular programs, including cell differentiation, cell movement, cell division, and cell death. A key question in studies of this cascade is, how does a ubiquitously activated regulatory enzume generate a specific and biologically appropriate cellular response? In this review we describe recent findings that provide insight into ways that the regulation, structure, and localization of MAPKs and the participation of adapters and scaffolds can help determine biological outcomes. MAPK cascades are evolutionarily conserved in all eucaryotes and play a key role in the regulation of gene expression as well as cytoplasmic activities. They typically are organized in a three-kinase architecture consisting of a MAPK, a MAPK activator (MEK, MKK, or MAPK kinase), and a MEK activator (MEK kinase [MEKK] or MAPK kinase kinase). Transmission of signals is achieved by sequential phosphorylation and activation of the components specific to a respective cascade. In the yeast Saccharomyces cerevisiae, five MAPK modules have been described; they regulate mating, filamentation, high-osmolarity responses, cell wall remodeling, and sporulation (Fig. (Fig.1A)1A) (reviewed in references 56 and 77). In mammalian systems five distinguishable MAPK modules have been identified so far (Fig. (Fig.1B).1B). These include the extracellular signal-regulated kinase 1 and 2 (ERK1/2) cascade, which preferentially regulates cell growth and differentiation, as well as the c-Jun N-terminal kinase (JNK) and p38 MAPK cascades, which function mainly in stress responses like inflammation and apoptosis (reviewed in references 57, 74, and 103). Moreover, MAPK pathways control several developmental programs, such as morphogenesis and spatial patterning in Dictyostelium amoebae (17, 45), eye development in Drosophila melanogaster (124), vulva induction in Caenorhabditis elegans (113), and T-cell development in mammals (31). FIG. 1 Schematic overview of MAPK modules. (A) In S. cerevisiae, five MAPK modules regulate mating, filamentation, high-osmolarity responses, cell wall remodeling, and sporulation. (B) Mammalian MAPK modules regulate cell growth, differentiation, stress responses, ... Individual MAPK modules generally can signal independently from each other, and this specificity is manifested in distinct physiologic responses. This is most obvious when studying MAPK signaling in S. cerevisiae. Here a particular extracellular event characteristically activates a specific MAPK module and initiates a unique cellular program (reviewed in references 56 and 77). For example, stimulation of cells with pheromone leads to the activation of the pheromone response pathway (STE11, STE7, and FUS3) (Fig. (Fig.2),2), which ultimately results in cell cycle arrest and the induction of mating-specific genes. However, related MAPKs whose modules share some components with the pheromone response pathway are not affected by pheromone stimulation but are activated only in response to the appropriate stimulus. For example, under conditions of high osmolarity Ste11 can lead to activation of Hog1 but does not induce mating-specific genes. Conversely, conditions that activate the filamentation pathway (which utilizes STE11 and STE7) induce only genes that regulate filamentous growth without triggering pheromone responses or responses to high osmolarity. These observations suggest that yeast cells have developed efficient mechanisms to generate pathway specificity and to successfully suppress cross talk, even when individual components participate in more than one signaling pathway. FIG. 2 Scaffold and adapter molecules in MAPK pathways. MAPK scaffolds and adapters (gray shading) are thought to promote the formation of oligomeric protein complexes with components that function in a specific MAPK module. Scaffolds have been identified in ... In metazoan cells the problem is more complex because each cell is simultaneously exposed to multiple extracellular signals and must integrate these inputs to choose an appropriate response. Thus, the biological context of a signal plays a determinative role in the way that MAPK activation is interpreted. For example, although ERKs generally regulate cell growth and cell differentiation and JNKs participate in a stress response, this is not always the case and in certain cell types activation of JNKs can induce proliferation (110). This indicates that in mammalian systems physiologic responses associated with a certain MAPK module can be cell type specific. Moreover, in PC12 cells, transient stimulation of the ERK cascade leads to proliferation whereas sustained stimulation leads to differentiation,

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1128/mcb.19.4.2435

Cites

144 of 144 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Specificity of receptor tyrosine kinase signaling: Transient versus sustained extracellular signal-regulated kinase activation
Marshall, C. J. (1995) · Cell · doi:10.1016/0092-8674(95)90401-8 · Cited by 3,906
JNK1: A protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain
Dérijard, B., Hibi, M., Wu, I.-H., Barrett, T., Su, B., Deng, T., Karin, M., & Davis, R. J. (1994) · Cell · doi:10.1016/0092-8674(94)90380-8 · Cited by 3,188
Mitogen-activated protein kinase pathways
Robinson, M. J., & Cobb, M. H. (1997) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(97)80061-0 · Cited by 2,489
Signaling Through Scaffold, Anchoring, and Adaptor Proteins
Pawson, T., & Scott, J. D. (1997) · Science · doi:10.1126/science.278.5346.2075 · Cited by 2,256
