Relation Results

Summary

Name Tubulin
Primary ID SIGNOR-PF46
Type protein family
Formed by TUBA1A, TUBA1B, TUBA1C, TUBA3C, TUBA3D, TUBA3E, TUBA4A, TUBA8, TUBB, TUBB1, TUBB2B, TUBB3, TUBB4A, TUBB4B, TUBB6, TUBB8, TUBG1
Relations 18

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Type: Score: Layout: SPV 
0.20.80.20.20.20.70.80.80.20.20.20.80.20.80.20.80.20.2TBCATubulincabazitaxelGNAO1GNAI1NUMA1Microtubule_polimerizationpaclitaxelVincristine sulfateCEP135TTLCalprotectin complexvincaleukoblastine sulfateTRiCeribulin mesylateS100A9ixabepiloneS100A8GNAS

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Relations
Regulator
Mechanism
target
score ℹ
+ TBCAup-regulates quantity by stabilization img/direct-activation.png binding Tubulin 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-261169 Homo sapiens
pmid sentence
These intermediates interact with a series of five tubulin-specific chaperones (termed TBCA-E); these function together as a nanomachine that assembles the α/β tubulin heterodimer
Publications: 1 Organism: Homo Sapiens
+ cabazitaxeldown-regulates activity img/direct_inhibition.png chemical inhibition Tubulin 0.8
Identifier Residue Sequence Organism Cell Line
SIGNOR-259445 Homo sapiens
pmid sentence
Among these, larotaxel (XRP9881, formerly RPR109881A)[3,4] and cabazitaxel (XRP6258, TXD258, RPR116258A)[5] share a mechanism of action unique to taxanes, promoting tubulin assembly and stabilizing microtubules against cold-induced depolymerization
Publications: 1 Organism: Homo Sapiens
+ GNAO1up-regulates activity img/direct-activation.png binding Tubulin 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-256540 in vitro
pmid sentence
G protein alpha subunits Gi1alpha, Gsalpha, and Goalpha are shown to activate the GTPase activity of tubulin, inhibit microtubule assembly, and accelerate microtubule dynamics.
Publications: 1 Organism: In Vitro
+ GNAI1up-regulates activity img/direct-activation.png binding Tubulin 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-256538 in vitro
pmid sentence
G protein alpha subunits Gi1alpha, Gsalpha, and Goalpha are shown to activate the GTPase activity of tubulin, inhibit microtubule assembly, and accelerate microtubule dynamics.
Publications: 1 Organism: In Vitro
+ NUMA1up-regulates img/direct-activation.png binding Tubulin 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-256541 Homo sapiens
pmid sentence
Direct binding of numa to tubulin is mediated by a novel sequence motif in the tail domain that bundles and stabilizes microtubules.
Publications: 1 Organism: Homo Sapiens
+ Tubulinup-regulates img/indirect-activation.png Microtubule_polimerization 0.7
Identifier Residue Sequence Organism Cell Line
SIGNOR-266827 Homo sapiens
pmid sentence
Microtubules are essential for the generation, migration and differentiation of neurons. Within dendrites microtubules have also been implicated in the formation and plasticity of spines. For instance, the treatment of hippocampal neurons with low doses of the microtubule destabilizing drug Nocodazole impairs BDNF induced dendritic spine formation
Publications: 1 Organism: Homo Sapiens
+ paclitaxeldown-regulates activity img/direct_inhibition.png chemical inhibition Tubulin 0.8
Identifier Residue Sequence Organism Cell Line
SIGNOR-259449 Homo sapiens
pmid sentence
Here we integrate a computational model for microtubule assembly with nanometer-scale fluorescence microscopy measurements to identify the kinetic and thermodynamic basis of kinetic stabilization by the MTAs paclitaxel, an assembly promoter, and vinblastine, a disassembly promoter. We identify two distinct modes of kinetic stabilization in live cells, one that truly suppresses on-off kinetics, characteristic of vinblastine, and the other a "pseudo" kinetic stabilization, characteristic of paclitaxel, that nearly eliminates the energy difference between the GTP- and GDP-tubulin thermodynamic states. By either mechanism, the main effect of both MTAs is to effectively stabilize the microtubule against disassembly in the absence of a robust GTP cap.
Publications: 1 Organism: Homo Sapiens
+ Vincristine sulfatedown-regulates activity img/direct_inhibition.png chemical inhibition Tubulin 0.8
Identifier Residue Sequence Organism Cell Line
SIGNOR-259254 Homo sapiens
pmid sentence
Vincristine is commonly administered as an effective anti-brain tumor drug. Vincristine treatment also impaired the microtubule-associated protein tubulin, and fibronectin, and downregulated MMP10 activity.
Publications: 1 Organism: Homo Sapiens
Tissue: Brain
+ CEP135up-regulates activity img/direct-activation.png binding Tubulin 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-269678 in vitro
pmid sentence
Here, we analyzed in detail the microtubule-binding activity of human CEP135 (HsCEP135).  Biochemical, cryo-electron, and fluorescence microscopy analyses revealed that in vitro HsCEP135-N interacts with tubulin, protofilaments, and microtubules and induces the formation of microtubule bundles
Publications: 1 Organism: In Vitro
