Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
IUBMB CommentsPhosphorylation of specific tyrosine and threonine residues in the activation loop of this enzyme by EC 2.7.12.2, mitogen-activated protein kinase kinase (MAPKK) is necessary for enzyme activation. Once activated, the enzyme phosphorylates target substrates on serine or threonine residues followed by a proline . A distinguishing feature of all MAPKs is the conserved sequence Thr-Xaa-Tyr (TXY). Mitogen-activated protein kinase (MAPK) signal transduction pathways are among the most widespread mechanisms of cellular regulation. Mammalian MAPK pathways can be recruited by a wide variety of stimuli including hormones (e.g. insulin and growth hormone), mitogens (e.g. epidermal growth factor and platelet-derived growth factor), vasoactive peptides (e.g. angiotensin-II and endothelin), inflammatory cytokines of the tumour necrosis factor (TNF) family and environmental stresses such as osmotic shock, ionizing radiation and ischaemic injury.
Synonyms
mapk, p38, erk1/2, p38 mapk, mitogen-activated protein kinase, map kinase, extracellular signal-regulated kinase, p38 mitogen-activated protein kinase, p38mapk, p38 map kinase,
more
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + GLH-1
ADP + phosphorylated GLH-1
-
-
-
?
additional information
?
-
additional information
?
-
enzyme is activated in response to a variety of cellular stresses and is involved in apoptosis in neurons
-
-
?
additional information
?
-
-
enzyme is activated in response to a variety of cellular stresses and is involved in apoptosis in neurons
-
-
?
additional information
?
-
UNC-16 may regulate the localization of vesicular cargo by integrating JNK signaling and kinesin-1 transport
-
-
?
additional information
?
-
-
UNC-16 may regulate the localization of vesicular cargo by integrating JNK signaling and kinesin-1 transport
-
-
?
additional information
?
-
-
promoting influence of JNK-1 on both nuclear DAF-16 translocations and DAF-16 target gene sod-3, encoding superoxide dismutase 3, expressions within peripheral, non-neuronal tissue, JNK-1 modulates the intestinal stress-induced translocation of DAF-16 from the cytosol into the cell nucleus. JNK-1 is controlled by the MAPK JKK-1 under heat stress
-
-
?
additional information
?
-
promoting influence of JNK-1 on both nuclear DAF-16 translocations and DAF-16 target gene sod-3, encoding superoxide dismutase 3, expressions within peripheral, non-neuronal tissue, JNK-1 modulates the intestinal stress-induced translocation of DAF-16 from the cytosol into the cell nucleus. JNK-1 is controlled by the MAPK JKK-1 under heat stress
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + GLH-1
ADP + phosphorylated GLH-1
-
-
-
?
additional information
?
-
additional information
?
-
enzyme is activated in response to a variety of cellular stresses and is involved in apoptosis in neurons
-
-
?
additional information
?
-
-
enzyme is activated in response to a variety of cellular stresses and is involved in apoptosis in neurons
-
-
?
additional information
?
-
UNC-16 may regulate the localization of vesicular cargo by integrating JNK signaling and kinesin-1 transport
-
-
?
additional information
?
-
-
UNC-16 may regulate the localization of vesicular cargo by integrating JNK signaling and kinesin-1 transport
-
-
?
additional information
?
-
-
promoting influence of JNK-1 on both nuclear DAF-16 translocations and DAF-16 target gene sod-3, encoding superoxide dismutase 3, expressions within peripheral, non-neuronal tissue, JNK-1 modulates the intestinal stress-induced translocation of DAF-16 from the cytosol into the cell nucleus. JNK-1 is controlled by the MAPK JKK-1 under heat stress
-
-
?
additional information
?
