Sentence examples for binding to the ATPases from inspiring English sources

Exact(1)

In fact, ATP binding to the ATPases by itself supports the rapid degradation of unfolded proteins.

Similar(59)

These data demonstrate that EGCG competes with ATP for binding to the ATPase domain of HSP70 and HSP90.

It was previously shown that EGCG antagonizes the function of the HSP70 family protein, Grp78, by directly competing with ATP for binding to the ATPase domain of Grp78 [ 14].

This also raises the question whether the effects of EGCG and HNK on intact cells result from binding to the ATPase domain and, if so, whether this occurs in mature ER-resident GRP78 as a result of conformational dynamics and intrinsic mobility of the ATPase domain, particularly the more-open conformational states that may interact with nucleotide exchange factors (Liu et al, 2010).

On the other hand, expression of an ATP7B segment (NMBD) including four copper-binding motifs protects bacterial cells from toxic effects of cisplatin, suggesting that cisplatin binding to the ATPase NMBD is involved and may be sufficient to produce drug resistance [ 69, 70].

First, our results show that CPV's ATPase activity and ATP binding to the putative ATPase sites are both SAM-dependent.

Although, BAG-2 has never been shown to be associated with p53, recent studies show that BAG -related proteins compete with Hip for binding to the Hsc70/Hsp70 ATPase domain and promote protein substrate release involving both the chaperoning, folding, and degradation of wild type and mutant p53 [25], [25].

Its structure is intrinsically disordered, but an α-helix is formed in PUP upon binding to the proteasomal ATPase subunit Mpa, revealing binding-induced folding.

The greater effectiveness of HNK at inducing ER stress was consistent with DSC data indicating greater efficacy of HNK for binding to the unfolded ATPase domain.

We provide evidence consistent with a mechanism of action for HNK that includes binding to the unfolded ATPase domain of GRP78 with a consequent induction of ER stress.

We show that rather than binding to the main ATPase site within dynein's AAA+ ring or its microtubule-binding stalk directly, Lis1 engages the interface between these elements.

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