Evidence map›Paper›PMID 28754692›Full record

ArticleThe Journal of biological chemistry2017

An

Kambiz M Hamadani, Jesse Howe, Madeleine K Jensen, Peng Wu, Jamie H D Cate, Susan Marqusee

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.2field-weighted citation impact, top 48% 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

1 citing paper in PubMed, 5 citations in OpenAlex.

  1. 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

6 authors at 5 institutions in 2 countries.

Kambiz M HamadaniFrom the California Institute for Quantitative Biosciences and khamadani@csusm.edu.
Jesse Howethe Department of Chemistry and Biochemistry, California State University, San Marcos, California 92096, and.
Madeleine K Jensenthe Departments of Molecular and Cell Biology and.
Peng Wuthe Department of Chemical Physiology, Scripps Research Institute, La Jolla, California 92037.
Jamie H D CateFrom the California Institute for Quantitative Biosciences and jcate@lbl.gov.
Susan MarquseeFrom the California Institute for Quantitative Biosciences and marqusee@berkeley.edu.
Quantitative BioSciences · USCalifornia State University, San Marcos · USInstitute of Molecular and Cell Biology · RUQB3 · USScripps Research Institute · US

Funding

ZOVIRAX CREAM TO TREAT HERPES LABIALIS IN ADOLESCENTSM01RR000827 · NCRR · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI HAAS, RICHARD H · 1985 to 2010
$74.3M
THE MOLECULAR BASIS OF CELL FUNCTIONT32GM007232 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI BILDER, DAVID, UNAL, ELCIN · 1985 to 2022
$36.4M
The Role of the Ribosome in the Accuracy of TranslationR01GM065050 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI CATE, JAMIE H · 2001 to 2022
$7.4M
Sequence and Environmental Determinants of the Protein Energy LandscapeR01GM050945 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI MARQUSEE, SUSAN · 1999 to 2022
$7.4M
NCRR NIH HHS M01 RR000827NIGMS NIH HHS R01 GM050945NIGMS NIH HHS R01 GM065050NIGMS NIH HHS T32 GM007232
6 · The paper itself

Abstract

Biomolecular systems exhibit many dynamic and biologically relevant properties, such as conformational fluctuations, multistep catalysis, transient interactions, folding, and allosteric structural transitions. These properties are challenging to detect and engineer using standard ensemble-based techniques. To address this drawback, single-molecule methods offer a way to access conformational distributions, transient states, and asynchronous dynamics inaccessible to these standard techniques. Fluorescence-based single-molecule approaches are parallelizable and compatible with multiplexed detection; to date, however, they have remained limited to serial screens of small protein libraries. This stems from the current absence of methods for generating either individual dual-labeled protein samples at high throughputs or protein libraries compatible with multiplexed screening platforms. Here, we demonstrate that by combining purified and reconstituted

Indexed as

Fluorescence Resonance Energy TransferAlkynesAzidesCatalysisCopperCycloaddition ReactionProtein FoldingProteinsAlkynesAzidesCopperProteinsbioconjugationclick chemistrydirected evolutionfluorescence resonance energy transfer (FRET)high-throughput screening (HTS)in vitro translationprotein foldingribosome displaysingle-molecule biophysicsunnatural amino acid incorporation

Identifiers

PMID28754692
PMCPMC5612098
OpenAlexW2740240759

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.