Evidence map›Paper›PMID 10737783›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2000

Structure and function in rhodopsin: destabilization of rhodopsin by the binding of an antibody at the N-terminal segment provides support for involvement of the latter in an intradiscal tertiary structure.

K Cha, P J Reeves, H G Khorana

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.9field-weighted citation impact, top 28% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

13 citing papers in PubMed, 37 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Molecular dynamics of rhodopsin and free opsin: computer simulation.Neuroscience and behavioral physiology · 2007
    Article
  10. Article
  11. Article
  12. Article
  13. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

K ChaDepartments of Biology and Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
P J Reeves
H G Khorana
Massachusetts Institute of Technology · US

Funding

SYNTHETIC AND BIOLOGICAL STUDIES OF NUCLEIC ACIDSR01GM028289 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI KHORANA, H. GOBIND · 1985 to 2003
$2.9M
RHODOPSIN MISFOLDING IN RETINITIS PIGMENTOSAR01EY011716 · NEI · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI KHORANA, H. GOBIND · 1998 to 2007
$1.7M
SYNTHETIC &BIOLOGICAL STUDIES OF NUCLEIC ACIDSR37GM028289 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI KHORANA, H. GOBIND · 1986 to 1995
–
NEI NIH HHS EY11716NEI NIH HHS R01 EY011716NIGMS NIH HHS GM28289NIGMS NIH HHS R01 GM028289
6 · The paper itself

Abstract

A monoclonal anti-rhodopsin antibody (B6-30N), characterized by Hargrave and coworkers [Adamus, G., Zam, Z. S., Arendt, A., Palczewski, K., McDowell, J. M. & Hargrave, P. (1991) Vision Res. 31, 17-31] as recognizing a short peptide sequence at the N terminus, failed to bind to rhodopsin when the latter was solubilized in dodecylmaltoside (DM). Of the detergents tested thus far, DM affords maximum stability to rhodopsin. Solubilization of rhodopsin in cholate allowed binding of the antibody, but the binding caused destabilization as evidenced by the accelerated loss of absorbance at 500 nm. The result provides support for the earlier conclusion that the N-terminal segment is an integral part of a tertiary structure in the intradiscal domain of native rhodopsin coupled to a tertiary structure in the transmembrane domain. Additional comparative studies on the stability of rhodopsin in different detergents were carried out after direct solubilization from rod outer segments and after extensive treatments to remove the endogenous phospholipids. Purification of rhodopsin in DM resulted in essentially quantitative removal of endogenous phospholipids. When rhodopsin thus purified was treated with the above antibody in DM and in cholate, enhanced destabilization (5-fold) was observed in the latter detergent.

Indexed as

Binding Sites, AntibodyAmino Acid SequenceAnimalsCattleChromatography, Thin LayerDetergentsKineticsMolecular Sequence DataPhospholipidsProtein Structure, SecondaryRhodopsinStructure-Activity RelationshipDetergentsPhospholipidsRhodopsin

Identifiers

PMID10737783
PMCPMC16184
OpenAlexW2052792449

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.