-
promoting influence of JNK-1 on both nuclear DAF-16 translocations and DAF-16 target gene sod-3, encoding superoxide dismutase 3, expressions within peripheral, non-neuronal tissue, JNK-1 modulates the intestinal stress-induced translocation of DAF-16 from the cytosol into the cell nucleus. JNK-1 is controlled by the MAPK JKK-1 under heat stress
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
arsenite
treatment of worms with arsenite, a toxic ROS-producing compound, induces a robust phosphorylation of PMK-1, induction of oxidative stress-responsive genes, and eventual lethality. Activation of PMK-1 following arsenite treatment is dependent on SEK-1 but independent of NSY-1, differing from the NSY-1/SEK-1/PMK-1 cascade used during infection and osmotic stress
additional information
-
JNK-1 is activated by phosphorylation, ambient temperature of 1-37°C specifically influences the activation/phosphorylation of the MAPkinase JNK-1
-
additional information
JNK-1 is activated by phosphorylation, ambient temperature of 1-37°C specifically influences the activation/phosphorylation of the MAPkinase JNK-1
-
additional information
-
C493C.10 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-5
-
additional information
C493C.10 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-5
-
additional information
C493C.10 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-5
-
additional information
C493C.10 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-5
-
additional information
C493C.10 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-5
-
additional information
C493C.10 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-5
-
additional information
C493C.10 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-5
-
additional information
-
jnk-1 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-4. Activation of JNK signaling occurs under conditions of heavy metal stress
-
additional information
jnk-1 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-4. Activation of JNK signaling occurs under conditions of heavy metal stress
-
additional information
jnk-1 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-4. Activation of JNK signaling occurs under conditions of heavy metal stress
-
additional information
jnk-1 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-4. Activation of JNK signaling occurs under conditions of heavy metal stress
-
additional information
jnk-1 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-4. Activation of JNK signaling occurs under conditions of heavy metal stress
-
additional information
jnk-1 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-4. Activation of JNK signaling occurs under conditions of heavy metal stress
-
additional information
jnk-1 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-4. Activation of JNK signaling occurs under conditions of heavy metal stress
-
additional information
-
kgb-1 is phosphorylated and activated by mitogen-activated protein kinase kinase jkk-1
-
additional information
kgb-1 is phosphorylated and activated by mitogen-activated protein kinase kinase jkk-1
-
additional information
kgb-1 is phosphorylated and activated by mitogen-activated protein kinase kinase jkk-1
-
additional information
kgb-1 is phosphorylated and activated by mitogen-activated protein kinase kinase jkk-1
-
additional information
kgb-1 is phosphorylated and activated by mitogen-activated protein kinase kinase jkk-1
-
additional information
kgb-1 is phosphorylated and activated by mitogen-activated protein kinase kinase jkk-1
-
additional information
kgb-1 is phosphorylated and activated by mitogen-activated protein kinase kinase jkk-1
-
additional information
-
kgb-2 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-3
-
additional information
kgb-2 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-3
-
additional information
kgb-2 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-3
-
additional information
kgb-2 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-3
-
additional information
kgb-2 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-3
-
additional information
kgb-2 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-3
-
additional information
kgb-2 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-3
-
additional information
-
pmk-1 is phosphorylated and activated by mitogen-activated protein kinase kinase mkk-4. Unique upstream components activating PMK-1 induce SKN-1 activation following toxin and bacterial exposure
-
additional information
pmk-1 is phosphorylated and activated by mitogen-activated protein kinase kinase mkk-4. Unique upstream components activating PMK-1 induce SKN-1 activation following toxin and bacterial exposure
-
additional information
pmk-1 is phosphorylated and activated by mitogen-activated protein kinase kinase mkk-4. Unique upstream components activating PMK-1 induce SKN-1 activation following toxin and bacterial exposure
-
additional information
pmk-1 is phosphorylated and activated by mitogen-activated protein kinase kinase mkk-4. Unique upstream components activating PMK-1 induce SKN-1 activation following toxin and bacterial exposure
-
