KEGG   PATHWAY: ppad04613
Entry
ppad04613                   Pathway                                
Name
Neutrophil extracellular trap formation - Panthera pardus (leopard)
Description
Neutrophils play a central role in innate immune defense. One of the mechanisms of neutrophil action is the formation of neutrophil extracellular traps (NETs), the extracellular structures composed of chromatin coated with histones, proteases and granular and cytosolic proteins that help catch and kill microorganisms. NETs are formed by a process known as "NETosis" that can be triggered by microorganisms and endogenous stimuli, such as damage-associated molecular patterns and immune complexes, and involves activation in most cases of nicotinamide adenine dinucleotide phosphate (NADPH)-oxidase, which produces reactive oxygen species (ROS). Recent study has reported that there are two different mechanisms of NETosis, including a lytic NETosis and a vital NETosis. Lytic NETosis begins with nuclear delobulation and the disassembly of the nuclear envelope and continues with loss of cellular polarization, chromatin decondensation and plasma membrane rupture. Vital NETosis can occur independently of cell death and involves the secreted expulsion of nuclear chromatin that is accompanied by the release of granule proteins through degranulation.
Class
Organismal Systems; Immune system
Pathway map
ppad04613  Neutrophil extracellular trap formation
ppad04613

Organism
Panthera pardus (leopard) [GN:ppad]
Gene
109276673  FCGR3A; low affinity immunoglobulin gamma Fc region receptor III-A isoform X1 [KO:K06463]
109275517  SYK; tyrosine-protein kinase SYK isoform X1 [KO:K05855] [EC:2.7.10.2]
109263420  MAP3K7; mitogen-activated protein kinase kinase kinase 7 isoform X1 [KO:K04427] [EC:2.7.11.25]
109257492  RAF1; RAF proto-oncogene serine/threonine-protein kinase isoform X1 [KO:K04366] [EC:2.7.11.1]
109262816  MAP2K1; dual specificity mitogen-activated protein kinase kinase 1 isoform X1 [KO:K04368] [EC:2.7.12.2]
109255967  MAP2K2; dual specificity mitogen-activated protein kinase kinase 2 isoform X1 [KO:K04369] [EC:2.7.12.2]
109259699  MAPK1; mitogen-activated protein kinase 1 [KO:K04371] [EC:2.7.11.24]
109261343  MAPK3; mitogen-activated protein kinase 3 [KO:K04371] [EC:2.7.11.24]
109248000  cytochrome b-245 heavy chain isoform X1 [KO:K21421] [EC:1.-.-.-]
109250624  NCF1; neutrophil cytosol factor 1 isoform X1 [KO:K08011]
109245544  cytochrome b-245 light chain [KO:K08009]
109253911  NCF2; neutrophil cytosol factor 2 isoform X1 [KO:K08010]
109265518  NCF4; neutrophil cytosol factor 4 isoform X1 [KO:K08012]
109251192  RAC1; ras-related C3 botulinum toxin substrate 1 isoform X1 [KO:K04392]
109265228  RAC2; ras-related C3 botulinum toxin substrate 2 [KO:K07860]
109248292  TLR7; toll-like receptor 7 isoform X1 [KO:K05404]
109248293  TLR8; toll-like receptor 8 [KO:K10170]
109257711  neutrophil elastase-like isoform X1 [KO:K01327] [EC:3.4.21.37]
109247205  MPO; myeloperoxidase isoform X1 [KO:K10789] [EC:1.11.2.2]
109276785  ACTG1; actin, cytoplasmic 2 [KO:K05692]
109251167  ACTB; actin, cytoplasmic 1 [KO:K05692]
109250866  VDAC1; voltage-dependent anion-selective channel protein 1 [KO:K05862]
109264442  VDAC2; voltage-dependent anion-selective channel protein 2 [KO:K15040]
109262260  VDAC3; voltage-dependent anion-selective channel protein 3 isoform X1 [KO:K15041]
109250770  SLC25A5; ADP/ATP translocase 2 [KO:K05863]
