ライフサイエンスコーパス: group II chaperonin

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1 nalling, driving the conformational cycle of group II chaperonins.

2 the substrate during the nucleotide cycle of group II chaperonins.

3 Eukaryotes contain eight genes for group II chaperonins, all of which are essential, and it

4 This organism contains three genes for group II chaperonins, and we show that all are individua

5 Group II chaperonins are ATP-ases indispensable for the

6 Group II chaperonins are ATP-dependent ring-shaped compl

7 Group II chaperonins are essential mediators of cellular

8 Group II chaperonins are found in archaea and the cytopl

9 ectron microscopy, conformational changes in group II chaperonins are not well characterized.

10 completely distinct closing mechanism in the group II chaperonins as compared with the group I chaper

11 Group II chaperonins belong to the Hsp60 family occurrin

12 a, there are one, two or three genes for the group II chaperonins, but whether they are essential for

13 nal reconstruction and modeling of Mm-cpn, a group II chaperonin, determined to 4.3 A resolution.

14 Lys-161, which is extremely conserved among group II chaperonins, forms interactions with the gamma-

15 Group II chaperonins, found in archaea and eukaryotes, c

16 We propose that these group II chaperonins function as a structural element in

17 mic structure of the thermosome, an archaeal group II chaperonin, has been determined in a fully clos

18 conformations of the thermosome, an archaeal group II chaperonin, have been determined by cryo-electr

19 we describe the first crystal structure of a group II chaperonin in an open conformation.

20 (cryo-EM) structures of Mm-cpn, an archaeal group II chaperonin, in the nucleotide-free (open) and n

21 uction, we describe three conformations of a group II chaperonin, including an asymmetric, bullet-sha

22 We observed, however, that the group II chaperonins known as rosettasomes in the hypert

23 philic archaeon Sulfolobus shibatae contains group II chaperonins, known as rosettasomes, which are t

24 Group II chaperonins mediate protein folding in an ATP-d

25 A major recurring problem within group II chaperonin research, especially with the hetero

26 ort here that human erythrocytes contain the group II chaperonin T-complex polypeptide 1 (TCP-1) and

27 Some of these peptides were bound to the group II chaperonin TRiC and were protected from degrada

28 The eukaryotic group II chaperonin TRiC/CCT is a 16-subunit complex wit

29 how that an adenosine-5'-triphosphate-driven group II chaperonin, which resembles a barrel with a bui

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