ライフサイエンスコーパス: assemblin

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1 nit can rescue activity of mutant simian CMV assemblin).

2 tion in each cleavage site (ICRMT-pPR and IC-assemblin).

3 similarity to the striated fiber protein SF-assemblin.

4 mated rates previously reported for purified assemblin.

5 proteolytic portion of the precursor, called assemblin.

6 ic characteristics that distinguish pPR from assemblin.

7 onal serine protease whose catalytic domain, assemblin (28 kDa), is released by self-cleavage from a

8 e structure and enzymatic characteristics of assemblin, a potential pharmacologic target, comparative

9 duction of >85% in the expression of CSP and assemblin and a reduction of 4000-fold in viral growth w

10 s), and dense bodies; (iii) established that assemblin and its cleavage products are present in NIEPs

11 suggesting that I-site cleavage destabilizes assemblin and its fragments, whereas C-site cleavage doe

12 de that although the enzymatic activities of assemblin and its precursor are comparable, there may be

13 al for the activity of two-chain recombinant assemblin, and (iii) the human CMV and simian CMV An and

14 cifically inhibits the expression of CSP and assemblin, and consequently blocks viral capsid formatio

15 cytomegalovirus (CMV) maturational protease, assemblin, contains an "internal" (I) cleavage site abse

16 RMT-pPR is 5- to 10-fold more efficient than assemblin for all cleavages measured (i.e., the M site o

17 cytomegalovirus with its proteolytic domain (assemblin) for the ability to cleave two biological subs

18 Cell-based cleavage assays of the two-chain assemblin formed from independently expressed An and Ac

19 cleavage frees the proteolytic amino domain, assemblin, from the nonproteolytic carboxyl domain of th

20 The 28-kDa CMV serine protease, assemblin, has a Ser-His-His catalytic triad and an inte

21 nterpart mutants of the human and simian CMV assemblin homologs and occurred in both living cells and

22 Two of these are common to the assemblin homologs of all herpes group viruses: one at t

23 ubstrates is similar to that of single-chain assemblin, (ii) R-site cleavage is not essential for the

24 I-site cleavage cuts assemblin in half without detected effect on its enzymat

25 te cleavage of assemblin nor the presence of assemblin in the mature virion.

26 eolytic cleavage at an internal site divides assemblin into an amino subunit (An) and a carboxyl subu

27 These results indicate that assemblin is able to form active multimeric structures t

28 The cytomegalovirus (CMV) serine proteinase assemblin is synthesized as a precursor that undergoes t

29 ndent clans of serine proteases, herpesvirus assemblin-like and ClpP-like.

30 are able to rescue the enzymatic activity of assemblin mutants.

31 ious CMV requires neither I-site cleavage of assemblin nor the presence of assemblin in the mature vi

32 I-site cleavage of the mutated assemblin occurred during complementation but was not ab

33 ive to chemical rescue in the context of the assemblin precursor, pUL80a.

34 tants were indistinguishable from that of IC-assemblin prepared in parallel for comparison, as determ

35 Parasite striated fiber assemblins (SFA) polymerize into a dynamic fiber that em

36 encode an essential serine proteinase called assemblin that is responsible for cleaving the precursor

37 her An or Ac) corresponding to the domain of assemblin that was mutated.

38 Ac do not require synthesis as single-chain assemblin to fold and associate correctly in these eukar

39 nt (point, deletion, and insertion) forms of assemblin together with the wild-type subunit (either An

40 In cytomegalovirus (CMV), assemblin undergoes autoproteolysis at an internal (I) s

41 d in human or insect cells, active two-chain assemblin was formed.

42 ns, the capsid scaffolding protein (CSP) and assemblin, which are essential for viral capsid formatio

43 ns, the capsid scaffolding protein (CSP) and assemblin, which are essential for viral capsid formatio

44 own by effective complementation of inactive assemblins with noncleavable I sites.

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