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1 at the active form of BCRP is a homodimer or homomultimer.
2 , two ISA1/ISA2 heteromultimers and one ISA1 homomultimer.
3 higher affinity for ShK-Dap(22) than K(v)1.1 homomultimers.
4 urrent, but not currents from KCNQ1 or KCNQ2 homomultimers.
5 ractions required for assembly of productive homomultimers.
6 tion at Leu236 retained the capacity to form homomultimers.
7 stics distinct from those of TRP or TRP-like homomultimers.
8 and enhanced activity compared with that of homomultimers.
9 9% for homodimers and 17.0% for higher-order homomultimers.
13 ter coexpression in HEK293T cells, they form homomultimers and heteromultimers, as shown by coimmunop
14 transformation, whereas its ability to form homomultimers and interact with the host cell H2A histon
15 ximal open probabilities (Po) of Kv7.2-Kv7.4 homomultimers and of Kv7.2/7.3 heteromultimers were foun
16 to bind to Crm1 and to RNA but also to form homomultimers and shuttle between nucleus and cytoplasm.
18 of plastid-localized ZmPTOX1, existing as a homomultimer, and established its interaction with ferre
22 showed that CsmA forms dimers, trimers, and homomultimers as large as dodecamers and that CsmA direc
24 on spectroscopy reveal that hNETs, which are homomultimers, bind one substrate molecule per transport
25 nstructural protein NSP2 self-assembles into homomultimers, binds single-stranded RNA nonspecifically
30 monomer but rather was present as an 8S-10S homomultimer consisting of 6 +/- 2 subunits of recombina
31 sequence alignments of a monomer that forms homomultimers contain the co-evolutionary signals of bot
32 ies support a model in which VirB4 dimers or homomultimers contribute structural information for the
33 hat enhance channel activity and that Kir3.4 homomultimers do not contribute significantly to the mus
37 tertiary structure of VirE2 is important for homomultimer formation whereas a central domain mediates
38 Kir3.1 and Kir3.4 subunits, although Kir3.4 homomultimers have also been proposed to contribute to t
39 xplains the ability of ISA1 to function as a homomultimer in maize leaves, in contrast to other speci
40 re intermediate between wild-type and mutant homomultimers in agonist efficacy and apparent affinity
42 ion, unlike AtxA1, AtxA2 did not form stable homomultimers in vitro, although AtxA1 and AtxA2 formed
43 e studies establish that VirB11 assembles as homomultimers in vivo via domains residing in each half
44 hese results indicate that myocilin can form homomultimers in vivo, independent of the olfactomedin-l
46 ulates currents from KCNQ3, KCNQ4, and KCNQ5 homomultimers, KCNQ2/3 heteromultimers and native M curr
48 ptor in Jurkat lymphocytes is comprised of a homomultimer of K(V)1.3, unlike the heteromultimeric arr
55 pparent affinities 3-fold lower than alphawt homomultimers, suggesting a channel with two alphawt and
56 DEG/ENaC subunits associate as hetero- and homomultimers to generate channels; however the stoichio
57 irus was previously shown to assemble into a homomultimer upon phosphorylation by casein kinase II.
58 both intrachain and interchain contacts for homomultimers using multiple sequence alignment (MSA) an
59 annel activity resembling recombinant Kir3.4 homomultimers was observed in 40% of the cell-attached p
60 evidence suggests that Orai1 can assemble as homomultimers, whether this assembly is necessary for th
61 iochemical analysis revealed that OeGLU is a homomultimer with high Mr In silico prediction modeling
62 additional beta-subunit(s) to form either a homomultimer with Kvbeta2 or a heteromultimer with Kvbet