Evidence map›Paper›PMID 26049759›Full record

ReviewCurrent opinion in hematology2015

The role of aberrant proteolysis in lymphomagenesis.

Anagh A Sahasrabuddhe, Kojo S J Elenitoba-Johnson

Abstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Current opinion in hematology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.3field-weighted citation impact, top 36% 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

2 citing papers in PubMed, 5 citations in OpenAlex.

  1. LBD: a manually curated database of experimentally validated lymphoma biomarkers.Database : the journal of biological databases and curation · 2022
    Article
  2. 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

2 authors at 1 institution in 1 country.

Anagh A SahasrabuddheDepartment of Pathology, University of Michigan, Ann Arbor, Michigan, USA.
Kojo S J Elenitoba-Johnson
University of Michigan–Ann Arbor · US

Funding

Mass spectrometry-driven systems biologic analysis of salivary MALT lymphomaR01DE019249 · NIDCR · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI ELENITOBA-JOHNSON, KOJO S. J. · 2008 to 2011
$1.5M
Proteomic analysis of api2-MALT1 positive gastric MALT lymphomaR01CA136905 · NCI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI ELENITOBA-JOHNSON, KOJO S. J. · 2009 to 2013
$1.4M
Quantitative proteomic analysis of lymphoma transformationR33CA112061 · NCI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI ELENITOBA-JOHNSON, KOJO S. J. · 2006 to 2008
$857k
NCI NIH HHS R01 CA136905NCI NIH HHS R33 CA112061NIDCR NIH HHS R01 DE019249NIDCR NIH HHS R01 DE119249
6 · The paper itself

Abstract

purpose of reviewDeregulated proteolysis is increasingly being implicated in pathogenesis of lymphoma. In this review, we highlight the major cellular processes that are affected by deregulated proteolysis of critical substrates that promote lymphoproliferative disorders. RECENT

findingsEmerging evidence supports the role of aberrant proteolysis by the ubiquitin proteasome system (UPS) in lymphoproliferative disorders. Several UPS mediators are identified to be altered in lymphomagenesis. However, the precise role of their alteration and comprehensive knowledge of their target substrate critical for lymphomagenesis is far from complete. SUMMARY: Many E3 ligase and deubiquitinases that contribute to regulated proteolysis of substrates critical for major cellular processes are altered in various lineages of lymphoma. Understanding of the proteolytic regulatory mechanisms of these major cellular pathways may offer novel biomarkers and targets for lymphoma therapy.

Indexed as

Gene Expression Regulation, NeoplasticCarcinogenesisCell Cycle ProteinsHumansLymphomaProteasome Endopeptidase ComplexProteolysisSignal TransductionTranscription FactorsUbiquitinUbiquitin-Protein LigasesUbiquitin-Specific ProteasesCell Cycle ProteinsProteasome Endopeptidase ComplexTranscription FactorsUbiquitinUbiquitin-Protein LigasesUbiquitin-Specific Proteases

Identifiers

PMID26049759
PMCPMC4459522
OpenAlexW2328350396

What OpenQuestion holds

Textmetadata
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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.