Evidence map›Paper›PMID 29272560›Full record

ArticleChembiochem : a European journal of chemical biology2018

Evaluation of β-Amino Acid Replacements in Protein Loops: Effects on Conformational Stability and Structure.

David E Mortenson, Dale F Kreitler, Nicole C Thomas, Ilia A Guzei, Samuel H Gellman, Katrina T Forest

Open access · greenAbstract read
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.4field-weighted citation impact, top 35% 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

11 citing papers in PubMed, 20 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

6 authors at 1 institution in 1 country.

David E MortensonDepartment of Chemistry, University of Wisconsin-Madison, 1101 University Avenue, Madison, WI, 53706, USA.
Dale F KreitlerDepartment of Chemistry, University of Wisconsin-Madison, 1101 University Avenue, Madison, WI, 53706, USA.
Nicole C ThomasDepartment of Chemistry, University of Wisconsin-Madison, 1101 University Avenue, Madison, WI, 53706, USA.
Ilia A GuzeiDepartment of Chemistry, University of Wisconsin-Madison, 1101 University Avenue, Madison, WI, 53706, USA.
Samuel H GellmanDepartment of Chemistry, University of Wisconsin-Madison, 1101 University Avenue, Madison, WI, 53706, USA.
Katrina T ForestDepartments of Chemistry and Bacteriology, University of Wisconsin-Madison, 1550 Linden Drive, Madison, WI, 53706, USA.ORCID 0000-0003-4197-7662
University of Wisconsin–Madison · US

Funding

Use of designed peptides to study folding and bindingR01GM061238 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI GELLMAN, SAMUEL H. · 2000 to 2023
$7.9M
PREDOCTORAL TRAINING IN MOLECULAR BIOPHYSICST32GM008293 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI JACKSON, MEYER B. · 1989 to 2016
$4.6M
Functional analysis of the MbtH-like protein superfamilyR01GM100346 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI FOREST, KATRINA T, THOMAS, MICHAEL GEORGE · 2013 to 2016
$1.1M
PREDOCTORAL TRAINING PROGRAM IN MOLECULAR BIOPHYSICST32GM008392 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI DILGER, JAMES P · 1990 to 1999
–
NIGMS NIH HHS R01 GM061238NIGMS NIH HHS R01 GM100346NIGMS NIH HHS T32 GM008293NIGMS NIH HHS T32 GM008392
6 · The paper itself

Abstract

β-Amino acids have a backbone that is expanded by one carbon atom relative to α-amino acids, and β residues have been investigated as subunits in protein-like molecules that adopt discrete and predictable conformations. Two classes of β residue have been widely explored in the context of generating α-helix-like conformations: β

Indexed as

Amino AcidsCycloleucineModels, MolecularMolecular StructureProteinsProtein StabilityTemperatureAmino AcidscispentacinCycloleucineProteinsalpha/beta-peptidesbeta-hairpinsconformation analysisfoldamersPin1 WWprotein design

Identifiers

PMID29272560
PMCPMC5944345
OpenAlexW2781244726

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.