Evidence map›Paper›PMID 32693593›Full record

ArticleLangmuir : the ACS journal of surfaces and colloids2020

Studies of Dynamic Binding of Amino Acids to TiO

Mengjun Xue, Janani Sampath, Rachel N Gebhart, Havard J Haugen, S Petter Lyngstadaas, Jim Pfaendtner, Gary Drobny

Open access · greenAbstract read
In one paragraph

Article in Langmuir : the ACS journal of surfaces and colloids, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

10 citing papers in PubMed, 31 citations in OpenAlex.

  1. KRSR and RGD Adsorption on TiOBiomolecules · 2026
    Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Aggregation Properties of Albumin in Interacting with Magnetic Fluids.International journal of molecular sciences · 2021
    Article
  9. Article
  10. 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

7 authors at 2 institutions in 2 countries.

Mengjun XueDepartment of Chemistry, University of Washington, Box 351700, Seattle, Washington 98195, United States.
Janani SampathDepartment of Chemical Engineering, University of Washington, Box 351700, Seattle, Washington 98195, United States.
Rachel N GebhartDepartment of Chemistry, University of Washington, Box 351700, Seattle, Washington 98195, United States.
Havard J HaugenDepartment for Biomaterials, Faculty for Odontology, University of Oslo, P.O. Box 1109, Blindern, Oslo NO-0317, Norway.ORCID 0000-0002-6690-7233
S Petter LyngstadaasDepartment for Biomaterials, Faculty for Odontology, University of Oslo, P.O. Box 1109, Blindern, Oslo NO-0317, Norway.
Jim PfaendtnerDepartment of Chemical Engineering, University of Washington, Box 351700, Seattle, Washington 98195, United States.ORCID 0000-0001-6727-2957
Gary DrobnyDepartment of Chemistry, University of Washington, Box 351700, Seattle, Washington 98195, United States.ORCID 0000-0002-7293-1897
University of Washington · USUniversity of Oslo · NO

Funding

Dynamic Aspects of Nucleic Acid-Protein RecognitionR01EB003152 · NIBIB · UNIVERSITY OF WASHINGTON · PI DROBNY, GARY PETER · 2004 to 2011
$3.3M
Exploratory Solid State NMR Study of Protein-Metal Oxide InteractionsR21DE026959 · NIDCR · UNIVERSITY OF WASHINGTON · PI DROBNY, GARY PETER · 2017 to 2018
$425k
NASA NNX17AK86GNIBIB NIH HHS R01 EB003152NIDCR NIH HHS R21 DE026959
6 · The paper itself

Abstract

Adsorption of biomolecules onto material surfaces involves a potentially complex mechanism where molecular species interact to varying degrees with a heterogeneous material surface. Surface adsorption studies by atomic force microscopy, sum frequency generation spectroscopy, and solid-state NMR detect the structures and interactions of biomolecular species that are bound to material surfaces, which, in the absence of a solid-liquid interface, do not exchange rapidly between surface-bound forms and free molecular species in bulk solution. Solution NMR has the potential to complement these techniques by detecting and studying transiently bound biomolecules at the liquid-solid interface. Herein, we show that dark-state exchange saturation transfer (DEST) NMR experiments on gel-stabilized TiO

Indexed as

Molecular Dynamics SimulationNanoparticlesAdsorptionAmino AcidsSurface PropertiesTitaniumAmino AcidsTitaniumtitanium dioxide

Identifiers

PMID32693593
PMCPMC8098425
OpenAlexW3044046437

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.