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1 apsid cores recognized by its C-terminal PRY/SPRY domain.
2 nd to MET tyrosine kinase domain through its SPRY domain.
3 9 and RanBP10, interact with MET through the SPRY domain.
4 he tyrosine kinase domain of MET through its SPRY domain.
5 expressed TbetaRII (and not TbetaRI) via its Spry domain.
6 2 and coiled-coil motifs) domain and a B30.2(SPRY) domain.
7 terminant of anti-HIV-1 potency is the B30.2(SPRY) domain.
8 coiled-coil domains, and a C-terminal B30.2 (SPRY) domain.
9 sts of RING, B-box 2, coiled-coil, and B30.2(SPRY) domains.
10 sts of RING, B-box 2, coiled-coil, and B30.2(SPRY) domains.
11 coiled-coil (CC), and, in some cases, B30.2(SPRY) domains.
12 sed of RING, B-box 2, coiled-coil, and B30.2(SPRY) domains.
16 through direct interactions mediated by the SPRY domain and demonstrate that these activities can be
17 incoming retroviruses via its C-terminal PRY/SPRY domain and rapidly recruits them to the proteasome
18 two fibronectin type III (FN3) repeats, and SPRY domains and interacts with the sarcomeric Z-disc pr
23 ger domain, a B box/coiled-coil domain and a SPRY domain, are involved in various cellular processes,
24 ce of the Ash2L SPIa and ryanodine receptor (SPRY) domain binds to a cluster of acidic residues, refe
25 -21R assembly did not require the C-terminal SPRY domain, but did require both protein dimerization a
26 with gain-of-function mutations in its B30.2/SPRY domain causes the autoinflammatory disease familial
27 ets comprised open hexameric rings, with the SPRY domains centered on the edges and the B-box and RIN
28 the v1 and v3 variable regions of the B30.2/SPRY domain contain potency determinants for N-MLV restr
30 our previous studies, we have found that two SPRY domain-containing proteins, RanBP9 and RanBP10, int
36 lpha isoform also encodes a C-terminal B30.2(SPRY) domain, differences within which define the breadt
37 in relatively low affinity of the individual SPRY domains for the capsid, and the TRIM5alpha-mediated
38 -terminal RING/B-Box or the C-terminal B30.2/SPRY domain form heteromultimers with full-length huTRIM
42 ata are consistent with a model in which one SPRY domain interacts with more than one capsid monomer
43 ly self-associating TRIM proteins, the B30.2(SPRY) domain is not required for higher order self-assoc
45 h identity of the target virus and the B30.2/SPRY domain-mediated affinity for the viral capsid deter
46 tion is essential for restriction when B30.2(SPRY) domain-mediated interactions with the retroviral c
48 small segment in the carboxy-terminal B30.2/SPRY domain of huTRIM5alpha with its rhesus macaque coun
50 adation was mediated by the highly conserved SPRY domain of TRIM14, which might involve the K48 ubiqu
54 ystal structure of the rhesus TRIM5alpha PRY/SPRY domain that reveals essential features for capsid b
55 by substitution with a less efficient B30.2/SPRY domain, the promotion of higher-order association b
56 investigate binding of the rhesus TRIM5alpha SPRY domain to a selection of HIV capsid constructs.
57 A few amino acids in the virus-interacting SPRY domain were found to be responsible for most of thi
58 cryo-EM studies disagree on the position of SPRY domains, which had been proposed based on homology
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