Evidence map›Paper›PMID 34948188›Full record

ArticleInternational journal of molecular sciences2021

X-ray Characterization of Conformational Changes of Human Apo- and Holo-Transferrin.

Camila Campos-Escamilla, Dritan Siliqi, Luis A Gonzalez-Ramirez, Carmen Lopez-Sanchez, Jose Antonio Gavira, Abel Moreno

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.9field-weighted citation impact, top 29% 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

4 citing papers in PubMed, 13 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. 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 3 institutions in 3 countries.

Camila Campos-EscamillaInstituto de Química, Universidad Nacional Autónoma de Mexico, Av. Universidad 3000, Ciudad Universitaria, Ciudad de Mexico 04510, Mexico.ORCID 0000-0002-7219-0494
Dritan SiliqiIstitituto di Cristallografia (IC), National Research Council (CNR), Via Amendola 122/O, 70126 Bari, Italy.ORCID 0000-0003-1415-8725
Luis A Gonzalez-RamirezLaboratorio de Estudios Cristalográficos, Instituto Andaluz de Ciencias de la Tierra, C.S.I.C. University of Granada, Avenida de las Palmeras No. 4, 18100 Armilla, Granada, Spain.ORCID 0000-0001-9179-1140
Carmen Lopez-SanchezLaboratorio de Estudios Cristalográficos, Instituto Andaluz de Ciencias de la Tierra, C.S.I.C. University of Granada, Avenida de las Palmeras No. 4, 18100 Armilla, Granada, Spain.
Jose Antonio GaviraLaboratorio de Estudios Cristalográficos, Instituto Andaluz de Ciencias de la Tierra, C.S.I.C. University of Granada, Avenida de las Palmeras No. 4, 18100 Armilla, Granada, Spain.ORCID 0000-0002-7386-6484
Abel MorenoInstituto de Química, Universidad Nacional Autónoma de Mexico, Av. Universidad 3000, Ciudad Universitaria, Ciudad de Mexico 04510, Mexico.ORCID 0000-0002-5810-078X
Universidad de Granada · ESNational Research Council · ITUniversidad Nacional Autónoma de México · MX

Funding

A Synchrotron Radiation Structural Biology ResourcesP30GM133894 · NIGMS · STANFORD UNIVERSITY · PI Aina E. Cohen, KEITH O HODGSON · 2020 to 2026
$43.3M
NIGMS NIH HHS P30 GM133894
6 · The paper itself

Abstract

Human serum transferrin (Tf) is a bilobed glycoprotein whose function is to transport iron through receptor-mediated endocytosis. The mechanism for iron release is pH-dependent and involves conformational changes in the protein, thus making it an attractive system for possible biomedical applications. In this contribution, two powerful X-ray techniques, namely Macromolecular X-ray Crystallography (MX) and Small Angle X-ray Scattering (SAXS), were used to study the conformational changes of iron-free (apo) and iron-loaded (holo) transferrin in crystal and solution states, respectively, at three different pH values of physiological relevance. A crystallographic model of glycosylated apo-Tf was obtained at 3.0 Å resolution, which did not resolve further despite many efforts to improve crystal quality. In the solution, apo-Tf remained mostly globular in all the pH conditions tested; however, the co-existence of closed, partially open, and open conformations was observed for holo-Tf, which showed a more elongated and flexible shape overall.

Indexed as

Binding SitesCrystallography, X-RayGlycosylationHumansHydrogen-Ion ConcentrationIronModels, MolecularProtein BindingProtein ConformationScattering, Small AngleSerumTransferrinX-Ray DiffractionIronTransferrinconformation changehuman serum transferrinpH-dependenceSmall-Angle X-ray ScatteringX-ray Crystallography

Identifiers

PMID34948188
PMCPMC8705962
OpenAlexW4200115907

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.