Epac is a Rap1 guanine-nucleotide-exchange factor directly activated by cyclic AMP
de Rooij, J., Zwartkruis, F. J. T., Verheijen, M. H. G., Cool, R. H., Nijman, S. M. B., Wittinghofer, A., & Bos, J. L. (1998) · Nature · doi:10.1038/24884 · Cited by 1,970
Activation of the estrogen receptor through phosphorylation by mitogen-activated protein kinase
Kato, S., Endoh, H., Masuhiro, Y., Kitamoto, T., Uchiyama, S., Sasaki, H., Masushige, S., Gotoh, Y., Nishida, E., Kawashima, H., et al. (1995) · Science · doi:10.1126/science.270.5241.1491 · Cited by 1,964
Activation of MAP kinase kinase is necessary and sufficient for PC12 differentiation and for transformation of NIH 3T3 cells
Cowley, S. A. (1994) · Cell · doi:10.1016/0092-8674(94)90133-3 · Cited by 1,959
Mammalian Ras interacts directly with the serine/threonine kinase raf
Vojtek, A. B., Hollenberg, S. M., & Cooper, J. A. (1993) · Cell · doi:10.1016/0092-8674(93)90307-c · Cited by 1,934
Crystal Structure of the Catalytic Subunit of Cyclic Adenosine Monophosphate-Dependent Protein Kinase
Knighton, D. R., Zheng, J., Eyck, L. F. T., Ashford, V. A., Xuong, N., Taylor, S. S., & Sowadski, J. M. (1991) · Science · doi:10.1126/science.1862342 · Cited by 1,764
Signal Transduction through MAP Kinase Cascades
Lewis, T. S., Shapiro, P. S., & Ahn, N. G. (1998) · Advances in cancer research · doi:10.1016/s0065-230x(08)60765-4 · Cited by 1,759

Flagged first, then by citations

Show all 144 references

Research works printed but not linked: 4

10.1128/mcb.12.3.915-927.1992 · DOI
10.1128/mcb.14.12.8212-8218.1994 · DOI
10.1128/mcb.14.10.6683-6688.1994 · DOI
10.1128/mcb.14.3.1594-1602.1994 · DOI

Sorted by citations

Items 301–400 of 1,000

Cadmium Stress Responses in Brassica juncea : Hints from Proteomics and Metabolomics
D’Alessandro, A., Taamalli, M., Gevi, F., Timperio, A. M., Zolla, L., & Ghnaya, T. (2013) · Journal of Proteome Research · doi:10.1021/pr400793e · Cited by 108
“phosphorylation cascades are known to exert a central role in mediating Cd and heavy metal-stress signaling.(82,83)”
Background
Region-specific effects of acute and repeated restraint stress on the phosphorylation of mitogen-activated protein kinases
Meller, E., Shen, C., Nikolao, T. A., Jensen, C. H., Tsimberg, Y., Chen, J., & Gruen, R. J. (2003) · Brain Research · doi:10.1016/s0006-8993(03)02866-x · Cited by 105
Involvement of a proline-rich motif and RING-H2 finger of Deltex in the regulation of Notch signaling
Matsuno, K., Ito, M., Hori, K., Miyashita, F., Suzuki, S., Kishi, N., Artavanis‐Tsakonas, S., & Okano, H. (2002) · Development · doi:10.1242/dev.129.4.1049 · Cited by 105
Pharmacotherapeutic potential of phytochemicals: Implications in cancer chemoprevention and future perspectives
Kaur, V., Kumar, M., Kumar, A., Kaur, K., Dhillon, V. S., & Kaur, S. (2017) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2017.10.124 · Cited by 108
Mitogen-Activated Protein Kinase Cascade in Human Normal and Tumoral Parathyroid Cells
Corbetta, S., Lania, A. G., Filopanti, M., Vicentini, L., Ballarè, E., & Spada, A. (2002) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.87.5.2201 · Cited by 104
Retinoic acid‐induced neuritogenesis of human neuroblastoma SH‐SY5Y cells is ERK independent and PKC dependent
Miloso, M., Villa, D., Crimi, M., Galbiati, S., Donzelli, E., Nicolini, G., & Tredici, G. (2003) · Journal of Neuroscience Research · doi:10.1002/jnr.10848 · Cited by 104
Apoptosis in lung injury and remodeling
Li, X., Shu, R., Filippatos, G. S., & Uhal, B. D. (2004) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00519.2004 · Cited by 101
“Activation of JNK (2, 47, 60) leads to phosphorylation of its targets, c-Jun and activating transcription factor (ATF)-2 (44, 87), and activation of downstream gene expression when epithelial cells are exposed to oxidative stress, which is a very important contributor to pulmonary injury and fibrosis.”
Background
Differential Activation of p38 Mitogen-activated Protein Kinase Isoforms Depending on Signal Strength
Alonso, G., Ambrosino, C., Jones, M., & Nebreda, Á. R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m007835200 · Cited by 104
Effect of fluid flow-induced shear stress on human mesenchymal stem cells: Differential gene expression of IL1B and MAP3K8 in MAPK signaling
Glossop, J. R., & Cartmell, S. H. (2009) · Gene Expression Patterns · doi:10.1016/j.gep.2009.01.001 · Cited by 103
“The substrates of MAP3K8 are MAP kinase kinases belonging to each of the ERK1/2 (MEK1 and MEK2), JNK (MEK4 and MEK7) and p38 (MEK3 and MEK6) MAPK signaling pathways (Schaeffer and Weber, 1999; Roux and Blenis, 2004).”
The Mitogen-Activated Protein Kinase Gene MAF1 Is Essential for the Early Differentiation Phase of Appressorium Formation in Colletotrichum lagenarium
Kojima, K., Kikuchi, T., Takano, Y., Oshiro, E., & Okuno, T. (2002) · Molecular Plant-Microbe Interactions · doi:10.1094/mpmi.2002.15.12.1268 · Cited by 103
The autoimmune suppressor Gadd45α inhibits the T cell alternative p38 activation pathway
Salvador, J. M., Mittelstadt, P. R., Belova, G. I., Fornace, A. J., & Ashwell, J. D. (2005) · Nature Immunology · doi:10.1038/ni1176 · Cited by 100
The evolutionarily conserved MAPK/Erk signaling promotes ancestral T-cell immunity in fish via c-Myc–mediated glycolysis
Wei, X., Zhang, Y., Cheng, L., Ai, K., Li, K., Li, H., & Yang, J. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.012231 · Cited by 97
“3 extracellular signal-regulated kinase 1/2 (Erk1/2), P38, and c-Jun N-terminal kinase (JNK), have been identified in mammalian cells (19-21).”