additional information
pmk-1 is phosphorylated and activated by mitogen-activated protein kinase kinase mkk-4. Unique upstream components activating PMK-1 induce SKN-1 activation following toxin and bacterial exposure
-
additional information
pmk-1 is phosphorylated and activated by mitogen-activated protein kinase kinase mkk-4. Unique upstream components activating PMK-1 induce SKN-1 activation following toxin and bacterial exposure
-
additional information
pmk-1 is phosphorylated and activated by mitogen-activated protein kinase kinase mkk-4. Unique upstream components activating PMK-1 induce SKN-1 activation following toxin and bacterial exposure
-
additional information
-
pmk-2 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-1
-
additional information
pmk-2 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-1
-
additional information
pmk-2 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-1
-
additional information
pmk-2 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-1
-
additional information
pmk-2 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-1
-
additional information
pmk-2 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-1
-
additional information
pmk-2 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-1
-
additional information
-
pmk-3 is phosphorylated and activated by mitogen-activated protein kinase kinase mek-1
-
additional information
pmk-3 is phosphorylated and activated by mitogen-activated protein kinase kinase mek-1
-
additional information
pmk-3 is phosphorylated and activated by mitogen-activated protein kinase kinase mek-1
-
additional information
pmk-3 is phosphorylated and activated by mitogen-activated protein kinase kinase mek-1
-
additional information
pmk-3 is phosphorylated and activated by mitogen-activated protein kinase kinase mek-1
-
additional information
pmk-3 is phosphorylated and activated by mitogen-activated protein kinase kinase mek-1
-
additional information
pmk-3 is phosphorylated and activated by mitogen-activated protein kinase kinase mek-1
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
evolution
C493C.10 is an orthologue of mammalian JNK
evolution
jnk-1 is an orthologue of mammalian JNK
evolution
kgb-1 is an orthologue of mammalian JNK
evolution
kgb-2 is an orthologue of mammalian JNK. The JNK homologue KGB-2 shows 84% identity with KGB-1
evolution
pmk-1 is an orthologue of mammalian p38. The three pmk genes pmk1, pmk-2, and pmk-3, are encoded by a single polycistronic transcript (operon), precluding the generation of double mutants by traditional genetic crosses
evolution
pmk-2 is an orthologue of mammalian p38. The three pmk genes pmk1, pmk-2, and pmk-3, are encoded by a single polycistronic transcript (operon), precluding the generation of double mutants by traditional genetic crosses
evolution
pmk-3 is an orthologue of mammalian p38. The three pmk genes pmk1, pmk-2, and pmk-3, are encoded by a single polycistronic transcript (operon), precluding the generation of double mutants by traditional genetic crosses
malfunction
a kgb-1 null mutant, obtained by targeted deletion, shows extra germ cells, increased number of P granules, and temperature-sensitive sterility. RNAi-mediated knockdown of glh-1 in kgb-1 mutants partially rescues the P granule number and temperature-sensitive sterility. Null mutations in vhp-1 cause larval lethality, which can be suppressed by null mutations in mlk-1, mek-1, kgb-1, dlk-1, or pmk-3
malfunction
null mutations in vhp-1 cause larval lethality, which can be suppressed by null mutations in mlk-1, mek-1, kgb-1, dlk-1, or pmk-3. DLK-1/PMK-3 are identified to affect cilia length, via regulation of RAB-5 endosomes
malfunction
removing the 3'-UTR of pmk-2 causes its expression in the intestine, which is sufficient to rescue the Esp phenotype of pmk-1 mutants. The Esp mutant phenotype worms show enhanced susceptibility to Pseudomonas aeruginosa that causes an intestinal infection and eventual death of the worm
metabolism
distinct p38 and JNK MAPK cascades regulate a diverse class of normal biological processes during development and nervous system function
metabolism
the core MAPK signaling cassette consists of a MAPKKK/MAPKK/MAPK cascade, stress-activated MAPK components involved in non-stress-associated processes, overview
metabolism
the core MAPK signaling cassette consists of a MAPKKK/MAPKK/MAPK cascade, stress-activated MAPK components involved in non-stress-associated processes, overview. Distinct p38 and JNK MAPK cascades regulate a diverse class of normal biological processes during development and nervous system function
metabolism
the core MAPK signaling cassette consists of a MAPKKK/MAPKK/MAPK cascade, stress-activated MAPK components involved in non-stress-associated processes, overview. Distinct p38 and JNK MAPK cascades regulate a diverse class of normal biological processes during development and nervous system function. Functional redundancy of pmk-1 and pmk-2
metabolism
