Evidence map›Paper›PMID 16505961›Full record

ArticleJournal of biomolecular NMR2006

Rapid preparation of stable isotope labeled peptides that bind to target proteins by a phage library system.

Yumiko Mizukoshi, Hideo Takahashi, Ichio Shimada

Abstract read
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In one paragraph

Article in Journal of biomolecular NMR, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.5field-weighted citation impact, top 29% 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

4 citing papers in PubMed, 7 citations in OpenAlex.

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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

3 authors at 3 institutions in 1 country.

Yumiko MizukoshiJapan Biological Information Research Center (JBIRC), Japan Biological Informatics Consortium (JBIC), Tokyo, 135-0064, Japan.
Hideo Takahashi
Ichio Shimada
Japan Biological Informatics Consortium · JPNational Institute of Advanced Industrial Science and Technology · JPThe University of Tokyo · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have developed a system for directly isolating foreign peptides displayed on the N-terminus of the major coat protein of bacteriophage M13. The phage particle in this system is formed as a mixture of wild type and modified coat proteins. The N-terminal segment of the modified coat protein was mutated for chemical cleavage, in order to obtain the displayed peptide from the major coat protein. Using 13C, 15N- labeled medium, we introduced stable isotopes, 13C and/or 15N, into the coat proteins. The NMR spectra for the cleaved peptides from the phage particles could be recorded within a few days after the selection of the phage clone.

Indexed as

Peptide LibraryAmino Acid SequenceBacteriophage M13Capsid ProteinsCarbon IsotopesIsotope LabelingMolecular Sequence DataNitrogen IsotopesNuclear Magnetic Resonance, BiomolecularPeptidesCapsid ProteinsCarbon IsotopesNitrogen IsotopesPeptide LibraryPeptides

Identifiers

PMID16505961
OpenAlexW2086712529

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.