109251009  SLC25A4; ADP/ATP translocase 1 [KO:K05863]
109256146  SLC25A6; ADP/ATP translocase 3 [KO:K05863]
109249044  SLC25A31; ADP/ATP translocase 4 [KO:K05863]
109264473  PPIF; peptidyl-prolyl cis-trans isomerase F, mitochondrial isoform X1 [KO:K09565] [EC:5.2.1.8]
109274195  PADI4; protein-arginine deiminase type-4 isoform X1 [KO:K24669] [EC:3.5.3.15]
109257074  LOW QUALITY PROTEIN: high affinity immunoglobulin gamma Fc receptor I-like [KO:K06498]
109259037  ITGAM; integrin alpha-M isoform X1 [KO:K06461]
109258109  ITGB2; integrin beta-2 [KO:K06464]
109259024  ITGAL; integrin alpha-L isoform X1 [KO:K05718]
109259085  CLEC7A; C-type lectin domain family 7 member A isoform X1 [KO:K10074]
109272472  SRC; proto-oncogene tyrosine-protein kinase Src isoform X1 [KO:K05704] [EC:2.7.10.2]
109246661  PLCB3; 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3 isoform X1 [KO:K05858] [EC:3.1.4.11]
109274721  PLCB4; 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-4 isoform X1 [KO:K05858] [EC:3.1.4.11]
109274722  PLCB1; 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1 isoform X1 [KO:K05858] [EC:3.1.4.11]
109263166  PLCB2; 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2 isoform X1 [KO:K05858] [EC:3.1.4.11]
109272437  PLCG1; 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1 isoform X1 [KO:K01116] [EC:3.1.4.11]
109245637  PLCG2; 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2 [KO:K05859] [EC:3.1.4.11]
109277056  PRKCA; protein kinase C alpha type isoform X1 [KO:K02677] [EC:2.7.11.13]
109255537  PRKCB; protein kinase C beta type isoform X1 [KO:K19662] [EC:2.7.11.13]
109259277  PRKCG; protein kinase C gamma type isoform X1 [KO:K19663] [EC:2.7.11.13]
109254351  ATG7; ubiquitin-like modifier-activating enzyme ATG7 [KO:K08337]
109252946  FPR2; N-formyl peptide receptor 2 [KO:K04173]
109274075  PIK3CD; phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform isoform X1 [KO:K00922] [EC:2.7.1.153]
109275159  PIK3CA; phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform [KO:K00922] [EC:2.7.1.153]
109259912  PIK3CB; phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoform [KO:K00922] [EC:2.7.1.153]
109266953  PIK3R3; phosphatidylinositol 3-kinase regulatory subunit gamma [KO:K02649]
109275060  PIK3R1; phosphatidylinositol 3-kinase regulatory subunit alpha isoform X1 [KO:K02649]
109247606  PIK3R2; phosphatidylinositol 3-kinase regulatory subunit beta [KO:K02649]
109256570  AKT2; RAC-beta serine/threonine-protein kinase [KO:K04456] [EC:2.7.11.1]
109251379  AKT3; RAC-gamma serine/threonine-protein kinase isoform X1 [KO:K04456] [EC:2.7.11.1]
109257810  AKT1; RAC-alpha serine/threonine-protein kinase isoform X1 [KO:K04456] [EC:2.7.11.1]
109274103  MTOR; serine/threonine-protein kinase mTOR [KO:K07203] [EC:2.7.11.1]
109247385  NFKB1; nuclear factor NF-kappa-B p105 subunit isoform X1 [KO:K02580]
109246747  RELA; transcription factor p65 isoform X1 [KO:K04735]
109261021  C3; complement C3 isoform X1 [KO:K03990]
109261022  complement C3-like [KO:K03990]
109255305  CR1L; complement component receptor 1-like protein [KO:K04011]
109269880  complement C5-like isoform X1 [KO:K03994]
109269885  complement C5-like [KO:K03994]
109253169  C5AR1; C5a anaphylatoxin chemotactic receptor 1 [KO:K04010]
109266100  HMGB1; high mobility group protein B1 [KO:K10802]
109262509  TLR2; toll-like receptor 2 [KO:K10159]