the core MAPK signaling cassette consists of a MAPKKK/MAPKK/MAPK cascade, stress-activated MAPK components involved in non-stress-associated processes, overview. Distinct p38 and JNK MAPK cascades regulate a diverse class of normal biological processes during development and nervous system function. The three kinases DLK-1/MKK-4/PMK-3 constitute a linear pathway. MAK-2 is the homologue of MAPKAPK2 (MK2), and acts downstream of PMK-3. The conserved pathway, the DLK-1/MKK-4/PMK-3 cascade, activation is necessary to initiate axonal regrowth. The cascade is tightly regulated by protein ubiquitination during synapse development
physiological function
activation of JNK signaling occurs under conditions of heavy metal stress. Olfactory memory in Caenorhabditis elegans allows for the association of cues with positive or negative experiences. The loss of these memories proceeds through the UNC-43/TIR-1/NSY-1/SEK-1/JNK-1 cascade
physiological function
PMK-3 acts during neuronal development. vhp-1 regulates MAP kinases in axon regeneration. svh-1 and svh-2 likely provide a layer of specificity in controlling the KGB-1/JNK pathway, independently of PMK-3 in axon injury response, crosstalk between the KGB-1 and PMK-3 cascades. The avoidance of high CO2 environments and pathogens is mediated by MOM-4/MKK-4/PMK-3 in the BAG neuron
physiological function
roles for KGB-2 are in excess carbon dioxide (hypercapnia)-induced fertility defects and a slight negative role in axon injury response
physiological function
the enzyme is involved in P granule formation in germ cell proliferation. KGB-1 can bind and phosphorylate GLH-1, which leads to degradation of phosphorylated GLH-1. KGB-1 activity negatively regulates GLH-1 and the steady state level of P granules to maintain fertility. vhp-1 regulates MAP kinases in axon regeneration. svh-1 and svh-2 likely provide a layer of specificity in controlling the KGB-1/JNK pathway, independently of PMK-3 in axon injury response, crosstalk between the KGB-1 and PMK-3 cascades. The aversive reaction to microbial exposure is mediated by a MLK-1/MEK-1(SEK-1)/KGB-1 pathway
physiological function
the NSY-1/SEK-1/PMK-1 and PMK-2 cascade acts during neuronal development to regulate AWC asymmetry. The activation of this cascade is regulated in part by calcium, via calmodulin kinase II, as well as the conserved protein TIR-1. PMK-1 and PMK-2 act redundantly downstream of TIR-1/NSY-1/SEK-1 to induce TPH-1 expression in the ADF neuron following exposure to bacteria. Genes pmk-1 and pmk-2 function redundantly during olfactory neuronal development
physiological function
the NSY-1/SEK-1/PMK-1 and PMK-2 cascade acts during neuronal development to regulate AWC asymmetry. The activation of this cascade is regulated in part by calcium, via calmodulin kinase II, as well as the conserved protein TIR-1. PMK-1 and PMK-2 act redundantly downstream of TIR-1/NSY-1/SEK-1 to induce TPH-1 expression in the ADF neuron following exposure to bacteria. Genes pmk-1 and pmk-2 function redundantly during olfactory neuronal development. Activation of PMK-1 following arsenite treatment is dependent on SEK-1 but independent of NSY-1, differing from the NSY-1/SEK-1/PMK-1 cascade used during infection and osmotic stress. Unique upstream components activating PMK-1 induce SKN-1 activation following toxin and bacterial exposure
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
additional information
-
transgenic jnk-1 deletion mutant, exhibits a reduced thermal tolerance and reproductive fitness at higher temperatures
additional information
transgenic jnk-1 deletion mutant, exhibits a reduced thermal tolerance and reproductive fitness at higher temperatures
additional information
-
construction of a JNK-1 deletion mutant expressing daf-16-GFP, the mutant exhibits a reduced thermal tolerance and reproductive fitness at higher temperatures compared to the wild-type enzyme, jnk-1 overexpression leads to enhanced translocation of DAF-16
additional information
construction of a JNK-1 deletion mutant expressing daf-16-GFP, the mutant exhibits a reduced thermal tolerance and reproductive fitness at higher temperatures compared to the wild-type enzyme, jnk-1 overexpression leads to enhanced translocation of DAF-16
additional information
-
a kgb-1 null mutant is obtained by targeted deletion
additional information
a kgb-1 null mutant is obtained by targeted deletion
additional information
a kgb-1 null mutant is obtained by targeted deletion
additional information
a kgb-1 null mutant is obtained by targeted deletion
additional information
a kgb-1 null mutant is obtained by targeted deletion
additional information
a kgb-1 null mutant is obtained by targeted deletion
additional information
a kgb-1 null mutant is obtained by targeted deletion
additional information
-
a strain with mutations in both pmk-1 and pmk-2 is serendipitously identified in a screen searching for suppressors of the pmk-1 loss of function phenotype following bacterial infection
additional information
a strain with mutations in both pmk-1 and pmk-2 is serendipitously identified in a screen searching for suppressors of the pmk-1 loss of function phenotype following bacterial infection
additional information
a strain with mutations in both pmk-1 and pmk-2 is serendipitously identified in a screen searching for suppressors of the pmk-1 loss of function phenotype following bacterial infection
