Evidence map›Paper›PMID 24698848›Full record

ArticleJournal of biotechnology2014

Metal-dependent amyloid β-degrading catalytic antibody construct.

Yasuhiro Nishiyama, Hiroaki Taguchi, Mariko Hara, Stephanie A Planque, Yukie Mitsuda, Sudhir Paul

Abstract read
In one paragraph

Article in Journal of biotechnology, 2014. 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
3.5field-weighted citation impact, top 8% 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, 22 citations in OpenAlex.

  1. Review
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  9. Review
  10. Specific amyloid β clearance by a catalytic antibody construct.The Journal of biological chemistry · 2015
    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 1 institution in 1 country.

Yasuhiro NishiyamaChemical Immunology Research Center, Department of Pathology and Laboratory Medicine, University of Texas-Houston Medical School, Houston, TX 77030, USA.
Hiroaki TaguchiChemical Immunology Research Center, Department of Pathology and Laboratory Medicine, University of Texas-Houston Medical School, Houston, TX 77030, USA.
Mariko HaraChemical Immunology Research Center, Department of Pathology and Laboratory Medicine, University of Texas-Houston Medical School, Houston, TX 77030, USA.
Stephanie A PlanqueChemical Immunology Research Center, Department of Pathology and Laboratory Medicine, University of Texas-Houston Medical School, Houston, TX 77030, USA.
Yukie MitsudaChemical Immunology Research Center, Department of Pathology and Laboratory Medicine, University of Texas-Houston Medical School, Houston, TX 77030, USA.
Sudhir PaulChemical Immunology Research Center, Department of Pathology and Laboratory Medicine, University of Texas-Houston Medical School, Houston, TX 77030, USA. Electronic address: Sudhir.Paul@uth.tmc.edu.
The University of Texas Health Science Center at Houston · US

Funding

Efficacious and safe antibody catalyzed amyloid beta clearanceU01AG033183 · NIA · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI PAUL, SUDHIR · 2010 to 2014
$2.0M
beta-Amyloid Antibodies w/ Specific Proteolytic ActivityR01AG025304 · NIA · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI PAUL, SUDHIR · 2005 to 2008
$1.5M
NIA NIH HHS R01 AG025304NIA NIH HHS R01AG025304NIA NIH HHS U01 AG033183NIA NIH HHS U01AG033183
6 · The paper itself

Abstract

Catalytic antibodies (catabodies) that degrade target antigens rapidly are rare. We describe the metal-dependence of catabody construct 2E6, an engineered heterodimer of immunoglobulin light chain variable domains that hydrolyzes amyloid β peptides (Aβ) specifically. In addition to the electrophilic phosphonate inhibitor of serine proteases, the metal chelators ethylenediaminetetraacetic acid (EDTA) and 1,10-phenanthroline completely inhibited the hydrolysis of Aβ by catabody 2E6. Formation of catabody-electrophilic phosphonate inhibitor adducts was unaffected by EDTA, suggesting that the metal exerts a favorable effect on a catalytic step after the initial catabody nucleophilic attack on Aβ. The EDTA inactivated catabody failed to disaggregate fibrillar Aβ, indicating the functional importance of the Aβ hydrolytic activity. Treating the EDTA-inactivated catabody with Zn(2+) or Co(2+) restored the Aβ hydrolytic activity, and Zn(2+)-induced catabody conformational transitions were evident by fluorescence emission spectroscopy. The studies reveal the absolute catabody dependence on a metal cofactor.

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesAntibodies, CatalyticChelating AgentsCopperEdetic AcidHumansHydrolysisZincAmyloid beta-PeptidesAntibodies, CatalyticChelating AgentsCopperEdetic AcidZincAlzheimer diseaseAmyloid β clearanceCatalytic antibody light chainMetal activation

Identifiers

PMID24698848
PMCPMC4512298
OpenAlexW2073116513

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.