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1 d) and free energy of association to the Vpu homooligomer.
2 iation dependent on the length of the target 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
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
16 cipitation analyses suggest that hVam6p is a homooligomer, and that its self-assembly is mediated by
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 ng recombinant LICs, we found that they form homooligomers, but not heterooligomers, and exhibit mutu
22 B isoform exists primarily as a cell-surface homooligomer composed of disulfide-linked, multidomain b
23 alysis for the triplexes of short-strand DNA homooligomers [d(pA)10-d(pA)23] and poly(dA) with the me
29 We performed a large-scale study of protein homooligomers in terms of their symmetry, interface size
30 ting that RRE binding drives assembly of Rev homooligomers into asymmetric particles, reminiscent of
31 n the distribution of symmetry in primordial homooligomers modeled as randomly interacting pairs of m
33 These studies confirm expression of nAChR as homooligomers of human alpha7 subunits from transgenes,
36 ides have previously been reported, both for homooligomers of trans-2-aminocyclopentanecarboxylic aci
37 sis showed that the P protein forms a stable homooligomer (perhaps a trimer) that is present in L-P a
38 rotein interactions, the assembly process of homooligomers plays a fundamental role because the major
39 hat hOAT1 exists in the plasma membrane as a homooligomer, possibly trimer, and higher order of oligo
40 2 exists both as a monomer (BRF-2M) and as a homooligomer, probably a homodimer (BRF-2D), in solution
41 secondary structure of organosoluble peptoid homooligomers ranging from 3 to 20 (R)-N-(1-phenylethyl)
42 nent of the toxin assembles into ring-shaped homooligomers that bind the two other enzyme components
46 experiments suggest that PEDF receptors form homooligomers under basal conditions, and PEDF dissociat
47 The thermal stabilities of nine candidate homooligomers were assessed; six unfolded cooperatively
49 recognition are elucidated by the studies of homooligomers which in turn mediate and regulate gene ex
50 oss-linked into homodimers, heterodimers and homooligomers with 1-ethyl-3-(3-dimethylaminopropyl)carb
52 ontext of the wider landscape of intertwined homooligomers, with a particular focus on the mechanisti
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