109269905  TLR4; toll-like receptor 4 isoform X1 [KO:K10160]
109265257  MAPK11; LOW QUALITY PROTEIN: mitogen-activated protein kinase 11 [KO:K04441] [EC:2.7.11.24]
109265767  mitogen-activated protein kinase 12 isoform X1 [KO:K04441] [EC:2.7.11.24]
109271512  MAPK14; mitogen-activated protein kinase 14 isoform X1 [KO:K04441] [EC:2.7.11.24]
109271515  MAPK13; mitogen-activated protein kinase 13 isoform X1 [KO:K04441] [EC:2.7.11.24]
109258195  ITGA2B; integrin alpha-IIb [KO:K06476]
109262500  FGA; fibrinogen alpha chain [KO:K03903]
109262501  FGB; fibrinogen beta chain [KO:K03904]
109262499  FGG; fibrinogen gamma chain isoform X1 [KO:K03905]
109246019  GP1BA; LOW QUALITY PROTEIN: platelet glycoprotein Ib alpha chain [KO:K06261]
109276146  VWF; von Willebrand factor [KO:K03900]
109252059  SELP; P-selectin isoform X1 [KO:K06496]
109277488  SELPLG; P-selectin glycoprotein ligand 1 isoform X1 [KO:K06544]
109260522  AGER; advanced glycosylation end product-specific receptor isoform X1 [KO:K19722]
109258467  caspase-1 isoform X1 [KO:K04394] [EC:3.4.22.57 3.4.22.64]
109258300  GSDMD; gasdermin-D [KO:K20917]
109272964  HAT1; histone acetyltransferase type B catalytic subunit [KO:K11303] [EC:2.3.1.48]
109268650  histone H2A.J [KO:K11251]
109259599  histone H2A type 3 [KO:K11251]
109260878  histone H2A-Bbd type 2/3-like [KO:K11251]
109247998  histone H2A-Bbd type 1-like [KO:K11251]
109257036  histone H2A type 2-C isoform X1 [KO:K11251]
109257037  histone H2A type 2-A [KO:K11251]
109257038  histone H2A type 2-B [KO:K11251]
109257039  histone H2A type 2-B [KO:K11251]
109267932  histone H2A.V isoform X1 [KO:K11251]
109259330  histone H2A-Bbd type 1-like [KO:K11251]
109278537  histone H2AX [KO:K11251]
109252657  histone H2A type 1-E [KO:K11251]
109252668  histone H2A type 1-H-like [KO:K11251]
109252671  histone H2A type 1-C-like [KO:K11251]
109252680  histone H2A-IV-like [KO:K11251]
109260937  histone H2A-Bbd type 2/3-like [KO:K11251]
109260939  histone H2A-Bbd type 2/3-like [KO:K11251]
109247286  histone H2A.Z [KO:K11251]
109264360  core histone macro-H2A.2 [KO:K11251]
109261801  histone H2A-Bbd type 2/3-like [KO:K11251]
109250833  core histone macro-H2A.1 isoform X1 [KO:K11251]
109252578  histone H2A type 1-E-like [KO:K11251]
109252588  histone H2A type 1 [KO:K11251]
109252589  histone H2A type 1 [KO:K11251]
109252590  histone H2A type 1-C [KO:K11251]
109252591  histone H2A type 1-E [KO:K11251]
109252592  histone H2A type 1-E [KO:K11251]
109252594  histone H2A type 1-H-like [KO:K11251]
109252595  histone H2A type 1-E [KO:K11251]
109252596  histone H2A type 1-E [KO:K11251]
109252597  histone H2A type 1-E [KO:K11251]
109252598  histone H2A type 1-H-like [KO:K11251]
109252599  histone H2A type 1-E-like [KO:K11251]
109259600  histone H2B type 3-B [KO:K11252]
109252746  histone H2B type 1 [KO:K11252]
109257040  histone H2B type 2-E [KO:K11252]
109257041  histone H2B type 2-E [KO:K11252]
109257042  histone H2B type 2-E [KO:K11252]
109252384  late histone H2B.L4-like [KO:K11252]
109252606  histone H2B type 1-J [KO:K11252]
109252607  histone H2B type 1-K [KO:K11252]
109252608  histone H2B type 1 [KO:K11252]
109252609  histone H2B type 1 [KO:K11252]
109252610  histone H2B type 1-K [KO:K11252]
109252611  histone H2B type 1 [KO:K11252]
109252612  histone H2B type 1 [KO:K11252]
109252614  histone H2B type 1 [KO:K11252]
109252615  histone H2B type 1-B [KO:K11252]
109252628  histone H2B type 1 [KO:K11252]