Background
Molecular mechanisms of nitrogen dioxide induced epithelial injury in the lung.
Persinger, R. L., Poynter, M. E., Ckless, K., & Janssen-Heininger, Y. M. W. (2002) · PubMed · Cited by 99
Targeted therapy in T-cell malignancies: dysregulation of the cellular signaling pathways
Zhao, W.-L. (2009) · Leukemia · doi:10.1038/leu.2009.223 · Cited by 100
Thrombopoietin-Mediated Sustained Activation of Extracellular Signal-Regulated Kinase in UT7-Mpl Cells Requires Both Ras–Raf-1- and Rap1–B-Raf-Dependent Pathways
Garcia, J., de Gunzburg, J., Eychène, A., Gisselbrecht, S., & Porteu, F. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.8.2659-2670.2001 · Cited by 99
Recent Insights into the Contribution of the Changing Hypertrophic Chondrocyte Phenotype in the Development and Progression of Osteoarthritis
Ripmeester, E. G., Timur, U. T., Caron, M. M. J., & Welting, T. J. M. (2018) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2018.00018 · Cited by 98
“AKT1 RAC-alphaserine/threonine-protein kinase Sherwood et al. (2015) and Bianchi et al. (2016)”
BackgroundInfluential
Role of Dynamin, Src, and Ras in the Protein Kinase C-mediated Activation of ERK by Gonadotropin-releasing Hormone
Benard, O., Naor, Z., & Seger, R. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m006995200 · Cited by 98
Retracted
Apoptosis in lung pathophysiology
Fine, A., Janssen-Heininger, Y. M. W., Soultanakis, R. P., Swisher, S. G., & Uhal, B. D. (2000) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.2000.279.3.l423 · Cited by 98
Stimulation of Endothelin B Receptors in Astrocytes Induces cAMP Response Element-Binding Protein Phosphorylation andc-fosExpression Via Multiple Mitogen-Activated Protein Kinase Signaling Pathways
Schinelli, S., Zanassi, P., Paolillo, M., Wang, H., Feliciello, A., & Gallo, V. (2001) · Journal of Neuroscience · doi:10.1523/jneurosci.21-22-08842.2001 · Cited by 98
Rule-based spatial modeling with diffusing, geometrically constrained molecules
Gruenert, G., Ibrahim, B., Lenser, T., Lohel, M., Hinze, T., & Dittrich, P. (2010) · BMC Bioinformatics · doi:10.1186/1471-2105-11-307 · Cited by 98
“Scaffold proteins bind other proteins and are thought to help isolating different signaling pathways but also to catalyze reactions by co-localizing their ligands (For reviews see [61,62]).”
Background
Expression and distribution of JNK/SAPK‐associated scaffold protein JSAP1 in developing and adult mouse brain
Miura, E., Fukaya, M., Sato, T., Sugihara, K., Asano, M., Yoshioka, K., & Watanabe, M. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03835.x · Cited by 97
The UV (Ribotoxic) Stress Response of Human Keratinocytes Involves the Unexpected Uncoupling of the Ras-Extracellular Signal-Regulated Kinase Signaling Cascade from the Activated Epidermal Growth Factor Receptor
Iordanov, M. S., Choi, R. J., Ryabinina, O. P., Dinh, T.-H., Bright, R. K., & Magun, B. E. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.15.5380-5394.2002 · Cited by 96
Proteomic response of Euglena gracilis to heavy metal exposure – Identification of key proteins involved in heavy metal tolerance and accumulation
Khatiwada, B., Hasan, M. T., Sun, A., Kamath, K. S., Mirzaei, M., Sunna, A., & Nevalainen, H. K. M. (2019) · Algal Research · doi:10.1016/j.algal.2019.101764 · Cited by 96
Reproduction without sex: conidiation in the filamentous fungus Trichoderma
Steyaert, J. M., Weld, R. J., Mendoza‐Mendoza, A., & Stewart, A. (2010) · Microbiology · doi:10.1099/mic.0.041715-0 · Cited by 96
“MAPK signalling cascades have been shown to regulate a variety of responses in the cell associated with growth, proliferation and virulence (Schaeffer & Weber, 1999; Xu, 2896 Microbiology 156 Downloaded from www.microbiologyresearch.org by IP: 54.70.40.11 On: Tue, 30 Oct 2018 18:31:33 2000).”
