Evidence map›Paper›PMID 11320236›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2001

Structure and function in rhodopsin: Mass spectrometric identification of the abnormal intradiscal disulfide bond in misfolded retinitis pigmentosa mutants.

J Hwa, J Klein-Seetharaman, H G Khorana

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

27 citing papers in PubMed, 66 citations in OpenAlex.

  1. Article
  2. Gobind's last graduate student.Biophysical reviews · 2023
    Article
  3. Structural aspects of rod opsin and their implication in genetic diseases.Pflugers Archiv : European journal of physiology · 2021
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Structure and activation of rhodopsin.Acta pharmacologica Sinica · 2012
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

J HwaDepartments of Biology and Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
J Klein-Seetharaman
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
Role of ubiqutin in quality control of lens proteinsR01EY011717 · NEI · TUFTS UNIVERSITY BOSTON · PI SHANG, FU · 2003 to 2010
$1.8M
UBIQUITIN DEPENDENT PATHWAY AND LENS EPITHELIUMR29EY011717 · NEI · TUFTS UNIVERSITY BOSTON · PI SHANG, FU · 1998 to 2002
$381k
SYNTHETIC &BIOLOGICAL STUDIES OF NUCLEIC ACIDSR37GM028289 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI KHORANA, H. GOBIND · 1986 to 1995
–
NEI NIH HHS EY11717NEI NIH HHS R01 EY011717NEI NIH HHS R29 EY011717NIGMS NIH HHS GM28289NIGMS NIH HHS R01 GM028289
6 · The paper itself

Abstract

Retinitis pigmentosa (RP) point mutations in both the intradiscal (ID) and transmembrane domains of rhodopsin cause partial or complete misfolding of rhodopsin, resulting in loss of 11-cis-retinal binding. Previous work has shown that misfolding is caused by the formation of a disulfide bond in the ID domain different from the native Cys-110-Cys-187 disulfide bond in native rhodopsin. Here we report on direct identification of the abnormal disulfide bond in misfolded RP mutants in the transmembrane domain by mass spectrometric analysis. This disulfide bond is between Cys-185 and Cys-187, the same as previously identified in misfolded RP mutations in the ID domain. The strategy described here should be generally applicable to identification of disulfide bonds in other integral membrane proteins.

Indexed as

Protein FoldingAmino Acid SequenceAnimalsCOS CellsCysteineDisulfidesEndopeptidase KHumansLysineMaleimidesModels, MolecularMolecular Sequence DataMutationProtein DenaturationProtein Structure, SecondaryRetinitis PigmentosaCysteineDisulfidesEndopeptidase KLysineMaleimidesmaleimido-butyryl-biocytinRhodopsinRod Opsins

Identifiers

PMID11320236
PMCPMC33130
OpenAlexW2124216990

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.