109252681  histone H2B type 1-A [KO:K11252]
109252682  histone H2B type 1-A-like [KO:K11252]
109257084  histone H2B type 2-F [KO:K11252]
109251916  histone H2B, gonadal-like [KO:K11252]
109275092  histone H2B subacrosomal variant-like [KO:K11252]
109252600  histone H2B type 1-M [KO:K11252]
109252601  histone H2B type 1-M [KO:K11252]
109252602  histone H2B type 1 [KO:K11252]
109252604  histone H2B type 1 [KO:K11252]
109252605  histone H2B type 1 [KO:K11252]
109256440  histone H2B type 1-A-like [KO:K11252]
109268648  histone H4 [KO:K11254]
109252616  histone H4-like [KO:K11254]
109252617  histone H4 [KO:K11254]
109252618  histone H4 [KO:K11254]
109252619  histone H4 [KO:K11254]
109252620  histone H4 [KO:K11254]
109252621  histone H4 [KO:K11254]
109252622  histone H4 [KO:K11254]
109252623  histone H4 [KO:K11254]
109252624  histone H4 [KO:K11254]
109252627  histone H4 [KO:K11254]
109252672  histone H4-like [KO:K11254]
109257094  histone H4 [KO:K11254]
109252582  histone H4 [KO:K11254]
109259607  LOW QUALITY PROTEIN: histone H3.3 [KO:K11253]
109263783  histone H3.3-like [KO:K11253]
109252626  histone H3.1 [KO:K11253]
109252658  histone H3.1-like [KO:K11253]
109252669  histone H3-like centromeric protein cpar-1 [KO:K11253]
109252670  uncharacterized protein LOC109252670 [KO:K11253]
109252675  uncharacterized protein LOC109252675 [KO:K11253]
109257083  histone H3 [KO:K11253]
109253796  histone H3.3-like [KO:K11253]
109250864  histone H3.3 [KO:K11253]
109252580  histone H3.3-like [KO:K11253]
109252583  histone H3.1 [KO:K11253]
109252584  histone H3.1 [KO:K11253]
109252586  histone H3.1 [KO:K11253]
109252587  histone H3.1 [KO:K11253]
109276921  histone H3.3 [KO:K11253]
109255290  HDAC1; histone deacetylase 1 isoform X1 [KO:K06067] [EC:3.5.1.98]
109263573  HDAC2; histone deacetylase 2 isoform X1 [KO:K06067] [EC:3.5.1.98]
109252210  HDAC3; histone deacetylase 3 isoform X1 [KO:K11404] [EC:3.5.1.98]
109258180  HDAC5; histone deacetylase 5 isoform X1 [KO:K11406] [EC:3.5.1.98]
109264820  HDAC4; histone deacetylase 4 [KO:K11406] [EC:3.5.1.98]
109248075  HDAC6; histone deacetylase 6 isoform X1 [KO:K11407] [EC:3.5.1.98]
109249024  HDAC7; histone deacetylase 7 isoform X1 [KO:K11408] [EC:3.5.1.98]
109260683  HDAC8; histone deacetylase 8 isoform X1 [KO:K11405] [EC:3.5.1.98]
109263789  HDAC9; histone deacetylase 9 isoform X1 [KO:K11409] [EC:3.5.1.98]
109265766  HDAC10; histone deacetylase 10 isoform X1 [KO:K18671] [EC:3.5.1.98]
109257498  HDAC11; histone deacetylase 11 [KO:K11418] [EC:3.5.1.98]
109254958  cathepsin G-like [KO:K01319] [EC:3.4.21.20]
109247748  CAMP; cathelicidin antimicrobial peptide [KO:K13916]
109248102  CLCN5; H(+)/Cl(-) exchange transporter 5 isoform X1 [KO:K05012]
109248279  CLCN4; H(+)/Cl(-) exchange transporter 4 isoform X1 [KO:K05012]
109262431  CLCN3; H(+)/Cl(-) exchange transporter 3 isoform X1 [KO:K05012]
109262921  AQP9; aquaporin-9 [KO:K09877]
Compound
C00027  Hydrogen peroxide
C00039  DNA
C00076  Calcium cation
C00165  Diacylglycerol
C00338  Lipopolysaccharide
C00464  Mannan
C00518  Hyaluronate
C00551  beta-D-Glucan
C00704  Superoxide
C01245  D-myo-Inositol 1,4,5-trisphosphate
C05151  12-O-Tetradecanoylphorbol 13-acetate
C05981  Phosphatidylinositol-3,4,5-trisphosphate
C11221  Formylmethionyl-leucyl-phenylalanine methyl ester
Reference
  Authors
Van Avondt K, Hartl D
  Title
Mechanisms and disease relevance of neutrophil extracellular trap formation.