Influential
The role of protein kinase B and mitogen-activated protein kinase in epidermal growth factor and tumor necrosis factor α-mediated rat hepatocyte survival and apoptosis
Roberts, R. A., James, N. H., & Cosulich, S. C. (2000) · Hepatology · doi:10.1002/hep.510310223 · Cited by 96
Crystal structure of the p14/MP1 scaffolding complex: How a twin couple attaches mitogen-activated protein kinase signaling to late endosomes
Kurzbauer, R., Teis, D., de Araujo, M. E. G., Maurer-Stroh, S., Eisenhaber, F., Bourenkov, G. P., Bartunik, H. D., Hekman, M., Rapp, U. R., Huber, L. A., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0403435101 · Cited by 95
Molecular mechanisms of nitrogen dioxide induced epithelial injury in the lung
Persinger, R. L., Poynter, M. E., Ckless, K., & Janssen-Heininger, Y. M. W. (2002) · Molecular and Cellular Biochemistry · doi:10.1023/a:1015973530559 · Cited by 117
Activation of the p38 Mitogen-activated Protein Kinase Pathway by Estrogen or by 4-Hydroxytamoxifen Is Coupled to Estrogen Receptor-induced Apoptosis
Zhang, C. C., & Shapiro, D. J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.1.479 · Cited by 95
Substrate Recognition Domains within Extracellular Signal-regulated Kinase Mediate Binding and Catalytic Activation of Mitogen-activated Protein Kinase Phosphatase-3
Nichols, A. C., Camps, M., Gilliéron, C., Chabert, C., Brunet, A., Wilsbacher, J. L., Cobb, M. H., Pouysségur, J., Shaw, J. P., & Arkinstall, S. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001515200 · Cited by 95
Requirement of Mitogen-activated Protein Kinase Kinase 3 (MKK3) for Activation of p38α and p38δ MAPK Isoforms by TGF-β1 in Murine Mesangial Cells
Wang, L., Ma, R., Flavell, R. A., & Choi, M. E. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m208573200 · Cited by 95
The Biotrophic, Non-Appressorium-Forming Grass Pathogen Claviceps purpurea Needs a Fus3/Pmk1 Homologous Mitogen-Activated Protein Kinase for Colonization of Rye Ovarian Tissue
Mey, G., Oeser, B., Lebrun, M., & Tudzynski, P. (2002) · Molecular Plant-Microbe Interactions · doi:10.1094/mpmi.2002.15.4.303 · Cited by 94
Phosphorylation of MafA Is Essential for Its Transcriptional and Biological Properties
Benkhelifa‐Ziyyat, S., Provot, S., Nabais, E., Eychène, A., Calothy, G., & Felder‐Schmittbuhl, M. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.14.4441-4452.2001 · Cited by 94
MAPK3/1 participates in the activation of primordial follicles through mTORC1‐KITL signaling
Zhao, Y., Zhang, Y., Li, J., Zheng, N., Xu, X., Yang, J., Xia, G., & Zhang, M. (2017) · Journal of Cellular Physiology · doi:10.1002/jcp.25868 · Cited by 94
“Mitogen-activated protein kinase (MAPK) signaling pathways are expressed in several mammalian tissues and have been implicated as key regulators of cell proliferation and differentiation (Pearson et al., 2001; Schaeffer & Weber, 1999).”
Background
Development of small molecule extracellular signal-regulated kinases (ERKs) inhibitors for cancer therapy
Pan, X., Pei, J., Wang, A., Wen, S., Feng, L., Bu, F., Zhu, Y., Zhang, L., Wang, G., & Ouyang, L. (2022) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2021.12.022 · Cited by 95
Pancreatic Stellate Cell Activation by Ethanol and Acetaldehyde: Is it Mediated by the Mitogen-Activated Protein Kinase Signaling Pathway?
McCarroll, J. A., Phillips, P. A., Park, S. B., Doherty, E., Pirola, R. C., Wilson, J. S., & Apte, M. V. (2003) · Pancreas · doi:10.1097/00006676-200308000-00008 · Cited by 93
“Briefly, PSCs were lysed using the same methods as described earlier and equal amounts of protein (250 g) were mixed with an N-terminal c-Jun (1-89) fusion protein (a known substrate for JNK) bound to glutathione sepharose beads to immunoprecipitate JNK from the cell lysates.”
Method
MEK1 activation by PAK: A novel mechanism
Park, E. R., Eblen, S. T., & Catling, A. D. (2007) · Cellular Signalling · doi:10.1016/j.cellsig.2007.01.018 · Cited by 93
Microarray expression analysis and identification of serum biomarkers for Niemann–Pick disease, type C1
Cluzeau, C. V. M., Watkins‐Chow, D. E., Fu, R., Borate, B. R., Yanjanin, N. M., Dail, M. K., Davidson, C. D., Walkley, S. U., Ory, D. S., Wassif, C. A., et al. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds193 · Cited by 93
Actin reorganization and morphological changes in human neutrophils stimulated by TNF, GM-CSF, and G-CSF: the role of MAP kinases
Kutsuna, H., Suzuki, K., Kamata, N., Kato, T., Hato, F., Mizuno, K., Kobayashi, H., Ishii, M., & Kitagawa, S. (2004) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00131.2003 · Cited by 93
Hydrophobic as Well as Charged Residues in Both MEK1 and ERK2 Are Important for Their Proper Docking
Xu, B.-E., Stippec, S., Robinson, F. L., & Cobb, M. H. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102769200 · Cited by 91
Redox Control of Neural Function: Background, Mechanisms, and Significance
Maher, P. A. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.1941 · Cited by 92
In Vivo Genome-Wide Expression Study on Human Circulating B Cells Suggests a NovelESR1andMAPK3Network for Postmenopausal Osteoporosis
Xiao, P., Chen, Y., Jiang, H., Liu, Y.-Z., Pan, F., Yang, T., Tang, Z.-H., Larsen, J. A., Lappe, J. M., Recker, R. R., et al. (2008) · Journal of Bone and Mineral Research · doi:10.1359/jbmr.080105 · Cited by 92
“(61) As we discussed, a suppressed ERK/MAPK3 signaling pathway decreases activation of ESR1.”
BackgroundInfluential
Dissecting the puzzle of life: modularization of signal transduction networks
Sáez-Rodríguez, J., Kremling, A., & Gilles, E. D. (2004) · Computers & Chemical Engineering · doi:10.1016/j.compchemeng.2004.08.035 · Cited by 92
Leucine-rich repeat kinase 2 induces α-synuclein expression via the extracellular signal-regulated kinase pathway
Carballo‐Carbajal, I., Weber-Endreß, S., Rovelli, G., Chan, D., Wolozin, B. L., Klein, C. L., Patenge, N., Gasser, T., & Kahle, P. J. (2010) · Cellular Signalling · doi:10.1016/j.cellsig.2010.01.006 · Cited by 93
The unforeseen challenge: from genotype-to-phenotype in cell populations
Braun, E. (2015) · Reports on Progress in Physics · doi:10.1088/0034-4885/78/3/036602 · Cited by 94
“In yeast for example, combinations of the same genes participate in MAPK modules with diverse functionalities operated by specific stimuli—mating response to a pheromone, sporulation resulting from carbon and nitrogen starvation, osmolyte synthesis due to high osmolarity etc [100].”
