7.4.2.3	medicine	import of the enteropathogenic Escherichia coli effector protein Map into mitochondria, which alters organelle morphology, is dependent on mtHsp70	672993	
7.4.2.3	medicine	in vivo binding of mortalin/mtHsp70 with HSP60, involvment in tumorigenesis, functional distinction in pathways involved in senescence	667512	
7.4.2.3	medicine	mtHsp70 forms complexes with wild-type DJ-1 and its mutants, DJ-1 is an oncogene and causative gene for familial form of the Parkinson's disease, translocation of DJ-1 to mitochondria after oxidative stress is carried out in association with chaperones like mtHsp70	673805	
7.4.2.3	additional information	mtHsp70 and Escherichia coli DnaK display different conformational and biochemical properties, chimeric Hsp70s can not complement DnaK function in vivo	668549	
7.4.2.3	additional information	Pam16 is selectively required for preprotein translocation into the matrix, but not for protein insertion into the inner membrane, Pam16 interacts with Pam18 and is needed for the association of Pam18 with the presequence translocase and for formation of a mtHsp70-Tim44 complex	676134	
7.4.2.3	additional information	Pam16's J-like domain strongly interacts with Pam18's J domain, leading to a productive interaction of Pam18 with mtHsp70 at the import channel	676773	
7.4.2.3	additional information	Pam16-Pam18 complex regulates the ATpase activity of mtHsp70, Pam17 is required for the correct organization of the Pam16-Pam18 complex and thus contributes to regulation of mtHsp70 activity	675964	
7.4.2.3	additional information	Tam41 faciliates mitochondrial protein import by maintaining the functional integrity of the TIM23 protein translocator complex, TIM44 provides an anchor for mtHsp70 to bind to the translocating polypeptide that emerges from the outlet of the TIM23 channel	675002	
7.4.2.3	additional information	the TIM23 complex is not a static complex but switches between TOM tethering and PAM binding, including the subunit mtHsp70, in a reaction cycle involving Tim21 and Tim17	672943	
7.4.2.3	additional information	Tim15/Zim17 cooperates with mtHsp70 to faciliate import of presequence-containing proteins into the matrix	-, 673628	
7.4.2.3	additional information	TIM44 binds to the peptide-binding domain of Hsp70 and thereby recruits it to the outlet of the translocation pore, so that mtHsp70 can bind to the incoming polypeptide chain as soon as it emerges from the channel	671931	
7.4.2.3	additional information	truncation of the N terminus of TIM17, a subunit of the TIM23 complex, severely diminishes mitochondrial import of preproteins, mitochondrial Hsp70 mediates the vectorial translocation of the preprotein into the matrix	-, 674522