Hsp70 chaperone dynamics and molecular mechanism
The chaperone functions of heat shock protein (Hsp)70 involve an allosteric control mechanism between the nucleotide-binding domain (NBD) and polypeptide substrate-binding domain (SBD): ATP binding and hydrolysis regulates the affinity for polypeptides, and polypeptide binding accelerates ATP hydrol...
Gespeichert in:
| 1. Verfasser: | |
|---|---|
| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
5 September 2013
|
| In: |
Trends in biochemical sciences
Year: 2013, Jahrgang: 38, Heft: 10, Pages: 507-514 |
| ISSN: | 1362-4326 |
| DOI: | 10.1016/j.tibs.2013.08.001 |
| Online-Zugang: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1016/j.tibs.2013.08.001 Verlag, lizenzpflichtig, Volltext: https://www.sciencedirect.com/science/article/pii/S0968000413001321 
|
| Verfasserangaben: | Matthias P. Mayer |
MARC
| LEADER | 00000caa a2200000 c 4500 | ||
|---|---|---|---|
| 001 | 1762346842 | ||
| 003 | DE-627 | ||
| 005 | 20220820012915.0 | ||
| 007 | cr uuu---uuuuu | ||
| 008 | 210707s2013 xx |||||o 00| ||eng c | ||
| 024 | 7 | |a 10.1016/j.tibs.2013.08.001 |2 doi | |
| 035 | |a (DE-627)1762346842 | ||
| 035 | |a (DE-599)KXP1762346842 | ||
| 035 | |a (OCoLC)1341418114 | ||
| 040 | |a DE-627 |b ger |c DE-627 |e rda | ||
| 041 | |a eng | ||
| 084 | |a 30 |2 sdnb | ||
| 100 | 1 | |a Mayer, Matthias P. |d 1960- |e VerfasserIn |0 (DE-588)1060239752 |0 (DE-627)799340510 |0 (DE-576)167058827 |4 aut | |
| 245 | 1 | 0 | |a Hsp70 chaperone dynamics and molecular mechanism |c Matthias P. Mayer |
| 264 | 1 | |c 5 September 2013 | |
| 300 | |a 8 | ||
| 336 | |a Text |b txt |2 rdacontent | ||
| 337 | |a Computermedien |b c |2 rdamedia | ||
| 338 | |a Online-Ressource |b cr |2 rdacarrier | ||
| 500 | |a Gesehen am 07.07.2021 | ||
| 520 | |a The chaperone functions of heat shock protein (Hsp)70 involve an allosteric control mechanism between the nucleotide-binding domain (NBD) and polypeptide substrate-binding domain (SBD): ATP binding and hydrolysis regulates the affinity for polypeptides, and polypeptide binding accelerates ATP hydrolysis. These data suggest that Hsp70s exist in at least two conformational states. Although structural information on the conformation with high affinity for polypeptides has been available for several years, the conformation with an open polypeptide binding cleft was elucidated only recently. In addition, other biophysical studies have revealed a more dynamic picture of Hsp70s, shedding light on the molecular mechanism by which Hsp70s assist protein folding. In this review recent insights into the structure and mechanism of Hsp70s are discussed. | ||
| 650 | 4 | |a allostery | |
| 650 | 4 | |a chaperone | |
| 650 | 4 | |a Hsp70 mechanism | |
| 650 | 4 | |a Hsp70 structure | |
| 650 | 4 | |a protein folding | |
| 773 | 0 | 8 | |i Enthalten in |t Trends in biochemical sciences |d Amsterdam [u.a.] : Elsevier Science, 1976 |g 38(2013), 10 vom: Okt., Seite 507-514 |h Online-Ressource |w (DE-627)306593068 |w (DE-600)1498901-3 |w (DE-576)094113513 |x 1362-4326 |7 nnas |a Hsp70 chaperone dynamics and molecular mechanism |
| 773 | 1 | 8 | |g volume:38 |g year:2013 |g number:10 |g month:10 |g pages:507-514 |g extent:8 |a Hsp70 chaperone dynamics and molecular mechanism |
| 856 | 4 | 0 | |u https://doi.org/10.1016/j.tibs.2013.08.001 |x Verlag |x Resolving-System |z lizenzpflichtig |3 Volltext |
| 856 | 4 | 0 | |u https://www.sciencedirect.com/science/article/pii/S0968000413001321 |x Verlag |z lizenzpflichtig |3 Volltext |
| 951 | |a AR | ||
| 992 | |a 20210707 | ||
| 993 | |a Article | ||
| 994 | |a 2013 | ||
| 998 | |g 1060239752 |a Mayer, Matthias P. |m 1060239752:Mayer, Matthias P. |d 700000 |d 706000 |e 700000PM1060239752 |e 706000PM1060239752 |k 0/700000/ |k 1/700000/706000/ |p 1 |x j |y j | ||
| 999 | |a KXP-PPN1762346842 |e 394647022X | ||
| BIB | |a Y | ||
| SER | |a journal | ||
| JSO | |a {"relHost":[{"id":{"issn":["1362-4326"],"zdb":["1498901-3"],"eki":["306593068"]},"language":["eng"],"name":{"displayForm":["publ. by the International Union of Biochemistry and Molecular Biology and Elsevier Trends Journals"]},"recId":"306593068","pubHistory":["1.1976 -"],"note":["Gesehen am 28.05.20"],"origin":[{"publisherPlace":"Amsterdam [u.a.]","dateIssuedKey":"1976","publisher":"Elsevier Science","dateIssuedDisp":"1976-"}],"physDesc":[{"extent":"Online-Ressource"}],"disp":"Hsp70 chaperone dynamics and molecular mechanismTrends in biochemical sciences","part":{"issue":"10","volume":"38","extent":"8","text":"38(2013), 10 vom: Okt., Seite 507-514","year":"2013","pages":"507-514"},"title":[{"title_sort":"Trends in biochemical sciences","subtitle":"TIBS","title":"Trends in biochemical sciences"}],"type":{"media":"Online-Ressource","bibl":"periodical"},"titleAlt":[{"title":"TIBS"}],"corporate":[{"role":"isb","display":"International Union of Biochemistry and Molecular Biology"}]}],"recId":"1762346842","note":["Gesehen am 07.07.2021"],"origin":[{"dateIssuedDisp":"5 September 2013","dateIssuedKey":"2013"}],"id":{"eki":["1762346842"],"doi":["10.1016/j.tibs.2013.08.001"]},"physDesc":[{"extent":"8 S."}],"person":[{"role":"aut","display":"Mayer, Matthias P.","given":"Matthias P.","family":"Mayer"}],"title":[{"title":"Hsp70 chaperone dynamics and molecular mechanism","title_sort":"Hsp70 chaperone dynamics and molecular mechanism"}],"type":{"media":"Online-Ressource","bibl":"article-journal"},"language":["eng"],"name":{"displayForm":["Matthias P. Mayer"]}} | ||
| SRT | |a MAYERMATTHHSP70CHAPE5201 | ||