Evidence map›Paper›PMID 30618247›Full record

ArticleJournal of the American Chemical Society2019

Solid-State NMR and MD Study of the Structure of the Statherin Mutant SNa15 on Mineral Surfaces.

Erika L Buckle, Arushi Prakash, Massimiliano Bonomi, Janani Sampath, Jim Pfaendtner, Gary P Drobny

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 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
1.4field-weighted citation impact, top 23% 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, 20 citations in OpenAlex.

  1. Review
  2. Developments and Ongoing Challenges for Analysis of Surface-Bound Proteins.Annual review of analytical chemistry (Palo Alto, Calif.) · 2021
    Article
  3. Role of Water in CaCOJournal of the American Chemical Society · 2021
    Article
  4. Data-Driven Molecular Dynamics: A Multifaceted Challenge.Pharmaceuticals (Basel, Switzerland) · 2020
    Review
  5. Studies of Dynamic Binding of Amino Acids to TiOLangmuir : the ACS journal of surfaces and colloids · 2020
    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

6 authors at 2 institutions in 2 countries.

Erika L BuckleDepartment of Chemistry , University of Washington , Box 351700, Seattle , Washington 98195 , United States.
Arushi PrakashDepartment of Chemical Engineering , University of Washington , Seattle , Washington 98195 , United States.
Massimiliano BonomiStructural Bioinformatics Unit , Institut Pasteur , CNRS UMR 3528, 75015 Paris , France.
Janani SampathDepartment of Chemical Engineering , University of Washington , Seattle , Washington 98195 , United States.
Jim PfaendtnerDepartment of Chemical Engineering , University of Washington , Seattle , Washington 98195 , United States.ORCID 0000-0001-6727-2957
Gary P DrobnyDepartment of Chemistry , University of Washington , Box 351700, Seattle , Washington 98195 , United States.ORCID 0000-0002-7293-1897
University of Washington · USCentre National de la Recherche Scientifique · FR

Funding

Solution and Solid State NMR studies of Conformational Adaptation and Dynamics inR01GM109417 · NIGMS · UNIVERSITY OF WASHINGTON · PI DROBNY, GARY PETER · 2013 to 2016
$1.4M
NIGMS NIH HHS R01 GM109417
6 · The paper itself

Abstract

Elucidation of the structure and interactions of proteins at native mineral interfaces is key to understanding how biological systems regulate the formation of hard tissue structures. In addition, understanding how these same proteins interact with non-native mineral surfaces has important implications for the design of medical and dental implants, chromatographic supports, diagnostic tools, and a host of other applications. Here, we combine solid-state NMR spectroscopy, isotherm measurements, and molecular dynamics simulations to study how SNa15, a peptide derived from the hydroxyapatite (HAP) recognition domain of the biomineralization protein statherin, interacts with HAP, silica (SiO

Indexed as

Molecular Dynamics SimulationNuclear Magnetic Resonance, BiomolecularDurapatiteHumansMutationProtein ConformationSalivary Proteins and PeptidesSilicon DioxideTitaniumDurapatiteSalivary Proteins and PeptidesSilicon DioxideSTATH protein, humanTitaniumtitanium dioxide

Identifiers

PMID30618247
PMCPMC6785181
OpenAlexW2910395406

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.