MODEL1204280018
type: SBMLModel
species: COPASI22
species: COPASI15
species: COPASI10
compartment: 667410
reaction: COPASI39
species: COPASI13
reaction: COPASI33
reaction: COPASI32
reaction: COPASI45
species: 667423
species: COPASI5
reaction: COPASI46
reaction: COPASI30
species: COPASI19
reaction: COPASI28
species: COPASI3
curated: false
species: COPASI12
reaction: COPASI26
species: COPASI21
species: COPASI14
species: COPASI9
length unit: length
species: COPASI24
units def: 667360
reaction: COPASI40
species: COPASI7
reaction: COPASI35
reaction: COPASI38
reaction: COPASI48
reaction: COPASI47
species: COPASI4
reaction: COPASI29
species: COPASI18
reaction: COPASI42
species: COPASI2
species: COPASI23
units def: 667385
reaction: COPASI27
reaction: COPASI34
species: COPASI16
species: COPASI11
species: COPASI20
volume units: 667360
substance units: 667385
species: COPASI8
time units: 291235
reaction: COPASI41
reaction: COPASI37
reaction: COPASI36
area units: 061696
species: COPASI6
reaction: COPASI31
name: Sarma2012 - Interaction topologies of MAPK cascade (M2_K2_USEQ)
reaction: COPASI44
reaction: COPASI43
is described by: http://identifiers.org/pubmed/22748295
notes: Sarma2012 - Interaction topologies of MAPK cascade (M2_K2_USEQ) The paper presents the various interaction topologies between the kinases and phosphatases of MAPK cascade. They are represented as M1, M2, M3 and M4. The kinases of the cascades are MKKK, MKK and MK, and Phos1, Phos2 and Phos3 are phosphatases of the system. All three kinases in a M1 type network have specific phosphatases Phos1, Phos2 and Phos3 for the dephosphorylation process. In a M2 type system, kinases MKKK and MKK are dephosphorylated by Phos1 and MK is dephosphorylated by Phos2. The architecture of system like M3 is such that MKKK gets dephosphorylated by Phos1, whereas Phos2 dephosphorylates both MKK and MK. Finally, the MAPK cascade exhibiting more complex design of interaction such as M4 is such that MKKK and MKK are dephosphorylated by Phos1 whereas MKK and MK are dephosphorylated by Phos2. In addition, as it is plausible that the kinases can sequester their respective phosphatases by binding to them, this is considered in the design of the systems (PSEQ-sequestrated system; USEQ-Unsequestrated system). The robustness of different interaction designs of the systems is checked, considering both MichaelisMenten type kinetics (K1) and elementary mass action kinetics (K2). In the living systems, the MAPK cascade transmit both short and long duration signals where short duration signals trigger proliferation and long duration signals trigger cell differentiation. These signal variants are considered to interpret the systems behaviour. It is also tested how the robustness and signal response behaviour of K2 models are affected when K2 assumes quasi steady state (QSS). The combinations of the above variants resulted in 40 models (MODEL1204280001-40). All these 40 models are available from BioModels Database . Models that correspond to type M4 with mass-action kinetics K2, in four condition 1) USEQ [ MODEL1204280020 - M4_K2_USEQ], 2) PSEQ [ MODEL1204280024 - M4_K2_PSEQ], 3) QSS_USEQ [ MODEL12042800…
species: COPASI17
parameter: COPASI25

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COPASI15
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name: MKKK_Sig

COPASI10
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name: MKK_MKKK-P

COPASI39
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COPASI46
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COPASI26
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667436
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COPASI4
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667448
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667500
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COPASI21
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COPASI14
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COPASI40
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COPASI35
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COPASI8
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COPASI42
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COPASI37
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COPASI36
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COPASI25
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