  Journal
Eur J Clin Invest 48 Suppl 2:e12919 (2018)
DOI:10.1111/eci.12919
Reference
  Authors
Sorvillo N, Cherpokova D, Martinod K, Wagner DD
  Title
Extracellular DNA NET-Works With Dire Consequences for Health.
  Journal
Circ Res 125:470-488 (2019)
DOI:10.1161/CIRCRESAHA.119.314581
Reference
  Authors
Papayannopoulos V
  Title
Neutrophil extracellular traps in immunity and disease.
  Journal
Nat Rev Immunol 18:134-147 (2018)
DOI:10.1038/nri.2017.105
Reference
  Authors
Liu FC, Chuang YH, Tsai YF, Yu HP
  Title
Role of neutrophil extracellular traps following injury.
  Journal
Shock 41:491-8 (2014)
DOI:10.1097/SHK.0000000000000146
Reference
  Authors
Yang H, Biermann MH, Brauner JM, Liu Y, Zhao Y, Herrmann M
  Title
New Insights into Neutrophil Extracellular Traps: Mechanisms of Formation and Role in Inflammation.
  Journal
Front Immunol 7:302 (2016)
DOI:10.3389/fimmu.2016.00302
Reference
  Authors
Zawrotniak M, Bochenska O, Karkowska-Kuleta J, Seweryn-Ozog K, Aoki W, Ueda M, Kozik A, Rapala-Kozik M
  Title
Aspartic Proteases and Major Cell Wall Components in Candida albicans Trigger the Release of Neutrophil Extracellular Traps.
  Journal
Front Cell Infect Microbiol 7:414 (2017)
DOI:10.3389/fcimb.2017.00414
Reference
  Authors
Honda M, Kubes P
  Title
Neutrophils and neutrophil extracellular traps in the liver and gastrointestinal system.
  Journal
Nat Rev Gastroenterol Hepatol 15:206-221 (2018)
DOI:10.1038/nrgastro.2017.183
Reference
  Authors
Hamam HJ, Palaniyar N
  Title
Post-Translational Modifications in NETosis and NETs-Mediated Diseases.
  Journal
Biomolecules 9:E369 (2019)
DOI:10.3390/biom9080369
Reference
  Authors
Burgener SS, Schroder K
  Title
Neutrophil Extracellular Traps in Host Defense.
  Journal
Cold Spring Harb Perspect Biol 12:a037028 (2020)
DOI:10.1101/cshperspect.a037028
Reference
  Authors
Vorobjeva NV, Chernyak BV
  Title
NETosis: Molecular Mechanisms, Role in Physiology and Pathology.
  Journal
Biochemistry (Mosc) 85:1178-1190 (2020)
DOI:10.1134/S0006297920100065
Reference
  Authors
Ravindran M, Khan MA, Palaniyar N
  Title
Neutrophil Extracellular Trap Formation: Physiology, Pathology, and Pharmacology.
  Journal
Biomolecules 9:E365 (2019)
DOI:10.3390/biom9080365
Reference
  Authors
Jorch SK, Kubes P
  Title
An emerging role for neutrophil extracellular traps in noninfectious disease.
  Journal
Nat Med 23:279-287 (2017)
DOI:10.1038/nm.4294
Reference
  Authors
Goggs R, Jeffery U, LeVine DN, Li RHL
  Title
Neutrophil-Extracellular Traps, Cell-Free DNA, and Immunothrombosis in Companion Animals: A Review.
