Evidence map›Paper›PMID 21575586›Full record

ArticleBiophysical journal2011

Labeling of specific cysteines in proteins using reversible metal protection.

Michael C Puljung, William N Zagotta

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.0field-weighted citation impact, top 27% 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

21 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
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  5. Article
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  7. Article
  8. Article
  9. Review
  10. Article
  11. Arylation Chemistry for Bioconjugation.Angewandte Chemie (International ed. in English) · 2019
    Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Cadmium-cysteine coordination in the BK inner pore region and its structural and functional implications.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  17. Article
  18. Article
  19. Fluorescent labeling and modification of proteins.Journal of chemical biology · 2013
    Review
  20. 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

2 authors at 1 institution in 1 country.

Michael C PuljungDepartment of Physiology and Biophysics, Howard Hughes Medical Institute, University of Washington, Seattle, Washington, USA.
William N Zagotta
University of Washington · US

Funding

GATING MECHANISMS OF RETINAL ROD CGMP-ACTIVATED CHANNELSR01EY010329 · NEI · UNIVERSITY OF WASHINGTON · PI ZAGOTTA, WILLIAM N · 1994 to 2023
$7.7M
CNG Channel Gating Movements Monitored via Fluorescene QuenchingF32EY018981 · NEI · UNIVERSITY OF WASHINGTON · PI PULJUNG, MICHAEL C · 2008 to 2009
$105k
Howard Hughes Medical InstituteNEI NIH HHS EY10329NEI NIH HHS F32 EY018981NEI NIH HHS F32EY018981NEI NIH HHS R01 EY010329
6 · The paper itself

Abstract

Fluorescence spectroscopy is an indispensible tool for studying the structure and conformational dynamics of protein molecules both in isolation and in their cellular context. The ideal probes for monitoring intramolecular protein motions are small, cysteine-reactive fluorophores. However, it can be difficult to obtain specific labeling of a desired cysteine in proteins with multiple cysteines, in a mixture of proteins, or in a protein's native environment, in which many cysteine-containing proteins are present. To obtain specific labeling, we developed a method we call cysteine metal protection and labeling (CyMPL). With this method, a desired cysteine can be reversibly protected by binding group 12 metal ions (e.g., Cd²⁺ and Zn²⁺) while background cysteines are blocked with nonfluorescent covalent modifiers. We increased the metal affinity for specific cysteines by incorporating them into minimal binding sites in existing secondary structural motifs (i.e., α-helix or β-strand). After the metal ions were removed, the deprotected cysteines were then available to specifically react with a fluorophore.

Indexed as

AnimalsBinding SitesCadmiumCysteineMiceProteinsProtein Structure, SecondaryStaining and LabelingThermodynamicsXenopusCadmiumCysteineProteins

Identifiers

PMID21575586
PMCPMC3093568
OpenAlexW2041200667

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.