ライフサイエンスコーパス: cpn10

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1 uman mitochondrial co-chaperonin protein 10 (cpn10).

2 C-terminal extension not found in any other cpn10.

3 th bacterial, mitochondrial, and chloroplast cpn10.

4 cooperative reaction that is potentiated by cpn10.

5 14-mers is only efficient with mitochondrial cpn10.

6 OH additions promptly unfold and precipitate cpn10.

7 ike protein HU form B, the 10 kDa chaperonin Cpn10, and the 50S ribosomal protein L24.

8 ist protein folding, their specificities for cpn10 are entirely different.

9 For cpn10, both MeOH and TFE additions govern initial unfold

10 Formation of heptamer Cpn10/Cpn20 hetero-oligomers was also observed with the

11 he E. coli GroEL previously known, models of cpn10:cpn60 and GroEL:GroES complexes are proposed.

12 In contrast, the GroES homolog, yeast cpn10, does give a stable derivative.

13 a domain and cpn20 and cpn23 encoding tandem cpn10 domains.

14 hree genes encode chaperonin cofactors, with cpn10 encoding a single approximately 10-kDa domain and

15 assembly experiments of chemically denatured cpn10 from Homo sapiens (hmcpn10) and Aquifex aeolicus (

16 Cpn10 from the deep-branching, hyperthermophilic bacteri

17 The cpn10 from the hyperthermophilic, ancient bacterium Aqui

18 or the heptameric co-chaperonin proteins 10 (cpn10) from Aquifex aeolicus (Aacpn10-del25) and human m

19 Co-chaperonin protein 10 (cpn10, GroES in Escherichia coli) is a ring-shaped hepta

20 the unique binary chloroplast chaperonin 10 (cpn10) have not been elucidated.

21 With the structure of a cpn10 heptamer now revealed and the structure of the E.

22 The architecture of the Ml-cpn10 heptamer resembles a dome with an oculus in its ro

23 of the heptameric co-chaperonin protein 10 (cpn10) in vitro.

24 The structure of cpn10 is conserved throughout nature: seven beta-barrel

25 s suggests that the binding of substrates to cpn10 is possible in the absence of cpn60.

26 rystal structure of the Mycobacterium leprae cpn10 (Ml-cpn10) oligomer has been elucidated at a resol

27 All known cochaperonin protein 10 (cpn10) molecules are heptamers of seven identical subuni

28 Tetradecameric cpn10(Mt) has also been observed in solution by dynamic

29 Two dome-shaped cpn10(Mt) heptamers complex through loops at their bases

30 Through its base loop sequence cpn10(Mt) is known to be the agent in the bacterium resp

31 Superimposition of the cpn10(Mt) sequences 26 to 32 and 66 to 72 and E. coli Gr

32 of Mycobacterium tuberculosis chaperonin 10 (cpn10(Mt)) has been determined to a resolution of 2.8 A.

33 ucture of the Mycobacterium leprae cpn10 (Ml-cpn10) oligomer has been elucidated at a resolution of 3

34 nsion in each monomer not found in any other cpn10 protein.

35 Members of the chaperonin-10 (cpn10) protein family, also called heat shock protein 10

36 d close to reported midpoints for mesophilic cpn10 proteins.

37 Both VlsE's and cpn10's non-native structures exhibit high stability tow

38 ology with mesophilic and other thermophilic cpn10 sequences, except for a 25-residue C-terminal exte

39 acid sequences of GroEL1 (cpn60) and GroES1 (cpn10) were in agreement with N-terminal sequences previ

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