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1                           Antibodies against visinin and GABA were used to distinguish photoreceptors
2 ressed photoreceptor-specific genes, such as visinin and opsins.
3 fferentiation (such as HuC/D, calretinin and visinin) are expressed by neurons that are found directl
4                     In the subretinal space, visinin(+) cells aligned along the RPE or an RPE-like st
5 lues, as determined by morphologic analysis, visinin immunocytochemistry, and peanut lectin binding.
6 NP rs16983422 (2.8 kilobases upstream of the visinin-like 1 gene (VSNL1)) was marginally associated w
7                                   The neural visinin-like Ca(2+)-binding domain at the C-terminal end
8 CCaMK) is characterized by the presence of a visinin-like Ca(2+)-binding domain unlike other known ca
9                            The presence of a visinin-like Ca2+-binding domain in CCaMK adds an additi
10 n, a calmodulin-binding domain, and a neural visinin-like Ca2+-binding domain was recently cloned fro
11 ase regulating the kinase activity, namely a visinin-like domain acting as a Ca(2+)-triggered switch
12 rotein kinase (CCaMK), namely the C-terminal visinin-like domain acting as Ca(2+)-sensitive molecular
13                                          The visinin-like domain binds three calcium ions, leading to
14                A deletion mutant lacking the visinin-like domain did not show Ca2+-stimulated autopho
15             The affinity for calcium ions of visinin-like domain EF-hands 1 and 2 (K(d) = 200 +/- 50
16    Studies with site-directed mutants of the visinin-like domain indicated that EF-hands II and III a
17 ted autophosphorylation mediated through the visinin-like domain is a new regulatory mechanism for CC
18                        Ca(2+)-Binding to the visinin-like domain leads to autophosphorylation and cha
19 ation rate constants were determined for the visinin-like domain of CCaMK, M. truncatula calmodulin 1
20  taken with constructs comprising either the visinin-like domain of Medicago truncatula CCaMK, which
21 n the visinin-like domain, we found that the visinin-like domain regulated Ca(2+)-stimulated autophos
22 in, a calmodulin-binding domain and a neural visinin-like domain with three EF-hands.
23               Using EF-hand deletions in the visinin-like domain, we found that the visinin-like doma
24 r Ca2+-induced conformational changes in the visinin-like domain.
25 dues 358 520 revealed that Ca2+ binds to the visinin-like domain.
26 ctions of the plant visinin-like proteins or visinin-like domains in plant proteins are not well know
27 ts point to a general role for a subgroup of visinin-like neuronal calcium sensor proteins in the act
28 he neuron-specific, calcium-binding protein, visinin-like protein (VILIP) contains one double-strande
29 +)-binding proteins, such as neurocalcin and visinin-like protein (VILIP)-1 have no such effects.
30                                              Visinin-like protein 1 (VILIP-1) belongs to the neuronal
31                                              Visinin-like protein 1 (VILIP-1) has demonstrated potent
32  phosphorylated at threonine 181 (P-tau181), visinin-like protein 1 (VILIP-1), and chitinase-3-like p
33 , some tumor-suppressor genes such as EPHB6, visinin-like protein 1 (VSNL-1), and BLU were up-regulat
34          The neuronal calcium sensor protein visinin-like protein 2 (VILIP-2) inhibits inactivation a
35                                              Visinin-like protein-1 (VILIP-1) has demonstrated potent
36                                              Visinin-like protein-1 (VILIP-1) is a member of the neur
37                   The calcium sensor protein visinin-like protein-1 (VILIP-1) was isolated from a bra
38                                              Visinin-like protein-1 (VILIP-1), a member of the neuron
39 fied cellular RNA 7SL, clathrin heavy chain, visinin-like protein-1, and three highly specific subreg
40         Ca(2+)-binding protein-1 (CaBP1) and Visinin-like protein-2 (VILIP-2) are neurospecific calmo
41 nCaBPs calcium-binding protein 1 (CaBP1) and visinin-like protein-2 (VILIP-2) differ from calmodulin
42                                              Visinin-like protein-2 (VILIP-2) is a CaM-related Ca2+-b
43            Biological functions of the plant visinin-like proteins or visinin-like domains in plant p
44 tory factor for gene expression of the other visinin-like subfamily members including HPCAL4, HPCAL1,
45             In the embryonic retina, we find visinin-positive photoreceptors that transiently express
46 idenced by a spatially restricted pattern of visinin RNA observed at E7.

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