AAAAAA

   
Results: 1-8 |
Results: 8
Intracellular aggregation of polypeptides with expanded polyglutamine domain is stimulated by stress-activated kinase MEKK1
Authors: Meriin, AB Mabuchi, K Gabai, VL Yaglom, JA Kazantsev, A Sherman, MY
Citation: Ab. Meriin et al., Intracellular aggregation of polypeptides with expanded polyglutamine domain is stimulated by stress-activated kinase MEKK1, J CELL BIOL, 153(4), 2001, pp. 851-864
HSP72 can protect cells from heat-induced apoptosis by accelerating the inactivation of stress kinase JNK
Authors: Volloch, V Gabai, VL Rits, S Force, T Sherman, MY
Citation: V. Volloch et al., HSP72 can protect cells from heat-induced apoptosis by accelerating the inactivation of stress kinase JNK, CELL STR CH, 5(2), 2000, pp. 139-147
Hsp72-mediated suppression of c-Jun N-terminal kinase is implicated in development of tolerance to caspase-independent cell death
Authors: Gabai, VL Yaglom, JA Volloch, V Meriin, AB Force, T Koutroumanis, M Massie, B Mosser, DD Sherman, MY
Citation: Vl. Gabai et al., Hsp72-mediated suppression of c-Jun N-terminal kinase is implicated in development of tolerance to caspase-independent cell death, MOL CELL B, 20(18), 2000, pp. 6826-6836
Suppression of stress kinase JNK is involved in Hsp72-mediated protection of myogenic cells from transient energy deprivation - Hsp72 alleviates the stress-induced inhibition of JNK dephosphorylation
Authors: Gabai, VL Meriin, AB Yaglom, JA Wei, JY Mosser, DD Sherman, MY
Citation: Vl. Gabai et al., Suppression of stress kinase JNK is involved in Hsp72-mediated protection of myogenic cells from transient energy deprivation - Hsp72 alleviates the stress-induced inhibition of JNK dephosphorylation, J BIOL CHEM, 275(48), 2000, pp. 38088-38094
Protein-damaging stresses activate c-jun N-terminal kinase via inhibition of its dephosphorylation: a novel pathway controlled by HSP72 (vol 19, pg 2547, 1999)
Authors: Meriin, AB Yaglom, JA Gabai, VL Zon, L Ganiatsas, S Mosser, DD Sherman, MY
Citation: Ab. Meriin et al., Protein-damaging stresses activate c-jun N-terminal kinase via inhibition of its dephosphorylation: a novel pathway controlled by HSP72 (vol 19, pg 2547, 1999), MOL CELL B, 19(7), 1999, pp. 5235-5235
Protein-damaging stresses activate c-Jun N-terminal kinase via inhibition of its dephosphorylation: a novel pathway controlled by HSP72
Authors: Meriin, AB Yaglom, JA Gabai, VL Mosser, DD Zon, L Sherman, MY
Citation: Ab. Meriin et al., Protein-damaging stresses activate c-Jun N-terminal kinase via inhibition of its dephosphorylation: a novel pathway controlled by HSP72, MOL CELL B, 19(4), 1999, pp. 2547-2555
The function of HSP72 in suppression of c-Jun N-terminal kinase activationcan be dissociated from its role in prevention of protein damage
Authors: Yaglom, JA Gabai, VL Meriin, AB Mosser, DD Sherman, MY
Citation: Ja. Yaglom et al., The function of HSP72 in suppression of c-Jun N-terminal kinase activationcan be dissociated from its role in prevention of protein damage, J BIOL CHEM, 274(29), 1999, pp. 20223-20228
ATPase activity of the heat shock protein Hsp72 is dispensable for its effects on dephosphorylation of stress kinase JNK and on heat-induced apoptosis
Authors: Volloch, V Gabai, VL Rits, S Sherman, MY
Citation: V. Volloch et al., ATPase activity of the heat shock protein Hsp72 is dispensable for its effects on dephosphorylation of stress kinase JNK and on heat-induced apoptosis, FEBS LETTER, 461(1-2), 1999, pp. 73-76
Risultati: 1-8 |