Evidence map›Paper›PMID 29922723›Full record

ArticleBiochemistry and biophysics reports2018

Experimental and bioinformatic approach to identifying antigenic epitopes in human α- and β-enolases.

Jadwiga Pietkiewicz, Regina Danielewicz, Iwona S Bednarz-Misa, Ireneusz Ceremuga, Jerzy Wiśniewski, Magdalena Mierzchala-Pasierb, Agnieszka Bronowicka-Szydełko, Edmund Ziomek, Andrzej Gamian

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

Article in Biochemistry and biophysics reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact, top 95% 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

0 citing papers in PubMed, 1 citations in OpenAlex.

No citing paper in PubMed yet.

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 2 institutions in 1 country.

Jadwiga PietkiewiczDepartment of Medical Biochemistry, Wroclaw Medical University,Chalubinskiego 10, 50-368 Wroclaw, Poland.
Regina DanielewiczDepartment of Medical Biochemistry, Wroclaw Medical University,Chalubinskiego 10, 50-368 Wroclaw, Poland.
Iwona S Bednarz-MisaDepartment of Medical Biochemistry, Wroclaw Medical University,Chalubinskiego 10, 50-368 Wroclaw, Poland.
Ireneusz CeremugaDepartment of Medical Biochemistry, Wroclaw Medical University,Chalubinskiego 10, 50-368 Wroclaw, Poland.
Jerzy WiśniewskiDepartment of Medical Biochemistry, Wroclaw Medical University,Chalubinskiego 10, 50-368 Wroclaw, Poland.
Magdalena Mierzchala-PasierbDepartment of Medical Biochemistry, Wroclaw Medical University,Chalubinskiego 10, 50-368 Wroclaw, Poland.
Agnieszka Bronowicka-SzydełkoDepartment of Medical Biochemistry, Wroclaw Medical University,Chalubinskiego 10, 50-368 Wroclaw, Poland.
Edmund ZiomekWroclaw Research Center, Stablowicka 147, 50-066 Wroclaw, Poland.
Andrzej GamianDepartment of Medical Biochemistry, Wroclaw Medical University,Chalubinskiego 10, 50-368 Wroclaw, Poland.
Wroclaw Medical University · PLWroclaw Research Centre EIT+ (Poland) · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human α- and β-enolases are highly homologous enzymes, difficult to differentiate immunologically. In this work, we describe production, purification and properties of anti-α- and anti-β-enolase polyclonal antibodies. To raise antibodies, rabbits were injected with enolase isoenzymes that were purified from human kidney (α-enolase) and skeletal muscle (β-enolase). Selective anti-α- and anti-β-enolase antibodies were obtained by affinity chromatography on either α- or β-enolase-Sepharose columns. On Western blots, antibodies directed against human β-enolase, did not react with human α-isoenzyme, but recognized pig and rat β-enolase. To determine what makes these antibodies selective bioinformatic tools were used to predict conformational epitopes for both enolase isoenzymes. Three predicted epitopes were mapped to the same regions in both α- and β-enolase. Peptides corresponding to predicted epitopes were synthesized and tested against purified antibodies. One of the pin-attached peptides representing α-enolase epitope (the C-terminal portion of the epitope 3 - S

Indexed as

AP, alkaline phosphataseBSA, bovine serum albuminCross-reactivityELISA, enzyme-linked immunosorbent assayEnolase purificationEpitope predictionESI, electrospray injectionHRP, horse radish peroxidaseIgG, immunoglobulin GLC, liquid chromatographyMass spectrometryMeOH, methanolMS, mass spectrometryOPD, ortho-phenylenediaminePAGE, polyacrylamide gel electrophoresisPBS, phosphate buffered salinePMSF, phenylmethylsulfonyl fluoridepNPP, para-nitrophenyl phosphateSDS, sodium dodecylsulfateSpecific antibodiesTBST, 20 mM Tris, pH 7.4, 150 mM NaCl, 0.05% Tween-20UPLC-Q-TOF-MS, ultrapressure liquid chromatography, quadrupole-time-of-flight mass spectrometerWB, western blotting

Identifiers

PMID29922723
PMCPMC6005794
OpenAlexW2808357439

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.