Background
Multiple Activation Mechanisms of p38α Mitogen-activated Protein Kinase
Kang, Y. J., Seit‐Nebi, A. S., Davis, R. J., & Han, J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m606800200 · Cited by 91
Down-regulation of the c-Jun N-terminal kinase (JNK) phosphatase M3/6 and activation of JNK by hydrogen peroxide and pyrrolidine dithiocarbamate
Chen, Y., Shrivastava, A., & Tan, T. (2001) · Oncogene · doi:10.1038/sj.onc.1204105 · Cited by 91
Stress Pathway Activation Induces Phosphorylation of Retinoid X Receptor
Lee, H., Suh, Y., Robinson, M. J., Clifford, J. L., Hong, W. K., Woodgett, J. R., Cobb, M. H., Mangelsdorf, D. J., & Kurie, J. M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m005490200 · Cited by 91
The Viral Protein A238L Inhibits TNF-α Expression through a CBP/p300 Transcriptional Coactivators Pathway
Granja, A. G., Nogal, M. L., Hurtado, C., del Aguila, C., Carrascosa, Á. L., Salas, M. L., Fresno, M., & Revilla, Y. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.176.1.451 · Cited by 91
“ATF-2/Jun proteins become transcriptionally active upon phosphorylation by the p38 and JNK1, members of the MAPK family (36).”
Background
CGRP stimulation of iNOS and NO release from trigeminal ganglion glial cells involves mitogen‐activated protein kinase pathways
Vause, C. V., & Durham, P. L. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06154.x · Cited by 90
“…regulated groups of MAPKs are present in mammalian cells, extracellular signal-regulated kinase 1/2 (ERK1/2), c-Jun amino-terminal kinases (JNK1/2/3), p38 proteins (p38a/b/c/d), and ERK5 that are activated by specific MAPKs (Schaeffer and Weber 1999; Widmann et al. 1999; Chang and Karin 2001).”
Krüppel‐like factor 5 promotes mitosis by activating the cyclin B1/Cdc2 complex during oncogenic Ras‐mediated transformation
Nandan, M. O., Chanchevalap, S., Dalton, W. B., & Yang, V. W. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.07.053 · Cited by 90
“Oncogenic Ras isoforms cause the constitutive activation of a signaling cascade involving several proteins including Raf and the mitogen-activated protein kinase (MAPK) [17-19].”
Background
The small GTPase Rac and the p21‐activated kinase Cla4 in Claviceps purpurea: interaction and impact on polarity, development and pathogenicity
Rolke, Y., & Tudzynski, P. (2008) · Molecular Microbiology · doi:10.1111/j.1365-2958.2008.06159.x · Cited by 89
“In mammals, MAPK cross-talk is well documented (Schaeffer and Weber, 1999).”
Background
Calcium-Mediated Activation of c-Jun NH2-Terminal Kinase (JNK) and Apoptosis in Response to Cadmium in Murine Macrophages
Kim, J. (2004) · Toxicological Sciences · doi:10.1093/toxsci/kfh221 · Cited by 90
“These MAPKs are believed to be important biomolecules in cell differentiation, cell movement, cell division, and cell death induced by extracellular stimuli ( Schaeffer and Weber, 1999 ).”
Influential
Phenylethyl Isothiocyanate Induces Apoptotic Signaling via Suppressing Phosphatase Activity against c-Jun N-terminal Kinase
Chen, Y., Han, J., Kori, R., Kong, A.-N. T., & Tan, T. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202070200 · Cited by 90
Ras induces NBT-II epithelial cell scattering through the coordinate activities of Rac and MAPK pathways
Edme, N., Downward, J., Thiery, J. P., & Boyer, B. (2002) · Journal of Cell Science · doi:10.1242/jcs.115.12.2591 · Cited by 90
CD40-mediated signaling in monocytic cells: up-regulation of tumor necrosis factor receptor-associated factor mRNAs and activation of mitogen-activated protein kinase signaling pathways
Pearson, L. L., Castle, B. E., & Kehry, M. R. (2001) · International Immunology · doi:10.1093/intimm/13.3.273 · Cited by 89
Signaling pathways for stress responses and adaptation in Aspergillus species: stress biology in the post-genomic era
Hagiwara, D., Sakamoto, K., Abe, K., & Gomi, K. (2016) · Bioscience Biotechnology and Biochemistry · doi:10.1080/09168451.2016.1162085 · Cited by 89
Differential activation of ERKs to focal adhesions by PKC ε is required for PMA-induced adhesion and migration of human glioma cells
Besson, A., Davy, A., Robbins, S. M., & Yong, V. W. (2001) · Oncogene · doi:10.1038/sj.onc.1204899 · Cited by 88
Activated MAPK/ERK kinase (MEK-1) induces transdifferentiation of pigmented epithelium into neural retina
Galy, A., Néron, B., Planque, N., Saule, S., & Eychène, A. (2002) · Developmental Biology · doi:10.1006/dbio.2002.0736 · Cited by 87
Lysophosphatidic acid induces prostate cancer PC3 cell migration via activation of LPA1, p42 and p38α
Feng, H., Tan, M., Xu, X., Han, J., Miller, D. D., Tigyi, G., & Cui, M. (2007) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2007.04.010 · Cited by 87
“ERK, p38 and JNK are the three major groups of MAPK [28].”
Background
A rice (Oryza sativa L.) MAP kinase gene, OsMAPK44, is involved in response to abiotic stresses
Jeong, M., Lee, S.-K., Kim, B., Kwon, T.-R., Cho, W.-S., Park, Y.-T., Lee, J.-O., Kwon, H.-B., Byun, M.-O., & Park, S.-C. (2006) · Plant Cell Tissue and Organ Culture (PCTOC) · doi:10.1007/s11240-005-9064-0 · Cited by 87
“MAPKs are activated through phosphorylation of specific threonine (T) and tyrosine (Y) molecules by dual specificity MAPK kinase (MAPKK), which in turn is phosphorylated and activated by MAP kinase kinase kinase (MAPKKK) (Schaeffer and Weber, 1999; Widemann et al., 1999).”
