Evidence map›Paper›PMID 34885818›Full record

ArticleMolecules (Basel, Switzerland)2021

A Pilot Study of Rare Renal Amyloidosis Based on FFPE Proteomics.

Shuang Meng, Wenwen Xia, Li Xia, Li Zhou, Jing Xu, Xiaoxia Pan, Liyuan Meng

Abstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Review
  3. 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

7 authors.

Shuang MengDepartment of Core Facility of Basic Medical Sciences, Shanghai Jiao Tong University School of Basic Medicine, Shanghai 200025, China.
Wenwen XiaDepartment of Pathology, Ninth People's Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai 200011, China.
Li XiaDepartment of Core Facility of Basic Medical Sciences, Shanghai Jiao Tong University School of Basic Medicine, Shanghai 200025, China.
Li ZhouDepartment of Core Facility of Basic Medical Sciences, Shanghai Jiao Tong University School of Basic Medicine, Shanghai 200025, China.
Jing XuDepartment of Nephrology, Ruijin Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai 200025, China.
Xiaoxia PanDepartment of Nephrology, Ruijin Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai 200025, China.
Liyuan MengDepartment of Core Facility of Basic Medical Sciences, Shanghai Jiao Tong University School of Basic Medicine, Shanghai 200025, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Renal amyloidosis typically manifests albuminuria, nephrotic-range proteinuria, and ultimately progresses to end-stage renal failure if diagnosed late. Different types of renal amyloidosis have completely different treatments and outcomes. Therefore, amyloidosis typing is essential for disease prognosis, genetic counseling and treatment. Thirty-six distinct proteins currently known to cause amyloidosis that have been described as amyloidogenic precursors, immunohistochemistry (IHC) or immunofluorescence (IF), can be challenging for amyloidosis typing especially in rare or hereditary amyloidosis in clinical practice. We made a pilot study that optimized the proteomics pre-processing procedures for trace renal amyloidosis formalin-fixed paraffin-embedded (FFPE) tissue samples, combined with statistical and bioinformatics analysis to screen out the amyloidosis-related proteins to accurately type or subtype renal amyloidosis in order to achieve individual treatment. A sensitive, specific and reliable FFPE-based proteomics analysis for trace sample manipulation was developed for amyloidosis typing. Our results not only underlined the great promise of traditional proteomics and bioinformatics analysis using FFPE tissues for amyloidosis typing, but also proved that retrospective diagnosis and analysis of previous cases laid a solid foundation for personalized treatment.

Indexed as

Paraffin EmbeddingProteomicsTissue FixationAmyloidosisBase SequenceCase-Control StudiesFormaldehydeHumansKidneyMass SpectrometryMuramidasePilot ProjectsFormaldehydeMuramidaseFFPEimmunoglobulin light chain amyloidosis (AL)lysozyme amyloidosis (ALys)proteomicsrenal amyloidosis

Identifiers

PMID34885818
PMCPMC8659071

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.