Evidence map›Paper›PMID 9843968›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1998

Mobility of cytochrome P450 in the endoplasmic reticulum membrane.

E Szczesna-Skorupa, C D Chen, S Rogers, B Kemper

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.7field-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

19 citing papers in PubMed, 62 citations in OpenAlex.

  1. Article
  2. Genome-wide analysis of theFrontiers in plant science · 2024
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  10. Membrane protein complexes catalyze both 4- and 3-hydroxylation of cinnamic acid derivatives in monolignol biosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  11. The signal-anchor sequence of CYP2C1 inserts into the membrane as a hairpin structure.Biochemical and biophysical research communications · 2011
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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

4 authors at 1 institution in 1 country.

E Szczesna-SkorupaDepartment of Molecular and Integrative Physiology, University of Illinois, Urbana, IL 61801, USA.
C D Chen
S Rogers
B Kemper
University of Illinois Urbana-Champaign · US

Funding

STRUCTURAL DETERMINANTS OF FUNCTIONAL CYTOCHROMES P450R01GM035897 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI KEMPER, BYRON W · 1986 to 2009
$2.3M
NIGMS NIH HHS GM35897NIGMS NIH HHS R01 GM035897
6 · The paper itself

Abstract

Cytochrome P450 2C2 is a resident endoplasmic reticulum (ER) membrane protein that is excluded from the recycling pathway and contains redundant retention functions in its N-terminal transmembrane signal/anchor sequence and its large, cytoplasmic domain. Unlike some ER resident proteins, cytochrome P450 2C2 does not contain any known retention/retrieval signals. One hypothesis to explain exclusion of resident ER proteins from the transport pathway is the formation of networks by interaction with other proteins that immobilize the proteins and are incompatible with packaging into the transport vesicles. To determine the mobility of cytochrome P450 in the ER membrane, chimeric proteins of either cytochrome P450 2C2, its catalytic domain, or the cytochrome P450 2C1 N-terminal signal/anchor sequence fused to green fluorescent protein (GFP) were expressed in transiently transfected COS1 cells. The laurate hydroxylase activities of cytochrome P450 2C2 or the catalytic domain with GFP fused to the C terminus were similar to the native enzyme. The mobilities of the proteins in the membrane were determined by recovery of fluorescence after photobleaching. Diffusion coefficients for all P450 chimeras were similar, ranging from 2.6 to 6.2 x 10(-10) cm2/s. A coefficient only slightly larger (7.1 x 10(-10) cm2/s) was determined for a GFP chimera that contained a C-terminal dilysine ER retention signal and entered the recycling pathway. These data indicate that exclusion of cytochrome P450 from the recycling pathway is not mediated by immobilization in large protein complexes.

Indexed as

AnimalsBiological TransportCOS CellsCytochrome P-450 Enzyme SystemEndoplasmic ReticulumFluorescenceIntracellular MembranesRecombinant Fusion ProteinsCytochrome P-450 Enzyme SystemRecombinant Fusion Proteins

Identifiers

PMID9843968
PMCPMC24528
OpenAlexW1987503123

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.