Evidence map›Paper›PMID 25724648›Full record

ArticleThe Journal of biological chemistry2015

Specific amyloid β clearance by a catalytic antibody construct.

Stephanie A Planque, Yasuhiro Nishiyama, Sari Sonoda, Yan Lin, Hiroaki Taguchi, Mariko Hara, Steven Kolodziej, Yukie Mitsuda, Veronica Gonzalez, Hameetha B R Sait and 6 more

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
–field-weighted citation impact
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

15 citing papers in PubMed.

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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

16 authors.

Stephanie A PlanqueFrom the Chemical Immunology Research Center, Department of Pathology and Laboratory Medicine, University of Texas-Houston Medical School, Houston, Texas 77030.
Yasuhiro NishiyamaFrom the Chemical Immunology Research Center, Department of Pathology and Laboratory Medicine, University of Texas-Houston Medical School, Houston, Texas 77030.
Sari SonodaFrom the Chemical Immunology Research Center, Department of Pathology and Laboratory Medicine, University of Texas-Houston Medical School, Houston, Texas 77030.
Yan Linthe Departments of Neuroscience, Physiology, and Psychiatry, New York University School of Medicine, New York, New York 10016.
Hiroaki TaguchiFrom the Chemical Immunology Research Center, Department of Pathology and Laboratory Medicine, University of Texas-Houston Medical School, Houston, Texas 77030.
Mariko HaraFrom the Chemical Immunology Research Center, Department of Pathology and Laboratory Medicine, University of Texas-Houston Medical School, Houston, Texas 77030.
Steven KolodziejFrom the Chemical Immunology Research Center, Department of Pathology and Laboratory Medicine, University of Texas-Houston Medical School, Houston, Texas 77030.
Yukie MitsudaFrom the Chemical Immunology Research Center, Department of Pathology and Laboratory Medicine, University of Texas-Houston Medical School, Houston, Texas 77030.
Veronica Gonzalezthe Departments of Neuroscience, Physiology, and Psychiatry, New York University School of Medicine, New York, New York 10016.
Hameetha B R Saitthe Departments of Neuroscience, Physiology, and Psychiatry, New York University School of Medicine, New York, New York 10016.
Ken-ichiro Fukuchithe Department of Cancer Biology and Pharmacology, University of Illinois College of Medicine, Peoria, Illinois 61605.
Richard J MasseyCovalent Bioscience Inc., Houston, Texas 77054.
Robert P Friedlandthe Department of Neurology, University of Louisville School of Medicine, Louisville, Kentucky 40202, and.
Brian O'Nuallainthe Center for Neurologic Diseases, Brigham and Women's Hospital and Harvard Medical School, Boston, Massachusetts 02115.
Einar M Sigurdssonthe Departments of Neuroscience, Physiology, and Psychiatry, New York University School of Medicine, New York, New York 10016, Einar.Sigurdsson@nyumc.org.
Sudhir PaulFrom the Chemical Immunology Research Center, Department of Pathology and Laboratory Medicine, University of Texas-Houston Medical School, Houston, Texas 77030, Sudhir.Paul@uth.tmc.edu.

Funding

Center for Clinical and Translational Sciences (CCTS)UL1TR000371 · NCATS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI MCPHERSON, DAVID D · 2012 to 2016
$13.4M
Research Supplement to Promote Diversity in Health-Related ResearchR01AG032611 · NIA · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI Einar M Sigurdsson · 2008 to 2026
$9.7M
Epitope-Specific Targeting of Tau Aggregates.R01NS077239 · NINDS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI Einar M Sigurdsson · 2011 to 2026
$7.9M
Immune Therapy for AD plaques and Tangles in Tg MiceR01AG020197 · NIA · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI SIGURDSSON, EINAR M · 2001 to 2013
$2.8M
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
NCATS NIH HHS UL1 TR000371NIA NIH HHS 5U01AG033183NIA NIH HHS R01 AG020197NIA NIH HHS R01AG020197NIA NIH HHS R01 AG025304NIA NIH HHS R01AG025304NIA NIH HHS R01 AG032611NIA NIH HHS U01 AG033183NINDS NIH HHS R01 NS077239
6 · The paper itself

Abstract

Classical immunization methods do not generate catalytic antibodies (catabodies), but recent findings suggest that the innate antibody repertoire is a rich catabody source. We describe the specificity and amyloid β (Aβ)-clearing effect of a catabody construct engineered from innate immunity principles. The catabody recognized the Aβ C terminus noncovalently and hydrolyzed Aβ rapidly, with no reactivity to the Aβ precursor protein, transthyretin amyloid aggregates, or irrelevant proteins containing the catabody-sensitive Aβ dipeptide unit. The catabody dissolved preformed Aβ aggregates and inhibited Aβ aggregation more potently than an Aβ-binding IgG. Intravenous catabody treatment reduced brain Aβ deposits in a mouse Alzheimer disease model without inducing microgliosis or microhemorrhages. Specific Aβ hydrolysis appears to be an innate immune function that could be applied for therapeutic Aβ removal.

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesAnimalsAntibodies, CatalyticBrainDisease Models, AnimalGene ExpressionHEK293 CellsHumansHydrolysisImmunity, InnateMicePeptide FragmentsProtein EngineeringProteolysisRecombinant ProteinsAmyloid beta-PeptidesAntibodies, CatalyticPeptide FragmentsRecombinant ProteinsSingle-Chain AntibodiesAlzheimer DiseaseAmyloid-β (Abeta)Antibody EngineeringCatalytic AntibodiesEnzyme CatalysisImmunotherapyInnate ImmunityLight Chain Variable DomainNeurotoxicity

Identifiers

PMID25724648
PMCPMC4400338

What OpenQuestion holds

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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.