additional information
a strain with mutations in both pmk-1 and pmk-2 is serendipitously identified in a screen searching for suppressors of the pmk-1 loss of function phenotype following bacterial infection
additional information
a strain with mutations in both pmk-1 and pmk-2 is serendipitously identified in a screen searching for suppressors of the pmk-1 loss of function phenotype following bacterial infection
additional information
a strain with mutations in both pmk-1 and pmk-2 is serendipitously identified in a screen searching for suppressors of the pmk-1 loss of function phenotype following bacterial infection
additional information
a strain with mutations in both pmk-1 and pmk-2 is serendipitously identified in a screen searching for suppressors of the pmk-1 loss of function phenotype following bacterial infection
additional information
-
a strain with mutations in both pmk-1 and pmk-2 is serendipitously identified in a screen searching for suppressors of the pmk-1 loss of function phenotype following bacterial infection. Removing the 3'-UTR of pmk-2 causes its expression in the intestine, which is sufficient to rescue the Esp phenotype of pmk-1 mutants
additional information
a strain with mutations in both pmk-1 and pmk-2 is serendipitously identified in a screen searching for suppressors of the pmk-1 loss of function phenotype following bacterial infection. Removing the 3'-UTR of pmk-2 causes its expression in the intestine, which is sufficient to rescue the Esp phenotype of pmk-1 mutants
additional information
a strain with mutations in both pmk-1 and pmk-2 is serendipitously identified in a screen searching for suppressors of the pmk-1 loss of function phenotype following bacterial infection. Removing the 3'-UTR of pmk-2 causes its expression in the intestine, which is sufficient to rescue the Esp phenotype of pmk-1 mutants
additional information
a strain with mutations in both pmk-1 and pmk-2 is serendipitously identified in a screen searching for suppressors of the pmk-1 loss of function phenotype following bacterial infection. Removing the 3'-UTR of pmk-2 causes its expression in the intestine, which is sufficient to rescue the Esp phenotype of pmk-1 mutants
additional information
a strain with mutations in both pmk-1 and pmk-2 is serendipitously identified in a screen searching for suppressors of the pmk-1 loss of function phenotype following bacterial infection. Removing the 3'-UTR of pmk-2 causes its expression in the intestine, which is sufficient to rescue the Esp phenotype of pmk-1 mutants
additional information
a strain with mutations in both pmk-1 and pmk-2 is serendipitously identified in a screen searching for suppressors of the pmk-1 loss of function phenotype following bacterial infection. Removing the 3'-UTR of pmk-2 causes its expression in the intestine, which is sufficient to rescue the Esp phenotype of pmk-1 mutants
additional information
a strain with mutations in both pmk-1 and pmk-2 is serendipitously identified in a screen searching for suppressors of the pmk-1 loss of function phenotype following bacterial infection. Removing the 3'-UTR of pmk-2 causes its expression in the intestine, which is sufficient to rescue the Esp phenotype of pmk-1 mutants
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Wu, Y.; Han, M.
Suppression of activated Let-60 ras protein defines a role of Caenorhabditis elegans Sur-1 MAP kinase in vulval differentiation
Genes Dev.
8
147-159
1994
Caenorhabditis elegans (P39745), Caenorhabditis elegans
brenda
Lackner, M.R.; Kornfeld, K.; Miller, L.M.; Horvitz, H.R.; Kim, S.K.
A MAP kinase homolog, mpk-1, is involved in ras-mediated induction of vulval cell fates in Caenorhabditis elegans
Genes Dev.
8
160-173
1994
Caenorhabditis elegans (P39745), Caenorhabditis elegans
brenda
Byrd, D.T.; Kawasaki, M.; Walcoff, M.; Hisamoto, N.; Matsumoto, K.; Jin, Y.
UNC-16, a JNK-signaling scaffold protein, regulates vesicle transport in C. elegans
Neuron
32
787-800
2001
Caenorhabditis elegans (Q8WQG9), Caenorhabditis elegans
brenda
Kawasaki, M.; Hisamoto, N.; Iino, Y.; Yamamoto, M.; Ninomiya-Tsuji, J.; Matsumoto, K.
A Caenorhabditis elegans JNK signal transduction pathway regulates coordinated movement via type-D GABAergic motor neurons
EMBO J.
18
3604-3615
1999
Caenorhabditis elegans (Q8WQG9), Caenorhabditis elegans
brenda
Wolf, M.; Nunes, F.; Henkel, A.; Heinick, A.; Paul, R.J.
The MAP kinase JNK-1 of Caenorhabditis elegans: Location, activation, and influences over temperature-dependent insulin-like signaling, stress responses, and fitness
J. Cell. Physiol.
214
721-729
2007
Caenorhabditis elegans, Caenorhabditis elegans (Q8WQG9)
brenda
Andrusiak, M.G.; Jin, Y.
Context specificity of stress-activated mitogen-activated protein (MAP) kinase signaling: the story as told by Caenorhabditis elegans
J. Biol. Chem.
291
7796-7804
2016
Caenorhabditis elegans, Caenorhabditis elegans (H2KZI0), Caenorhabditis elegans (O44408), Caenorhabditis elegans (O44514), Caenorhabditis elegans (Q17446), Caenorhabditis elegans (Q8MXI4), Caenorhabditis elegans (Q8WQG9)
brenda