Evidence map›Paper›PMID 24648510›Full record

Trial reportThe Journal of biological chemistry2014

Physiological IgM class catalytic antibodies selective for transthyretin amyloid.

Stephanie A Planque, Yasuhiro Nishiyama, Mariko Hara, Sari Sonoda, Sarah K Murphy, Kenji Watanabe, Yukie Mitsuda, Eric L Brown, Richard J Massey, Stanley R Primmer and 2 more

Open access · hybridAbstract readClinical Trial
In one paragraph

Trial report in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed, 1 pooled it
4.6field-weighted citation impact, top 6% 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

28 citing papers in PubMed, 1 synthesis or guideline pooled it, 53 citations in OpenAlex.

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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

12 authors at 3 institutions in 1 country.

Stephanie A PlanqueFrom the Chemical Immunology Research Center, Department of Pathology and Laboratory Medicine, University of Texas-Houston Medical School, Houston, Texas 77030.
Yasuhiro Nishiyama
Mariko Hara
Sari Sonoda
Sarah K Murphy
Kenji Watanabe
Yukie Mitsuda
Eric L Brown
Richard J Massey
Stanley R Primmer
Brian O'Nuallain
Sudhir Paul
The University of Texas Health Science Center at Houston · USBrigham and Women's Hospital · USValent BioSciences (United States) · US

Funding

Tumor BiologyP30CA125123 · NCI · BAYLOR COLLEGE OF MEDICINE · PI Suzanne AW Fuqua · 2007 to 2026
$73.9M
Virology CoreP30AI036211 · NIAID · BAYLOR COLLEGE OF MEDICINE · PI RICE, ANDREW P · 1994 to 2015
$21.7M
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
Efficacious and safe antibody catalyzed amyloid beta clearanceU01AG033183 · NIA · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI PAUL, SUDHIR · 2010 to 2014
$2.0M
BD Biosciences Special Order LSRIIS10RR024574 · NCRR · BAYLOR COLLEGE OF MEDICINE · PI LUMPKIN, ELLEN A · 2009 to 2009
$430k
Catalytic Antibodies To Staphylococcus Aureus: Identification and CharacterizatioR21AI072439 · NIAID · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI BROWN, ERIC L · 2009 to 2010
$413k
NCATS NIH HHS UL1 TR000371NCI NIH HHS P30 CA125123NCI NIH HHS P30CA125123NCRR NIH HHS S10 RR024574NCRR NIH HHS S10RR024574NIAID NIH HHS AI036211NIAID NIH HHS P30 AI036211NIAID NIH HHS R21 AI072439NIA NIH HHS U01 AG033183NIA NIH HHS U01AG033183
6 · The paper itself

Abstract

Peptide bond-hydrolyzing catalytic antibodies (catabodies) could degrade toxic proteins, but acquired immunity principles have not provided evidence for beneficial catabodies. Transthyretin (TTR) forms misfolded β-sheet aggregates responsible for age-associated amyloidosis. We describe nucleophilic catabodies from healthy humans without amyloidosis that degraded misfolded TTR (misTTR) without reactivity to the physiological tetrameric TTR (phyTTR). IgM class B cell receptors specifically recognized the electrophilic analog of misTTR but not phyTTR. IgM but not IgG class antibodies hydrolyzed the particulate and soluble misTTR species. No misTTR-IgM binding was detected. The IgMs accounted for essentially all of the misTTR hydrolytic activity of unfractionated human serum. The IgMs did not degrade non-amyloidogenic, non-superantigenic proteins. Individual monoclonal IgMs (mIgMs) expressed variable misTTR hydrolytic rates and differing oligoreactivity directed to amyloid β peptide and microbial superantigen proteins. A subset of the mIgMs was monoreactive for misTTR. Excess misTTR was dissolved by a hydrolytic mIgM. The studies reveal a novel antibody property, the innate ability of IgMs to selectively degrade and dissolve toxic misTTR species as a first line immune function.

Indexed as

ProteolysisAdultAmyloidAntibodies, CatalyticAntibody SpecificityFemaleHumansImmunoglobulin MMalePrealbuminAmyloidAntibodies, CatalyticImmunoglobulin MPrealbuminAgingAmyloidAmyloidosisAntibodiesCatalytic AntibodyInnate ImmunityProtein EvolutionSuperantigenTransthyretin

Identifiers

PMID24648510
PMCPMC4036335
OpenAlexW2050613453

What Socratic 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 Socratic graph.