Evidence map›Paper›PMID 27419667›Full record

ArticleProtein science : a publication of the Protein Society2016

An insight into the thermodynamic characteristics of human thrombopoietin complexation with TN1 antibody.

Shigeki Arai, Chie Shibazaki, Motoyasu Adachi, Eijiro Honjo, Taro Tamada, Yoshitake Maeda, Tomoyuki Tahara, Takashi Kato, Hiroshi Miyazaki, Michael Blaber and 1 more

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

Article in Protein science : a publication of the Protein Society, 2016. 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
0.2field-weighted citation impact, top 37% 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. 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

11 authors at 5 institutions in 2 countries.

Shigeki AraiQuantum Beam Science Research Directorate, National Institutes for Quantum and Radiological Science and Technology, 2-4 Shirakata, Tokai, Ibaraki, 319-1106, Japan. arai.shigeki@qst.go.jp.
Chie ShibazakiQuantum Beam Science Research Directorate, National Institutes for Quantum and Radiological Science and Technology, 2-4 Shirakata, Tokai, Ibaraki, 319-1106, Japan.
Motoyasu AdachiQuantum Beam Science Research Directorate, National Institutes for Quantum and Radiological Science and Technology, 2-4 Shirakata, Tokai, Ibaraki, 319-1106, Japan.
Eijiro HonjoQuantum Beam Science Research Directorate, National Institutes for Quantum and Radiological Science and Technology, 2-4 Shirakata, Tokai, Ibaraki, 319-1106, Japan.
Taro TamadaQuantum Beam Science Research Directorate, National Institutes for Quantum and Radiological Science and Technology, 2-4 Shirakata, Tokai, Ibaraki, 319-1106, Japan.
Yoshitake MaedaKyowa Hakko Kirin Co. Ltd, 3-6-6 Asahi-Cho, Machida, Tokyo, 194-8533, Japan.
Tomoyuki TaharaKyowa Hakko Kirin Co. Ltd, 3-6-6 Asahi-Cho, Machida, Tokyo, 194-8533, Japan.
Takashi KatoDepartment of Biology, Faculty of Education and Integrated Arts and Sciences, Waseda University, 2-2 Wakamatsu, Shinjuku, Tokyo, 162-8480, Japan.
Hiroshi MiyazakiDepartment of Innovative Drug Discovery and Development, Japan Agency for Medical Research and Development, 1-5-5 Nihonbashi-muromachi, Chuo, Tokyo, 103-0022, Japan.
Michael BlaberCollege of Medicine, Florida State University, 1115 West Call Street, Tallahassee, Florida, 32306-4300, USA.
Ryota KurokiQuantum Beam Science Research Directorate, National Institutes for Quantum and Radiological Science and Technology, 2-4 Shirakata, Tokai, Ibaraki, 319-1106, Japan.
National Institutes for Quantum and Radiological Science and Technology · JPKyowa Kirin (Japan) · JPFlorida State University · USJapan Agency for Medical Research and Development · JPWaseda University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human thrombopoietin (hTPO) primarily stimulates megakaryocytopoiesis and platelet production and is neutralized by the mouse TN1 antibody. The thermodynamic characteristics of TN1 antibody-hTPO complexation were analyzed by isothermal titration calorimetry (ITC) using an antigen-binding fragment (Fab) derived from the TN1 antibody (TN1-Fab). To clarify the mechanism by which hTPO is recognized by TN1-Fab the conformation of free TN1-Fab was determined to a resolution of 2.0 Å using X-ray crystallography and compared with the hTPO-bound form of TN1-Fab determined by a previous study. This structural comparison revealed that the conformation of TN1-Fab does not substantially change after hTPO binding and a set of 15 water molecules is released from the antigen-binding site (paratope) of TN1-Fab upon hTPO complexation. Interestingly, the heat capacity change (ΔCp) measured by ITC (-1.52 ± 0.05 kJ mol(-1)  K(-1) ) differed significantly from calculations based upon the X-ray structure data of the hTPO-bound and unbound forms of TN1-Fab (-1.02 ∼ 0.25 kJ mol(-1)  K(-1) ) suggesting that hTPO undergoes an induced-fit conformational change combined with significant desolvation upon TN1-Fab binding. The results shed light on the structural biology associated with neutralizing antibody recognition.

Indexed as

AnimalsAntibodies, Monoclonal, Murine-DerivedCrystallography, X-RayHumansImmunoglobulin Fab FragmentsMiceProtein Structure, QuaternaryThermodynamicsThrombopoietinAntibodies, Monoclonal, Murine-DerivedImmunoglobulin Fab FragmentsThrombopoietinantigen-antibody interactionisothermal titration calorimetrythrombopoietinTN1X-ray crystallography

Identifiers

PMID27419667
PMCPMC5029525
OpenAlexW2486843362

What OpenQuestion holds

Textmetadata
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.