| + |
vincaleukoblastine sulfate | down-regulates activity 
chemical inhibition
|
Tubulin |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259260 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15579115 |
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 |
| + |
S100A8 | up-regulates quantity by stabilization 
binding
|
Tubulin |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261937 |
|
|
Homo sapiens |
Monocyte |
| pmid |
sentence |
| 16690079 |
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 |
| + |
Calprotectin complex | up-regulates quantity by stabilization
binding
|
Tubulin |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262827 |
|
|
Homo sapiens |
Monocyte |
| pmid |
sentence |
| 16690079 |
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 |
| + |
TRiC | up-regulates quantity by stabilization
binding
|
Tubulin |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272868 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 36185250 |
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 |
| + |
NUMA1 | up-regulates
binding
|
Tubulin |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256541 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11956313 |
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 |
| + |
eribulin mesylate | down-regulates activity
chemical inhibition
|
Tubulin |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259444 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16940412 |
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 |
| + |
Tubulin | up-regulates 
|
Microtubule_polimerization |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266827 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28347630 |
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 |
| + |
CEP135 | up-regulates activity
binding
|
Tubulin |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269678 |
|
|
in vitro |
|
| pmid |
sentence |
| 27477386 |
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 |
| + |
GNAS | up-regulates activity
binding
|
Tubulin |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256539 |
|
|
in vitro |
|
| pmid |
sentence |
| 10224115 |
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 |
| + |
GNAI1 | up-regulates activity
binding
|
Tubulin |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256538 |
|
|
in vitro |
|
| pmid |
sentence |
| 10224115 |
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 |
| + |
S100A9 | up-regulates quantity by stabilization
binding
|
Tubulin |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261936 |
|
|
Homo sapiens |
Monocyte |
| pmid |
sentence |
| 16690079 |
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 |
| + |
ixabepilone | down-regulates activity
chemical inhibition
|
Tubulin |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259450 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18945860 |
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 |
| + |
GNAO1 | up-regulates activity
binding
|
Tubulin |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256540 |
|
|
in vitro |
|
| pmid |
sentence |
| 10224115 |
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 |
| + |
TTL | down-regulates
tyrosination
|
Tubulin |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266826 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22020298 |
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 |
| + |
cabazitaxel | down-regulates activity
chemical inhibition
|
Tubulin |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259445 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21770474 |
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 |
| + |
TBCA | up-regulates quantity by stabilization
binding
|
Tubulin |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261169 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28158450 |
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 |
| + |
paclitaxel | down-regulates activity
chemical inhibition
|
Tubulin |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259449 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28298489 |
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 sulfate | down-regulates activity
chemical inhibition
|
Tubulin |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259254 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30599272 |
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 |
3.0
Tubulin