Evidence map›Paper›PMID 22104179›Full record

ReviewCurrent opinion in chemical biology2011

Visualizing protein partnerships in living cells and organisms.

Melissa A Lowder, Jacob S Appelbaum, Elissa M Hobert, Alanna Schepartz

Abstract readReview
In one paragraph

Review in Current opinion in chemical biology, 2011. 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
–field-weighted citation impact
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.

  1. Article
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  5. Thrombin-Induced Podocyte Injury Is Protease-Activated Receptor Dependent.Journal of the American Society of Nephrology : JASN · 2017
    Article
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  7. Review
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  9. Article
  10. Review
  11. Article
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  15. Review
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  18. Solubility-based genetic screen identifies RING finger protein 126 as an E3 ligase for activation-induced cytidine deaminase.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  19. 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

4 authors.

Melissa A LowderYale University, Department of Molecular Biophysics and Biochemistry, 60 Whitney Ave., New Haven, CT 06520-8114, USA.
Jacob S Appelbaum
Elissa M Hobert
Alanna Schepartz

Funding

MEDICAL SCIENTIST TRAINING PROGRAMT32GM007205 · NIGMS · YALE UNIVERSITY · PI KAZMIERCZAK, BARBARA I · 1985 to 2019
$42.9M
Skill Development for Diverse Scientific Careers: A New Course Predoctoral Program in Cellular and Molecular BiologyT32GM007223 · NIGMS · YALE UNIVERSITY · PI BASERGA, SUSAN J · 1985 to 2019
$31.0M
Surveying protein partnerships and assembly with bipartite tetracysteine displayR01GM083257 · NIGMS · YALE UNIVERSITY · PI SCHEPARTZ, ALANNA · 2008 to 2018
$3.2M
A novel small-molecule approach to detect specifc peptide-MHC complexesF30HL094078 · NHLBI · YALE UNIVERSITY · PI APPELBAUM, JACOB · 2008 to 2010
$126k
NHLBI NIH HHS F30 HL094078NIGMS NIH HHS GM7223-37NIGMS NIH HHS GM83257NIGMS NIH HHS R01 GM083257NIGMS NIH HHS T32 GM007205NIGMS NIH HHS T32 GM007223NIGMS NIH HHS T32GM07205
6 · The paper itself

Abstract

In recent years, scientists have expanded their focus from cataloging genes to characterizing the multiple states of their translated products. One anticipated result is a dynamic map of the protein association networks and activities that occur within the cellular environment. While in vitro-derived network maps can illustrate which of a multitude of possible protein-protein associations could exist, they supply a falsely static picture lacking the subtleties of subcellular location (where) or cellular state (when). Generating protein association network maps that are informed by both subcellular location and cell state requires novel approaches that accurately characterize the state of protein associations in living cells and provide precise spatiotemporal resolution. In this review, we highlight recent advances in visualizing protein associations and networks under increasingly native conditions. These advances include second generation protein complementation assays (PCAs), chemical and photo-crosslinking techniques, and proximity-induced ligation approaches. The advances described focus on background reduction, signal optimization, rapid and reversible reporter assembly, decreased cytotoxicity, and minimal functional perturbation. Key breakthroughs have addressed many challenges and should expand the repertoire of tools useful for generating maps of protein interactions resolved in both time and space.

Indexed as

Cross-Linking ReagentsFluorescence Resonance Energy TransferFluorescent DyesMicroscopy, FluorescencePhotochemical ProcessesPhotochemistryProtein Interaction MappingProtein Interaction MapsProteinsStaining and LabelingUltraviolet RaysCross-Linking ReagentsFluorescent DyesProteins

Identifiers

PMID22104179
PMCPMC3238055

What OpenQuestion holds

Textmetadata
LicenceTDM
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.