ライフサイエンスコーパス: quasi-equivalent

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1 s that may be distributed unevenly among the quasi-equivalent A, B, and C subunits.

2 at have been proposed to correspond to seven quasi-equivalent actin binding sites.

3 ich the 3'-end of the tRNA shuttles from one quasi-equivalent active site to another, demonstrate tha

4 orm of the S. shibatae enzyme might have two quasi-equivalent active sites, one adding CTP and the ot

5 gest conformational change when adopting the quasi-equivalent B conformation.

6 The method was applied to all quasi-equivalent capsid structures (T=3, 4, 7 and 13) in

7 in the solvent accessibilities of the seven quasi-equivalent capsid subunits, attributed to differen

8 It has a T = 4 quasi-equivalent capsid with a dramatic maturation pathw

9 r of the hexon and thus contains four unique quasi-equivalent coat protein conformations that are the

10 mation of the FG loop, the site of the major quasi-equivalent conformational change.

11 We showed previously that such quasi-equivalent conformers of RNA bacteriophage MS2 coa

12 The FG-loops define the quasi-equivalent conformers of the coat protein subunit

13 f programmed primary structures derived from quasi-equivalent constitutional isomeric libraries of se

14 Structurally, the two DEDs in caspase-8 use quasi-equivalent contacts to enable assembly.

15 h that cradles two c-di-AMP molecules making quasi-equivalent contacts with the riboswitch.

16 emble, using both the classical mechanism of quasi-equivalent contacts, which are achieved through tr

17 nequivalent environments, in contrast to the quasi-equivalent CP environments throughout the 180-subu

18 Our studies show that quasi-equivalent CTDs exhibit different rates of exposur

19 ion, implying that they closely resemble the quasi-equivalent dimers (A/B and C/C) seen in the final

20 V) was clearly reflected in high Q-scores of quasi-equivalent dimers.

21 bly mechanism, all DDs in the complex are in quasi-equivalent environments.

22 the periods tested (periods 1, 2, and 5) are quasi-equivalent for actin binding.

23 Quasi-equivalent generation of both the pentamer and hex

24 Differences in the T = 4 quasi-equivalent heterodimer components show their adapt

25 Assembly of the quasi-equivalent hexamers and pentamers requires remarka

26 subunits occupying different positions in a quasi-equivalent icosahedral capsid play different roles

27 this property may be key to the formation of quasi-equivalent interactions within hexamers and pentam

28 in a domain-swapped symmetric MV dimer via a quasi-equivalent interface compared with vinculin involv

29 t the proteins are arranged as dimers of 120 quasi-equivalent molecules, with each dimer extending be

30 Assembly of the quasi-equivalent oligomers requires remarkably subtle re

31 The (quasi-)equivalent organization of their protein building

32 ndent and occur at rates determined by their quasi-equivalent position in the capsid, explaining the

33 tric dimers, D(1)D(2) and D(3)D(4), in a non-quasi-equivalent structure.

34 of quasi-equivalence to account also for non-quasi-equivalent subunit arrangements in icosahedral vir

35 of one or more gene products and displaying quasi-equivalent subunit associations are discussed at t

36 cle surface, while identical polypeptides in quasi-equivalent subunits are produced later or are in p

37 or carrying out non-icosahedral averaging of quasi-equivalent subunits during three-dimensional struc

38 s of allosteric communication among the four quasi-equivalent subunits in the icosahedral asymmetric

39 interfaces in icosahedral virus capsids with quasi-equivalent surface lattices.

40 viral capsids comprising different sizes and quasi-equivalent symmetries by performing normal mode an

41 ve zero readily identify interfaces that are quasi-equivalent to each other.

42 DNA-DNA interfaces by interactions that are "quasi-equivalent" to those in the tetramer, analogous to

43 psid shell are present under four of the six quasi-equivalent triplex positions.

44 ults indicate that the amino termini of both quasi-equivalent VP2 molecules are located near the icos

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