Evidence map›Paper›PMID 35538994›Full record

ArticleRSC advances2018

Mapping molecular binding by means of conformational dynamics measurements.

Noelle M do Nascimento, Augusto Juste-Dolz, Paulo R Bueno, Isidro Monzó, Roberto Tejero, José L Lopez-Paz, Angel Maquieira, Sergi Morais, David Gimenez-Romero

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in RSC advances, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.5field-weighted citation impact, top 33% 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

1 citing paper in PubMed, 4 citations in OpenAlex.

  1. Review
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

9 authors at 3 institutions in 2 countries.

Noelle M do NascimentoInstituto Interuniversitario de Investigación de Reconocimiento Molecular y Desarrollo Tecnológico, Departamento de Química, Universitat Politècnica de València Camino de Vera s/n Valencia 46022 Spain.
Augusto Juste-DolzInstituto Interuniversitario de Investigación de Reconocimiento Molecular y Desarrollo Tecnológico, Departamento de Química, Universitat Politècnica de València Camino de Vera s/n Valencia 46022 Spain.
Paulo R BuenoInstituto de Química, Univ. Estadual Paulista (UNESP), Departamento de Físico-Química, Nanobionics Research Group Araraquara São Paulo Brazil http://www.nanobionics.pro.br.ORCID https://orcid.org/0000-0003-2827-0208
Isidro MonzóDepartamento de Química-Física, Universitat de València C/Dr Moliner 50 46100 Burjassot Spain giroda@uv.es.
Roberto TejeroDepartamento de Química-Física, Universitat de València C/Dr Moliner 50 46100 Burjassot Spain giroda@uv.es.
José L Lopez-PazInstituto Interuniversitario de Investigación de Reconocimiento Molecular y Desarrollo Tecnológico, Departamento de Química, Universitat Politècnica de València Camino de Vera s/n Valencia 46022 Spain.ORCID https://orcid.org/0000-0003-4015-4357
Angel MaquieiraInstituto Interuniversitario de Investigación de Reconocimiento Molecular y Desarrollo Tecnológico, Departamento de Química, Universitat Politècnica de València Camino de Vera s/n Valencia 46022 Spain.
Sergi MoraisInstituto Interuniversitario de Investigación de Reconocimiento Molecular y Desarrollo Tecnológico, Departamento de Química, Universitat Politècnica de València Camino de Vera s/n Valencia 46022 Spain.
David Gimenez-RomeroDepartamento de Química-Física, Universitat de València C/Dr Moliner 50 46100 Burjassot Spain giroda@uv.es.ORCID https://orcid.org/0000-0001-6489-9308
Universitat Politècnica de València · ESUniversitat de València · ESCentro Universitário de Araraquara · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein-protein interactions are key in virtually all biological processes. The study of these interactions and the interfaces that mediate them play a key role in the understanding of biological function. In particular, the observation of protein-protein interactions in their dynamic environment is technically difficult. Here two surface analysis techniques, dual polarization interferometry and quartz crystal microbalance with dissipation monitoring, were paired for real-time mapping of the conformational dynamics of protein-protein interactions. Our approach monitors this dynamics in real time and

Identifiers

PMID35538994
PMCPMC9076986
OpenAlexW2781772148

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.