+ TTLdown-regulates img/direct_inhibition.png tyrosination Tubulin 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-266826 Homo sapiens
pmid sentence
Tubulin tyrosine ligase (ttl) adds a c-terminal tyr to __tubulin as part of a tyrosination/detyrosination cycle present in most eukaryotic cells. / ttl inhibits spontaneous tubulin polymerization
Publications: 1 Organism: Homo Sapiens
+ Calprotectin complexup-regulates quantity by stabilization img/direct-activation.png binding Tubulin 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-262827 Homo sapiens Monocyte
pmid sentence
Calcium-induced complexes of S100A8 and S100A9 have been shown to colocalize with microtubules (MTs) during activation of monocytes. Functional analyses demonstrated that the complexes are involved in cytoskeletal organization and that they directly bind to tubulin and promote tubulin polymerization in a calcium-dependent manner
Publications: 1 Organism: Homo Sapiens
+ vincaleukoblastine sulfatedown-regulates activity img/direct_inhibition.png chemical inhibition Tubulin 0.8
Identifier Residue Sequence Organism Cell Line
SIGNOR-259260 Homo sapiens
pmid sentence
Tubulin binding molecules have generated considerable interest after the successful introduction of the taxanes into clinical oncology and the widespread use of the vinca alkaloids vincristine and vinblastine. These compounds inhibit cell mitosis by binding to the protein tubulin in the mitotic spindle and preventing polymerization into the MTs.
Publications: 1 Organism: Homo Sapiens
+ TRiCup-regulates quantity by stabilization img/direct-activation.png binding Tubulin 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-272868 Homo sapiens
pmid sentence
Mammalian cells contain an evolutionarily conserved type II chaperonin called chaperonin containing tailless complex polypeptide 1 (CCT) or tailless complex polypeptide 1 ring complex (TRiC). The CCT complex is composed of eight subunits [CCT1-8 (yeast) or CCTα-θ (mammals)] and folds substrates needed for cell invasion and proliferation, such as actin, tubulin, and cell division cycle protein 20 homolog (cdc20), as well as oncoproteins like signal transducer and activator of transcription 3 (STAT3), Kirsten rat sarcoma viral oncogene homolog (KRAS), and Myelocytomatosis (MYC).
Publications: 1 Organism: Homo Sapiens
+ eribulin mesylatedown-regulates activity img/direct_inhibition.png chemical inhibition Tubulin 0.8
Identifier Residue Sequence Organism Cell Line
SIGNOR-259444 Homo sapiens
pmid sentence
The complex marine natural product halichondrin B was compared with NSC 707389 (E7389), a structurally simplified, synthetic macrocyclic ketone analog, which has been selected for clinical trials in human patients. NSC 707389 was invariably more potent than halichondrin B in its interactions with tubulin. Both compounds inhibited tubulin assembly, inhibited nucleotide exchange on beta-tubulin, and were noncompetitive inhibitors of the binding of radiolabeled vinblastine and dolastatin 10 to tubulin.
Publications: 1 Organism: Homo Sapiens
+ S100A9up-regulates quantity by stabilization img/direct-activation.png binding Tubulin 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-261936 Homo sapiens Monocyte
pmid sentence
Calcium-induced complexes of S100A8 and S100A9 have been shown to colocalize with microtubules (MTs) during activation of monocytes. Functional analyses demonstrated that the complexes are involved in cytoskeletal organization and that they directly bind to tubulin and promote tubulin polymerization in a calcium-dependent manner
Publications: 1 Organism: Homo Sapiens
+ ixabepilonedown-regulates activity img/direct_inhibition.png chemical inhibition Tubulin 0.8
Identifier Residue Sequence Organism Cell Line
SIGNOR-259450 Homo sapiens
pmid sentence
Ixabepilone, the first drug in a new class of microtubule-stabilizing agents called epothilones, offers a new treatment option for patients with metastatic or locally advanced breast cancer who are refractory to standard chemotherapy.
Publications: 1 Organism: Homo Sapiens
+ S100A8up-regulates quantity by stabilization img/direct-activation.png binding Tubulin 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-261937 Homo sapiens Monocyte
pmid sentence
Calcium-induced complexes of S100A8 and S100A9 have been shown to colocalize with microtubules (MTs) during activation of monocytes. Functional analyses demonstrated that the complexes are involved in cytoskeletal organization and that they directly bind to tubulin and promote tubulin polymerization in a calcium-dependent manner
Publications: 1 Organism: Homo Sapiens
+ GNASup-regulates activity img/direct-activation.png binding Tubulin 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-256539 in vitro
pmid sentence
G protein alpha subunits Gi1alpha, Gsalpha, and Goalpha are shown to activate the GTPase activity of tubulin, inhibit microtubule assembly, and accelerate microtubule dynamics.
Publications: 1 Organism: In Vitro
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