ライフサイエンスコーパス: homooligomer

1 iation dependent on the length of the target homooligomer.

2 d) and free energy of association to the Vpu homooligomer.

3 ediate or disrupt the formation of different homooligomers.

4 e formation of CotE multimers, most probably homooligomers.

5 increasing binding affinity to nucleic acid homooligomers (A approximately C < U < G approximately I

6 tested with several protein complex systems (homooligomers, a heterooligomer, and a protein-ligand co

7 nin subunits, which form biologically active homooligomers, also promote the disassembly of MCC.

8 Nercc1 exists as a homooligomer and can autoactivate in vitro by autophosph

9 tive C. thermocellum cellulosome exists as a homooligomer and the high-affinity interaction of BglA-C

10 sembly of an RNP composed of the Rev protein homooligomer and the Rev response element (RRE) RNA to m

11 profile that was consistent with assembly of homooligomers and bound the glutamate receptor agonist a

12 diate the formation of glycosyltransferases' homooligomers and directly contribute to the specific bi

13 h abundant evidence suggests that MDM2 forms homooligomers and heterooligomers with MDMX, the functio

14 protein binding modes from nine families of homooligomers and mapped 60 different binding modes and

15 Complementary short-strand DNA homooligomers and methylthiourea-linked homonucleosides

16 cipitation analyses suggest that hVam6p is a homooligomer, and that its self-assembly is mediated by

17 We hypothesize that AtpZ and AtpI, as homooligomers, and perhaps as heterooligomers, are Mg2+

18 leads to a model in which Vpu monomers, Vpu homooligomers, and Vpu-target heterooligomers coexist, a

19 ur analyses reveal that disulfide-linked Vp1 homooligomers are present in the simian virus 40-infecte

20 ily exchanged subunits with alphaBDelta54-61 homooligomers at 37 degrees C, forming heterooligomers w

21 modified submonomer protocol, we synthesized homooligomers at sequence lengths of up to 12-mer and al

22 ng recombinant LICs, we found that they form homooligomers, but not heterooligomers, and exhibit mutu

23 B isoform exists primarily as a cell-surface homooligomer composed of disulfide-linked, multidomain b

24 alysis for the triplexes of short-strand DNA homooligomers [d(pA)10-d(pA)23] and poly(dA) with the me

25 The CDCs form large homooligomers (estimated to be comprised of up to 50 CDC

26 residues are destabilizing, some stabilized homooligomer formation.

27 it of the ATR kinase and ATR itself exist as homooligomers in cells.

28 helices are also able to form homodimers or homooligomers in micelles and bacterial membranes.

29 formational change enabling formation of Bax homooligomers in mitochondrial membranes.

30 We performed a large-scale study of protein homooligomers in terms of their symmetry, interface size

31 ere, we demonstrate that the Mcl-1 TMD forms homooligomers in the mitochondrial membrane, competes wi

32 ting that RRE binding drives assembly of Rev homooligomers into asymmetric particles, reminiscent of

33 n the distribution of symmetry in primordial homooligomers modeled as randomly interacting pairs of m

34 Homooligomers of 6HalphaA (750 kDa) readily exchanged su

35 These studies confirm expression of nAChR as homooligomers of human alpha7 subunits from transgenes,

36 Homooligomers of meprin alpha are secreted; oligomers co

37 estrictions induced by a four-membered ring, homooligomers of the cyclic alpha-hydrazino acid (R)-N-a

38 properties derives primarily from studies of homooligomers of the original hERG 1a isolate.

39 condary structure of the corresponding tACBC homooligomers of the same length.

40 replacing the N- and C-terminal residues of homooligomers of trans-2-aminocyclobutanecarboxylic acid

41 ides have previously been reported, both for homooligomers of trans-2-aminocyclopentanecarboxylic aci

42 Many proteins exist naturally as symmetrical homooligomers or homopolymers(1).

43 sis showed that the P protein forms a stable homooligomer (perhaps a trimer) that is present in L-P a

44 rotein interactions, the assembly process of homooligomers plays a fundamental role because the major

45 hat hOAT1 exists in the plasma membrane as a homooligomer, possibly trimer, and higher order of oligo

46 2 exists both as a monomer (BRF-2M) and as a homooligomer, probably a homodimer (BRF-2D), in solution

47 secondary structure of organosoluble peptoid homooligomers ranging from 3 to 20 (R)-N-(1-phenylethyl)

48 nent of the toxin assembles into ring-shaped homooligomers that bind the two other enzyme components

49 It has been proposed that SERCA forms homooligomers that increase the catalytic rate of calciu

50 elerated assembly of the protein into stable homooligomers that resemble mature, native PLP.

51 r basal conditions, and PEDF dissociates the homooligomer to activate the receptors.

52 experiments suggest that PEDF receptors form homooligomers under basal conditions, and PEDF dissociat

53 The thermal stabilities of nine candidate homooligomers were assessed; six unfolded cooperatively

54 ing cells, forms misfolded, disulfide-linked homooligomers when translated alone.

55 recognition are elucidated by the studies of homooligomers which in turn mediate and regulate gene ex

56 oss-linked into homodimers, heterodimers and homooligomers with 1-ethyl-3-(3-dimethylaminopropyl)carb

57 The synthesis of peptoid homooligomers with four or eight pendant 1,2,3-triazoliu

58 These three protein types form cyclic homooligomers with pores at the center of symmetry that

59 ontext of the wider landscape of intertwined homooligomers, with a particular focus on the mechanisti

60 nts and conditions destabilizing ecto-ATPase homooligomers would inhibit the ecto-ATPase.