Evidence map›Paper›PMID 30861211›Full record

ArticleChemistry (Weinheim an der Bergstrasse, Germany)2019

How Outer Coordination Sphere Modifications Can Impact Metal Structures in Proteins: A Crystallographic Evaluation.

Leela Ruckthong, Jeanne A Stuckey, Vincent L Pecoraro

Open access · greenAbstract read
In one paragraph

Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.0field-weighted citation impact, top 22% 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

7 citing papers in PubMed, 12 citations in OpenAlex.

  1. Review
  2. Article
  3. Catalysis and Electron Transfer inChemical reviews · 2022
    Review
  4. De novo metalloprotein design.Nature reviews. Chemistry · 2022
    Article
  5. Article
  6. Article
  7. 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

3 authors at 1 institution in 2 countries.

Leela RuckthongDepartment of Chemistry, University of Michigan, Ann Arbor, Michigan, 48109, USA.ORCID http://orcid.org/0000-0001-9352-2534
Jeanne A StuckeyLife Sciences Institute, University of Michigan, Ann Arbor, Michigan, 48109, USA.ORCID http://orcid.org/0000-0002-4192-8900
Vincent L PecoraroDepartment of Chemistry, University of Michigan, Ann Arbor, Michigan, 48109, USA.ORCID http://orcid.org/0000-0002-1540-5735
University of Michigan · US

Funding

Toxic Metal Complexation By de Novo Designed PeptidesR01ES012236 · NIEHS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI PECORARO, VINCENT L · 2003 to 2018
$4.4M
Foundation for the National Institutes of Health ES012236Michigan Economic Development Corporation 085P1000817NIEHS NIH HHS R01 ES012236The Royal Thai Government Funding, ThailandThe Skill Development Grant, King Mongkut's University of Technology Thonburi, Thailand
6 · The paper itself

Abstract

A challenging objective of de novo metalloprotein design is to control of the outer coordination spheres of an active site to fine tune metal properties. The well-defined three stranded coiled coils, TRI and CoilSer peptides, are used to address this question. Substitution of Cys for Leu yields a thiophilic site within the core. Metals such as Hg

Indexed as

d-amino acidsde novo protein engineeringmetalloprotein engineeringnonnatural amino acids

Identifiers

PMID30861211
PMCPMC6510599
OpenAlexW2921833319

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.