Background
Pharmacological blockade of mGlu2/3 metabotropic glutamate receptors reduces cell proliferation in cultured human glioma cells
D’Onofrio, M., Arcella, A., Bruno, V., Ngomba, R. T., Battaglia, G., Lombari, V., Ragona, G., Calogero, A., & Nicoletti, F. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01633.x · Cited by 86
Extracellular signal-regulated kinase as an inducer of non-apoptotic neuronal death
Subramaniam, S., & Unsicker, K. (2006) · Neuroscience · doi:10.1016/j.neuroscience.2005.12.013 · Cited by 86
Effects of Stimulation of AMP-activated Protein Kinase on Insulin-like Growth Factor 1- and Epidermal Growth Factor-dependent Extracellular Signal-regulated Kinase Pathway
Kim, J., Yoon, M., Choi, S.-L., Kang, I., Kim, S. S., Kim, Y.-S., Choi, Y.-K., & Ha, J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m011579200 · Cited by 88
RSK2 mediates muscle cell differentiation through regulation of NFAT3
Cho, Y.-Y., Yao, K., Bode, A. M., Bergen, H. R., Madden, B. J., Oh, S.-M., Ermakova, S., Kang, B. S., Choi, H. S., Shim, J.-H., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m611322200 · Cited by 85
Acute ethanol exposure inhibits macrophage IL-6 production: role of p38 and ERK1/2 MAPK
Góral, J., Choudhry, M. A., & Kovacs, E. J. (2003) · Journal of Leukocyte Biology · doi:10.1189/jlb.0703350 · Cited by 85
“p38 preferentially responds to inflammation and stress factors [21, 22]; ERK1/2 is activated by growth and differentiation signals, including growth factors, cytokines, and viral infection [23–25].”
Background
Signal transduction pathways linking polyamines to apoptosis
Pignatti, C., Tantini, B., Stefanelli, C., & Flamigni, F. (2004) · Amino Acids · doi:10.1007/s00726-004-0115-3 · Cited by 85
“MAPK cascades have been shown to participate in a wide array of cellular functions, such as cell growth, cell differentiation and cell death (Schaeffer and Weber, 1999; Robinson and Cobb, 1997; Cross et al., 2000).”
Background
Glycogen Synthase Kinase 3β Is a Natural Activator of Mitogen-activated Protein Kinase/Extracellular Signal-regulated Kinase Kinase Kinase 1 (MEKK1)
Kim, J. W., Lee, J. E., Kim, M., Cho, E., Cho, S., & Choi, E. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300253200 · Cited by 85
RACK1 Targets the Extracellular Signal-Regulated Kinase/Mitogen-Activated Protein Kinase Pathway To Link Integrin Engagement with Focal Adhesion Disassembly and Cell Motility
Vomastek, T., Iwanicki, M., Schaeffer, H. J., Tarcsafalvi, A., Parsons, J. T., & Weber, M. J. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00598-07 · Cited by 85
“These nonenzymatic components associate with and enhance functional interaction of the components of the ERK pathway and can regulate the amplitude, timing, and location of signals (20, 24, 32).”
BackgroundSelf-citation
Respiratory Syncytial Virus Infection Results in Activation of Multiple Protein Kinase C Isoforms Leading to Activation of Mitogen-Activated Protein Kinase
Monick, M. M., Staber, J. M. R., Thomas, K. W., & Hunninghake, G. W. (2001) · The Journal of Immunology · doi:10.4049/jimmunol.166.4.2681 · Cited by 85
Advances in understanding the regulation of apoptosis and mitosis by peroxisome-proliferator activated receptors in pre-clinical models: relevance for human health and disease
Boitier, E., Gautier, J., & Roberts, R. A. (2003) · Comparative Hepatology · doi:10.1186/1476-5926-2-3 · Cited by 86
Regulation of G1 phase progression by growth factors and the extracellular matrix
Hulleman, E., & Boonstra, J. (2001) · Cellular and Molecular Life Sciences · doi:10.1007/pl00000780 · Cited by 85
Signal transduction by tumour necrosis factor and tumour necrosis factor related ligands and their receptors
Darnay, B. G., & Aggarwal, B. B. (1999) · Annals of the Rheumatic Diseases · doi:10.1136/ard.58.2008.i2 · Cited by 84
The p53 Protein Is a Novel Substrate of Ribosomal S6 Kinase 2 and a Critical Intermediary for Ribosomal S6 Kinase 2 and Histone H3 Interaction
Cho, Y., He, Z., Zhang, Y., Choi, H. S., Zhu, F., Choi, B. Y., Kang, B. S., Ma, W., Bode, A. M., & Dong, Z. (2005) · Cancer Research · doi:10.1158/0008-5472.can-04-3935 · Cited by 88
“Especially, the Ras/extracellular signal–regulated kinase (ERK) pathway regulates cell proliferation, survival, growth and motility (3, 4), and tumorigenesis (5).”
Background
New emerging roles of CD133 in cancer stem cell: Signaling pathway and miRNA regulation
Aghajani, M., Mansoori, B., Mohammadi, A., Asadzadeh, Z., & Baradaran, B. (2019) · Journal of Cellular Physiology · doi:10.1002/jcp.28824 · Cited by 83
“Subsequently, MEK activates a mitogen‐activated protein kinase (MAPK; J. Chen, Fujii, Zhang, Roberts, & Fu, 2001; Schaeffer & Weber, 1999) (Figure 2b) Akt and MAPK pathways are concerned with the tumorigenesis of CD133 + CSCs.”
