Evidence map›Paper›PMID 11320238›Full record

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

Mapping of contact sites in complex formation between light-activated rhodopsin and transducin by covalent crosslinking: use of a chemically preactivated reagent.

Y Itoh, K Cai, 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 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

31 citing papers in PubMed, 99 citations in OpenAlex.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Y ItohDepartments of Biology and Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
K Cai
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

Contact sites in interaction between light-activated rhodopsin and transducin (T) have been investigated by using a chemically preactivated crosslinking reagent, N-succinimidyl 3-(2-pyridyldithio)propionate. The 3 propionyl-N-succinimidyl group in the reagent was attached by a disulfide exchange reaction to rhodopsin mutants containing single reactive cysteine groups in the cytoplasmic loops. Complex formation between the derivatized rhodopsin mutants and T was carried out by illumination at lambda > 495 nm. Subsequent increase in pH (from 6 to 7.5 or higher) of the complex resulted in crosslinking of rhodopsin to the T(alpha) subunit. Crosslinking to T(alpha) was demonstrated for the rhodopsin mutants K141C, S240C, and K248C, and the crosslinked sites in T(alpha) were identified for the rhodopsin mutant S240C. The peptides carrying the crosslinking moiety were isolated from the trypsin-digested peptide mixture, and their identification was carried out by matrix-assisted laser desorption ionization-time of flight mass spectrometry. The main site of crosslinking is within the peptide sequence, Leu-19-Arg-28 at the N-terminal region of T(alpha). The total results show that both the N and the C termini of T(alpha) are in close vicinity to the third cytoplasmic loop of rhodopsin in the complex between rhodopsin and T.

Indexed as

LightAmino Acid SequenceAmino Acid SubstitutionAnimalsAzidesBinding SitesBlotting, WesternCattleCross-Linking ReagentsCysteineHydrogen-Ion ConcentrationModels, MolecularMolecular Sequence DataMutationPeptide FragmentsProtein BindingAzidesCross-Linking ReagentsCysteineN-((2-pyridyldithio)ethyl)-4-azidosalicylamideN-succinimidyl 3-(2-pyridyldithio)propionatePeptide FragmentsProtein SubunitsPyridinesRhodopsinSuccinimidesTransducin

Identifiers

PMID11320238
PMCPMC33132
OpenAlexW2124961362

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.