Evidence map›Paper›PMID 8108405›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1994

Invariant tryptophan at a shielded site promotes folding of the conformational unit of spectrin.

R I MacDonald, A Musacchio, R A Holmgren, M Saraste

Open access · greenAbstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.5field-weighted citation impact, top 17% 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

17 citing papers in PubMed, 44 citations in OpenAlex.

  1. Multiple Functions of Spectrin: Convergent Effects.The Journal of membrane biology · 2020
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  11. Structure and dynamics of de novo proteins from a designed superfamily of 4-helix bundles.Protein science : a publication of the Protein Society · 2008
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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

4 authors at 1 institution in 1 country.

R I MacDonaldDepartment of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, IL 60208.
A Musacchio
R A Holmgren
M Saraste
Northwestern University · US

Funding

TRANSFORMATION OF HEMATOPOIETIC PROGENITOR CELLSP01HL045168 · NHLBI · NORTHWESTERN UNIVERSITY · 1991 to 1995
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NHLBI NIH HHS 1PO1 HL45168
6 · The paper itself

Abstract

The tryptophan that is highly conserved among repeating structural units of spectrin is reported to promote the conformational stability of one such unit of chicken brain alpha-spectrin. Four constructs were inserted into pET vectors for overexpression in Escherichia coli of the following spectrin peptides: (i) two adjacent but separately expressed "conformationally phased" repeating units, R16 and R17, one of which (R17) contains a single tryptophan; (ii) a mutant, M17, of the single tryptophan-containing unit with alanine substituted for the tryptophan; and (iii) a conformationally unphased unit, 1617, composed of half of each of the phased units. Both the mutant unit and the unphased unit were much more readily digested by chymotrypsin and by elastase than the phased units and exhibited only 38% and 54% as much alpha-helical structure, respectively, as the phased units by their far UV CD spectra; 90 degrees light scattering measurements revealed the folded peptides to be predominantly monomeric in solution, whereas the unfolded, protease-sensitive peptides consisted of dimers and/or trimers. This trend was corroborated by their dynamic light scattering. Both the blue-shifted wavelength of maximal emission and the relative inaccessibility to acrylamide of the single tryptophan in the folded unit indicate that the invariant tryptophan occupies a site that is shielded from the aqueous phase.

Indexed as

Protein FoldingAmino Acid SequenceAnimalsBrain ChemistryChickensChymotrypsinCircular DichroismConserved SequenceDNA Mutational AnalysisEscherichia coliMolecular Sequence DataPancreatic ElastasePeptide FragmentsRecombinant ProteinsScattering, RadiationSpectrinChymotrypsinPancreatic ElastasePeptide FragmentsRecombinant ProteinsSpectrinTryptophan

Identifiers

PMID8108405
PMCPMC43145
OpenAlexW2005492152

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.