Profiling and Identification of Small rDNA-Derived RNAs and Their Potential Biological Functions
Wei, H., Zhou, B. Z., Zhang, F., Tu, Y., Hu, Y., Zhang, B., & Zhai, Q. (2013) · PLoS ONE · doi:10.1371/journal.pone.0056842 · Cited by 87
“ERK pathway plays an important role in the transmission of cellular proliferation and developmental signals [40], and then we detected the effect of srRNAs on ERK pathway including the phosphorylation of ERK1/2, p90RSK, Elk-1 and p70S6K.”
Method
Anti-cancer role of SPARC, an inhibitor of adipogenesis
Nagaraju, G. P., & Sharma, D. (2011) · Cancer Treatment Reviews · doi:10.1016/j.ctrv.2010.12.001 · Cited by 86
Type II Keratins Are Phosphorylated on a Unique Motif during Stress and Mitosis in Tissues and Cultured Cells
Toivola, D. M., Zhou, Q., English, L., & Omary, M. B. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.01-12-0591 · Cited by 84
Geraniol, a Component of Plant Essential Oils, Sensitizes Human Colonic Cancer Cells to 5-Fluorouracil Treatment
Carnésecchi, S., Langley, K., Exinger, F., Gossé, F., & Raul, F. (2002) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.301.2.625 · Cited by 84
Protein Phosphorylation Cascades Associated with Methamphetamine‐induced Glial Activation
Hebert, M. A., & O'Callaghan, J. P. (2000) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2000.tb05200.x · Cited by 84
Rhein Inhibits Interleukin-1β-Induced Activation of MEK/ERK Pathway and DNA Binding of NF-κB and AP-1 in Chondrocytes Cultured in Hypoxia: A Potential Mechanism for Its Disease-Modifying Effect in Osteoarthritis
Martin, G., Bogdanowicz, P., Domagala, F., Ficheux, H., & Pujol, J. ‐. (2003) · Inflammation · doi:10.1023/a:1025040631514 · Cited by 83
“The MAPK family is composed of extracellular signal-regulated kinases (ERK 1 and ERK 2), c-Jun N-terminal kinases (JNKs) and p38 kinase (15, 16).”
Background
Basic Fibroblast Growth Factor-induced Neuronal Differentiation of Mouse Bone Marrow Stromal Cells Requires FGFR-1, MAPK/ERK, and Transcription Factor AP-1
Yang, H., Xia, Y., Lu, S. Q., Soong, T. W., & Feng, Z. W. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m706917200 · Cited by 83
Anthrax Lethal Toxin Kills Macrophages in a Strain-Specific Manner by Apoptosis or Caspase-1-Mediated Necrosis
Muehlbauer, S. M., Evering, T. H., Bonuccelli, G., Squires, R. C., Ashton, A. W., Porcelli, S. A., Lisanti, M. P., & Brojatsch, J. (2007) · Cell Cycle · doi:10.4161/cc.6.6.3991 · Cited by 83
Anthrax Lethal Toxin-Mediated Killing of Human and Murine Dendritic Cells Impairs the Adaptive Immune Response
Alileche, A., Serfass, E. R., Muehlbauer, S. M., Porcelli, S. A., & Brojatsch, J. (2005) · PLoS Pathogens · doi:10.1371/journal.ppat.0010019 · Cited by 83
“LF cleaves six of seven mitogen-activated protein kinase (MAPK) kinases (MAPKKs), thereby disrupting MAPK signaling pathways (reviewed in [7,8]).”
Alterations of MAPK Activities Associated with Intestinal Cell Differentiation
Ding, Q., Wang, Q., & Evers, B. M. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.4969 · Cited by 83
Mitogenic action of LPA in prostate
Daaka, Y. (2002) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/s1388-1981(02)00180-4 · Cited by 83
IL-1β induction of IL-6 and LIF in normal articular human chondrocytes involves the ERK, p38 and NFκB signaling pathways
Fan, Z., Bau, B., Yang, H., & Aigner, T. G. (2004) · Cytokine · doi:10.1016/j.cyto.2004.06.003 · Cited by 82
The cytoplasmic part of L1-CAM controls growth and gene expression in human tumors that is reversed by therapeutic antibodies
Gast, D., Riedle, S., Issa, Y., Pfeifer, M., Beckhove, P., Sanderson, M. P., Arlt, M., Moldenhauer, G., Fogel, M., Krüger, A., et al. (2007) · Oncogene · doi:10.1038/sj.onc.1210747 · Cited by 82
“The latter mode is required for the translocation of activated Erk from the cytoplasm to the nucleus where it regulates gene transcription (Schaeffer and Weber, 1999; Colucci-D’Amato et al., 2003).”
The MAP kinase‐encoding gene MgFus3 of the non‐appressorium phytopathogen Mycosphaerella graminicola is required for penetration and in vitro pycnidia formation
Cousin, A., Mehrabi, R., Guilleroux, M., Dufresne, M., van der Lee, T., Waalwijk, C., Langin, T., & Kema, G. H. J. (2006) · Molecular Plant Pathology · doi:10.1111/j.1364-3703.2006.00337.x · Cited by 82
Genistein induces G2/M cell cycle arrest via stable activation of ERK1/2 pathway in MDA-MB-231 breast cancer cells
Li, Z., Li, J., Bao-qing, M., Hu, C., Liu, H., Qi, H., Wang, X., & Xu, J. (2008) · Cell Biology and Toxicology · doi:10.1007/s10565-008-9054-1 · Cited by 82
Role of the p38 Mitogen-Activated Protein Kinase Pathway in the Generation of Arsenic Trioxide–Dependent Cellular Responses
Giafis, N., Katsoulidis, E., Sassano, A., Tallman, M. S., Higgins, L. S., Nebreda, Á. R., Davis, R. J., & Platanias, L. C. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-3699 · Cited by 81
MSK1 and JNKs mediate phosphorylation of STAT3 in UVA-irradiated mouse epidermal JB6 cells
Zhang, Y., Liu, G., & Dong, Z. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106044200 · Cited by 81
Intranasal deferoxamine attenuates synapse loss via up-regulating the P38/HIF-1α pathway on the brain of APP/PS1 transgenic mice
Guo, C., Zhang, Y., Wang, T., Zhong, M., Yang, Z., Hao, L.-J., Chai, R., & Zhang, S. (2015) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2015.00104 · Cited by 80
“It has been reported that different MAPKs are activated by different stimuli and target different downstream molecules; therefore, they each perform different functions (Schaeffer and Weber, 1999; Roux and Blenis, 2004).”
