Monoclonal antibodies to rhodopsin: characterization, cross-reactivity, and application as structural probes

Molday, Robert S.; MacKenzie, Donald J.

doi:10.1021/bi00272a020

Cited by 406 publications

(303 citation statements)

References 30 publications

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“…This may be because the antigen has different conformations under the different conditions used, resulting in exposure of different epitopes and thus having different reactivities with the ,monoclonal antibody. Similar observations have been reported previously (Molday & MacKenzie, 1983;Kuismanen et aL, 1984). Another possibility is that these differences may be due to the methods of preparing the antigens, i.e.…”

supporting

confidence: 92%

Monoclonal Antibodies to Cowpox Virus: Polypeptide Analysis of Several Major Antigens

Kitamoto

Tanimoto

Hiroi

et al. 1987

Journal of General Virology

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SUMMARYMonoclonal antibodies directed against major antigens induced by cowpox virus (CPV) were produced. The specificities of these antibodies were established by immunoprecipitation, immunoblotting and several serological analyses, and from the cross-reactivities of these antibodies with cells infected with various other poxviruses, ectromelia virus (EV), vaccinia virus and Shope fibroma virus. The antibodies defined included ones reacting with each of the known major antigens of poxviruses, i.e. the common antigen of all poxviruses (probably NP antigen), the Orthopoxvirus-specific antigen (probably LS antigen), the haemagglutinin, the cell surface antigen, the common A-type inclusions in CPV and EV, and the antigen involved in neutralization.

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supporting

confidence: 92%

Monoclonal Antibodies to Cowpox Virus: Polypeptide Analysis of Several Major Antigens

Kitamoto

Tanimoto

Hiroi

et al. 1987

Journal of General Virology

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“…Streptavidin-agarose beads (Life Technologies) were used to pull down biotinylated protein followed by western blotting analysis. WT TRPV2 and TRPV2 D564-589 were detected with 1D4 antibody (1:1,000), which was generated from our laboratory 46 . Na þ /K þ ATPase (catalogue number 3010, 1:100, Cell Signaling Technology) and b-actin (catalogue number 3700, 1:1,000, Cell Signaling Technology) were used as surface biotinylation and loading controls, respectively.…”

Section: Methodsmentioning

confidence: 99%

Structure of the Full-Length TRPV2 Channel by Cryo-EM

et al. 2016

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Transient receptor potential (TRP) proteins form a superfamily Ca 2 þ -permeable cation channels regulated by a range of chemical and physical stimuli. Structural analysis of a 'minimal' TRP vanilloid subtype 1 (TRPV1) elucidated a mechanism of channel activation by agonists through changes in its outer pore region. Though homologous to TRPV1, other TRPV channels (TRPV2-6) are insensitive to TRPV1 activators including heat and vanilloids. To further understand the structural basis of TRPV channel function, we determined the structure of full-length TRPV2 at B5 Å resolution by cryo-electron microscopy. Like TRPV1, TRPV2 contains two constrictions, one each in the pore-forming upper and lower gates. The agonist-free full-length TRPV2 has wider upper and lower gates compared with closed and agonist-activated TRPV1. We propose these newly revealed TRPV2 structural features contribute to diversity of TRPV channels.

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“…PBS with 40 mM 11-cis-retinal in the dark. Dodecyl maltoside (1% (w/v)) and PMSF (20 mg ml K1 ) were then added before passage over a CNBr-activated sepharose-binding column coupled to an anti-1D4 monoclonal antibody (Molday & MacKenzie 1983).…”

Section: Materials and Methods (A) Animalsmentioning

confidence: 99%

Cone visual pigments in two marsupial species: the fat-tailed dunnart (Sminthopsis crassicaudata) and the honey possum (Tarsipes rostratus)

Cowing¹,

Arrese²,

Davies

et al. 2008

Proc. R. Soc. B.

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Uniquely for non-primate mammals, three classes of cone photoreceptors have been previously identified by microspectrophotometry in two marsupial species: the polyprotodont fat-tailed dunnart (Sminthopsis crassicaudata) and the diprotodont honey possum (Tarsipes rostratus). This report focuses on the genetic basis for these three pigments. Two cone pigments were amplified from retinal cDNA of both species and identified by phylogenetics as members of the short wavelength-sensitive 1 (SWS1) and long wavelengthsensitive (LWS) opsin classes. In vitro expression of the two sequences from the fat-tailed dunnart confirmed the peak absorbances at 363 nm in the UV for the SWS1 pigment and 533 nm for the LWS pigment. No additional expressed cone opsin sequences that could account for the middle wavelength cones could be amplified. However, amplification from the fat-tailed dunnart genomic DNA with RH1 (rod) opsin primer pairs identified two genes with identical coding regions but sequence differences in introns 2 and 3. Uniquely therefore for a mammal, the fat-tailed dunnart has two copies of an RH1 opsin gene. This raises the possibility that the middle wavelength cones express a rod rather than a cone pigment.

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Monoclonal antibodies to rhodopsin: characterization, cross-reactivity, and application as structural probes

Cited by 406 publications

References 30 publications

Monoclonal Antibodies to Cowpox Virus: Polypeptide Analysis of Several Major Antigens

Monoclonal Antibodies to Cowpox Virus: Polypeptide Analysis of Several Major Antigens

Structure of the Full-Length TRPV2 Channel by Cryo-EM

Cone visual pigments in two marsupial species: the fat-tailed dunnart (Sminthopsis crassicaudata) and the honey possum (Tarsipes rostratus)

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