  Journal
Vet Pathol 57:6-23 (2020)
DOI:10.1177/0300985819861721
Reference
  Authors
Kim SJ, Jenne CN
  Title
Role of platelets in neutrophil extracellular trap (NET) production and tissue injury.
  Journal
Semin Immunol 28:546-554 (2016)
DOI:10.1016/j.smim.2016.10.013
Reference
  Authors
de Bont CM, Boelens WC, Pruijn GJM
  Title
NETosis, complement, and coagulation: a triangular relationship.
  Journal
Cell Mol Immunol 16:19-27 (2019)
DOI:10.1038/s41423-018-0024-0
Reference
  Authors
Zawrotniak M, Bartnicka D, Rapala-Kozik M
  Title
UVA and UVB radiation induce the formation of neutrophil extracellular traps by human polymorphonuclear cells.
  Journal
J Photochem Photobiol B 196:111511 (2019)
DOI:10.1016/j.jphotobiol.2019.111511
Reference
  Authors
Remijsen Q, Kuijpers TW, Wirawan E, Lippens S, Vandenabeele P, Vanden Berghe T
  Title
Dying for a cause: NETosis, mechanisms behind an antimicrobial cell death modality.
  Journal
Cell Death Differ 18:581-8 (2011)
DOI:10.1038/cdd.2011.1
Reference
  Authors
Zawrotniak M, Rapala-Kozik M
  Title
Neutrophil extracellular traps (NETs) - formation and implications.
  Journal
Acta Biochim Pol 60:277-84 (2013)
Reference
  Authors
Rosales C
  Title
Fcgamma Receptor Heterogeneity in Leukocyte Functional Responses.
  Journal
Front Immunol 8:280 (2017)
DOI:10.3389/fimmu.2017.00280
Reference
  Authors
Vorobjeva NV, Pinegin BV
  Title
Neutrophil extracellular traps: mechanisms of formation and role in health and disease.
  Journal
Biochemistry (Mosc) 79:1286-96 (2014)
DOI:10.1134/S0006297914120025
Reference
  Authors
Delgado-Rizo V, Martinez-Guzman MA, Iniguez-Gutierrez L, Garcia-Orozco A, Alvarado-Navarro A, Fafutis-Morris M
  Title
Neutrophil Extracellular Traps and Its Implications in Inflammation: An Overview.
  Journal
Front Immunol 8:81 (2017)
DOI:10.3389/fimmu.2017.00081
Reference
  Authors
Fonseca Z, Diaz-Godinez C, Mora N, Aleman OR, Uribe-Querol E, Carrero JC, Rosales C
  Title
Entamoeba histolytica Induce Signaling via Raf/MEK/ERK for Neutrophil Extracellular Trap (NET) Formation.
  Journal
Front Cell Infect Microbiol 8:226 (2018)
DOI:10.3389/fcimb.2018.00226
Reference
  Authors
Agraz-Cibrian JM, Giraldo DM, Mary FM, Urcuqui-Inchima S
  Title
Understanding the molecular mechanisms of NETs and their role in antiviral innate immunity.
  Journal
Virus Res 228:124-133 (2017)
DOI:10.1016/j.virusres.2016.11.033
Reference
  Authors
Schonrich G, Raftery MJ
  Title
Neutrophil Extracellular Traps Go Viral.
  Journal
Front Immunol 7:366 (2016)
DOI:10.3389/fimmu.2016.00366
Reference
  Authors
Saitoh T, Komano J, Saitoh Y, Misawa T, Takahama M, Kozaki T, Uehata T, Iwasaki H, Omori H, Yamaoka S, Yamamoto N, Akira S
  Title
Neutrophil extracellular traps mediate a host defense response to human immunodeficiency virus-1.
  Journal
Cell Host Microbe 12:109-16 (2012)
DOI:10.1016/j.chom.2012.05.015
Reference
  Authors
Kumar S, Gupta E, Kaushik S, Jyoti A
  Title
Neutrophil Extracellular Traps: Formation and Involvement in Disease Progression.
  Journal
Iran J Allergy Asthma Immunol 17:208-220 (2018)
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