BackgroundMethodInfluential
Excitatory amino acid induced oligodendrocyte cell death in vitro: receptor‐dependent and ‐independent mechanisms
Rosin, C., Bates, T. E., & Skaper, S. D. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02584.x · Cited by 83
Arabidopsis MKKK20 is involved in osmotic stress response via regulation of MPK6 activity
Kim, J.-M., Woo, D.-H., Kim, S., Lee, S.-Y., Park, H.-Y., Seok, H., Chung, W. S., & Moon, Y. (2011) · Plant Cell Reports · doi:10.1007/s00299-011-1157-0 · Cited by 80
Involvement of the extracellular signal-regulated protein kinase (ERK) pathway in the induction of apoptosis by cadmium chloride in CCRF-CEM cells
Iryo, Y., Matsuoka, M., Wispriyono, B., Sugiura, T., & Igisu, H. (2000) · Biochemical Pharmacology · doi:10.1016/s0006-2952(00)00510-4 · Cited by 80
Genipin, a constituent of Gardenia jasminoides Ellis, induces apoptosis and inhibits invasion in MDA-MB-231 breast cancer cells
Moon, A. (2011) · Oncology Reports · doi:10.3892/or.2011.1508 · Cited by 79
“Activation of mitogen-activated protein kinases (MAPKs) are important intermediates in the signal-transduction pathway regulating cell proliferation and apoptosis (15-18).”
JNK3 as Therapeutic Target and Biomarker in Neurodegenerative and Neurodevelopmental Brain Diseases
Musi, C. A., Agrò, G., Santarella, F., Iervasi, E., & Borsello, T. (2020) · Cells · doi:10.3390/cells9102190 · Cited by 78
Synchronous Activation of ERK and Phosphatidylinositol 3-Kinase Pathways Is Required for Collagen and Extracellular Matrix Production in Keloids
Lim, I. J., Phan, T. T., Tan, E.-K., Nguyen, T.-T. T., Tran, E., Longaker, M. T., Song, C., Lee, S.-T., & Huynh, H.-T. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305759200 · Cited by 79
Methyl angolensate, a natural tetranortriterpenoid induces intrinsic apoptotic pathway in leukemic cells
CHIRUVELLA, K. K., Kari, V., Choudhary, B., Nambiar, M., Ghanta, R. G., & Raghavan, S. C. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.11.001 · Cited by 79
“cells distinct MAPK members have been identified, which include extracellular signal-regulated kinases (ERKs), stressactivated protein kinases (SAPKs)/c-Jun NH2-terminal kinases (JNKs), and the p38 kinases [43–45].”
Background
Proteasomes Control Caspase-1 Activation in Anthrax Lethal Toxin-mediated Cell Killing
Squires, R. C., Muehlbauer, S. M., & Brojatsch, J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705687200 · Cited by 79

Authors: Schaeffer, H. J., & Weber, M. J.
Affiliations: University of Virginia (US)
ORCID: Schaeffer, Hans J.
Weber, Michael J.
Venue: Molecular and Cellular Biology
Publisher: Informa UK Limited
Published: 1999-04
Volume: 19
Issue: 4
Pages: 2435-2444
ISSN: 0270-7306 (ISSN-L)
1098-5549
DOI: 10.1128/mcb.19.4.2435
PMC: PMC84036
OpenAlex: W1899552864
Semantic Scholar: bf5b29dd374f8bafd23fa8c6a133d764aa27c83f
Cited by: 1,600
References: 144
Citations by year: 2026: 12 · 2025: 12 · 2024: 24 · 2023: 32 · 2022: 23 · 2021: 28 · 2020: 19 · 2019: 37 · 2018: 43 · 2017: 27 · 2016: 31 · 2015: 41 · 2014: 42 · 2013: 49 · 2012: 61
FWCI: 9.18
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
Locations: Molecular and Cellular Biology (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health (5r01gm047332-08, 1r01ca076500-01a1)
U.S. Public Health Service
National Cancer Institute (CA-39076, CA76500)
National Institute of General Medical Sciences (GM-47332)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Melanoma and MAPK Pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
Keywords: mitogen-activated protein kinase, MAPK signaling, signal transduction, ERK1/2, JNK, p38 MAPK, adaptor proteins, Saccharomyces cerevisiae, cell differentiation, stress response, apoptosis, cell growth and division
MeSH terms: Carrier Proteins, Cell Compartmentation, Fungal Proteins, Models, Biological, Morphogenesis, Protein Kinases, Saccharomyces cerevisiae, Substrate Specificity, Time Factors, Signal Transduction, Calcium-Calmodulin-Dependent Protein Kinases, Receptor Cross-Talk, Mitogen-Activated Protein Kinase Kinases, Saccharomyces cerevisiae Proteins, Adaptor Proteins, Signal Transducing

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Mitogen-Activated Protein Kinases: Specific Messages from Ubiquitous Messengers

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks