Evidence map›Paper›PMID 21255213›Full record

ArticleTraffic (Copenhagen, Denmark)2011

Superfolder GFP is fluorescent in oxidizing environments when targeted via the Sec translocon.

Deborah E Aronson, Lindsey M Costantini, Erik L Snapp

Abstract read
In one paragraph

Article in Traffic (Copenhagen, Denmark), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 88 papers.

0numbers the graph read from it
0cells of the map it votes in
88citing papers in PubMed
10.8field-weighted citation impact, top 1% 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

88 citing papers in PubMed, 135 citations in OpenAlex.

  1. ER discontinuities are common inbioRxiv : the preprint server for biology · 2026
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28 more citing papers are in PubMed but not listed here.

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.

Deborah E AronsonDepartment of Anatomy and Structural Biology, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA.
Lindsey M Costantini
Erik L Snapp
Albert Einstein College of Medicine · US

Funding

TRAINING PROGRAM IN CELLULAR &MOLEC. BIOLOGY &GENETICST32GM007491 · NIGMS · YESHIVA UNIVERSITY · PI QUERY, CHARLES C · 1985 to 2021
$17.0M
ER Chaperone Availability in Cells During Homeostasis and Misfolded Protein StresR01GM086530 · NIGMS · ALBERT EINSTEIN COLLEGE OF MEDICINE · PI SNAPP, ERIK L. · 2009 to 2010
$638k
DETECTING AND RESPONDING TO MISFOLDED PROTEIN BURDENS IN AGING CELLSR21AG032544 · NIA · ALBERT EINSTEIN COLLEGE OF MEDICINE · PI SCHMIDT, MARION, SNAPP, ERIK L. · 2008 to 2009
$457k
Mechanism of Targeting of a Luminal KDEL-containing Protein to the Golgi ComplexF31GM089090 · NIGMS · ALBERT EINSTEIN COLLEGE OF MEDICINE · PI ARONSON, DEBORAH · 2009 to 2010
$83k
NIA NIH HHS R21 AG032544NIGMS NIH HHS F31 GM089090NIGMS NIH HHS F31GM089090NIGMS NIH HHS R01 GM086530NIGMS NIH HHS R01GM086530-01NIGMS NIH HHS T32 GM007491
6 · The paper itself

Abstract

The ability to study proteins in live cells using genetically encoded fluorescent proteins (FPs) has revolutionized cell biology (1-3). Researchers have created numerous FP biosensors and optimized FPs for specific organisms and subcellular environments in a rainbow of colors (4,5). However, expressing FPs in oxidizing environments such as the eukaryotic endoplasmic reticulum (ER) or the bacterial periplasm can impair folding, thereby preventing fluorescence (6,7). A substantial fraction of enhanced green fluorescent protein (EGFP) oligomerizes to form non-fluorescent mixed disulfides in the ER (6) and EGFP does not fluoresce in the periplasm when targeted via the SecYEG translocon (7). To overcome these obstacles, we exploited the highly efficient folding capability of superfolder GFP (sfGFP) (8). Here, we report sfGFP does not form disulfide-linked oligomers in the ER and maltose-binding protein (MBP) signal sequence (peri)-sfGFP (9) is brightly fluorescent in the periplasm of Escherichia coli. Thus, sfGFP represents an important research tool for studying resident proteins of oxidizing environments.

Indexed as

Protein ConformationProtein FoldingCell LineDisulfidesEscherichia coli ProteinsFluorescenceGreen Fluorescent ProteinsHumansMembrane ProteinsOxidation-ReductionSEC Translocation ChannelsDisulfidesenhanced green fluorescent proteinEscherichia coli ProteinsGreen Fluorescent ProteinsMembrane ProteinsSecE protein, E coliSecG protein, E coliSEC Translocation ChannelsSecY protein, E coli

Identifiers

PMID21255213
PMCPMC3079558
OpenAlexW2062731288

What OpenQuestion holds

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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.