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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.                                          
  
  
  
    12 ter coexpression in HEK293T cells, they form homomultimers and heteromultimers, as shown by coimmunop
    13  transformation, whereas its ability to form homomultimers and interact with the host cell H2A histon
    14 ximal open probabilities (Po) of Kv7.2-Kv7.4 homomultimers and of Kv7.2/7.3 heteromultimers were foun
    15  to bind to Crm1 and to RNA but also to form homomultimers and shuttle between nucleus and cytoplasm.
  
  
  
  
    20  showed that CsmA forms dimers, trimers, and homomultimers as large as dodecamers and that CsmA direc
  
    22 on spectroscopy reveal that hNETs, which are homomultimers, bind one substrate molecule per transport
    23 nstructural protein NSP2 self-assembles into homomultimers, binds single-stranded RNA nonspecifically
  
  
  
  
    28  monomer but rather was present as an 8S-10S homomultimer consisting of 6 +/- 2 subunits of recombina
    29 ies support a model in which VirB4 dimers or homomultimers contribute structural information for the 
    30 hat enhance channel activity and that Kir3.4 homomultimers do not contribute significantly to the mus
  
  
  
    34 tertiary structure of VirE2 is important for homomultimer formation whereas a central domain mediates
    35  Kir3.1 and Kir3.4 subunits, although Kir3.4 homomultimers have also been proposed to contribute to t
    36 xplains the ability of ISA1 to function as a homomultimer in maize leaves, in contrast to other speci
    37 re intermediate between wild-type and mutant homomultimers in agonist efficacy and apparent affinity 
  
    39 ion, unlike AtxA1, AtxA2 did not form stable homomultimers in vitro, although AtxA1 and AtxA2 formed 
    40 e studies establish that VirB11 assembles as homomultimers in vivo via domains residing in each half 
    41 hese results indicate that myocilin can form homomultimers in vivo, independent of the olfactomedin-l
  
    43 ulates currents from KCNQ3, KCNQ4, and KCNQ5 homomultimers, KCNQ2/3 heteromultimers and native M curr
  
    45 ptor in Jurkat lymphocytes is comprised of a homomultimer of K(V)1.3, unlike the heteromultimeric arr
  
  
  
  
  
  
    52 pparent affinities 3-fold lower than alphawt homomultimers, suggesting a channel with two alphawt and
    53   DEG/ENaC subunits associate as hetero- and homomultimers to generate channels; however the stoichio
    54 irus was previously shown to assemble into a homomultimer upon phosphorylation by casein kinase II.  
    55 annel activity resembling recombinant Kir3.4 homomultimers was observed in 40% of the cell-attached p
    56 evidence suggests that Orai1 can assemble as homomultimers, whether this assembly is necessary for th
    57 iochemical analysis revealed that OeGLU is a homomultimer with high Mr In silico prediction modeling 
    58  additional beta-subunit(s) to form either a homomultimer with Kvbeta2 or a heteromultimer with Kvbet
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