Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.6.1.3 (ATPase)
 65,361 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

With regards to the applications of three Chinese herbs poria, rhizoma atractylodis macrocephalae, and radix angelicae sinensis to vascular dementia (VD), the work was performed to assess the nootropic action and explore neuroprotective mechanisms of three herbs combinations (FBD) on mice injured by cerebral repetitive ischemia-reperfusion (IR). Aqueous extracts from FBD (115-460 mg/kg) administered p.o. significantly improved cognitive function through elongating latency and reducing number of errors in step-through test. Aqueous extracts from FBD inhibited lipid peroxidation (LPO), elevated activity in (Na+)-(K+)-ATPase and (Ca2+)-ATPase, reduced the production of nitric oxide (NO) in cortical tissue after IR, and artificial cerebrospinal fluid (ACSF) containing aqueous extracts from FBD (ACSF-FBD) (0.01-10 mg/L) protected also primary cortical cortex neurons (PCCN) from hypoxic and excitotoxic insult induced by sodium dithionite (1 mM) and monosodium glutamate (MSG) (0.5 mM) in vitro. Multiple anti-IR properties contributed probably FBD to ameliorate cognitive dysfunction shown in this murine model for VD.
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PMID:Protective effects of FBD--an experimental Chinese traditional medicinal formula on memory dysfunction in mice induced by cerebral ischemia-reperfusion. 1574 Aug 83

The essential eukaryotic molecular chaperone Hsp90 operates with the help of different co-chaperones, which regulate its ATPase activity and serve as adaptors to recruit client proteins and other molecular chaperones, such as Hsp70, to the Hsp90 complex. Several Hsp90 and Hsp70 co-chaperones contain the tetratricopeptide repeat (TPR) domain, which interacts with the highly conserved EEVD motif at the C-terminal ends of Hsp90 and Hsp70. The acidic side chains in EEVD interact with a subset of basic residues in the TPR binding pocket called a 'carboxylate clamp'. Since the carboxylate clamp residues are conserved in the TPR domains of known Hsp90/Hsp70 co-chaperones, we carried out an in silico search for TPR proteins in Arabidopsis and rice comprising of at least one three-motif TPR domain with conserved amino acid residues required for Hsp90/Hsp70 binding. This approach identified in Arabidopsis a total of 36 carboxylate clamp (CC)-TPR proteins, including 24 novel proteins, with potential to interact with Hsp90/Hsp70. The newly identified CC-TPR proteins in Arabidopsis and rice contain additional protein domains such as ankyrin, SET, octicosapeptide/Phox/Bem1p (Phox/PB1), DnaJ-like, thioredoxin, FBD and F-box, and protein kinase and U-box, indicating varied functions for these proteins. To provide proof-of-concept of the newly identified CC-TPR proteins for interaction with Hsp90, we demonstrated interaction of AtTPR1 and AtTPR2 with AtHsp90 in yeast two-hybrid and in vitro pull down assays. These findings indicate that the in silico approach used here successfully identified in a genome-wide context CC-TPR proteins with potential to interact with Hsp90/Hsp70, and further suggest that the Hsp90/Hsp70 system relies on TPR co-chaperones more than it was previously realized.
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PMID:In silico identification of carboxylate clamp type tetratricopeptide repeat proteins in Arabidopsis and rice as putative co-chaperones of Hsp90/Hsp70. 2085 8