ArticleScientific reports2016
In situ characterization of protein aggregates in human tissues affected by light chain amyloidosis: a FTIR microspectroscopy study.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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.
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.
Who cites it
35 citing papers in PubMed, 81 citations in OpenAlex.
- Label-free protein-structure-sensitive live-cell microscopy for patient-specific assessment of myeloma therapy.Nature biomedical engineering · 2026Article
- Lipid mediated formation of antiparallel aggregates in cerebral amyloid angiopathy.Acta neuropathologica · 2025Article
- Intraepineurial Fat Fraction: A Novel MR Neurography-Based Biomarker in Transthyretin Amyloidosis Polyneuropathy.European journal of neurology · 2025Article
- Pilot Study on the Use of Attenuated Total Reflectance-Fourier Transform Infrared Spectroscopy for Diagnosing and Characterizing Cardiac Amyloidosis.International journal of molecular sciences · 2024Article
- Characterizing the amyloid core region of the tumor suppressor protein p16The Journal of biological chemistry · 2024Article
- AnAnnals of medicine · 2023Article
- A Linear Predictor Based on FTIR Spectral Biomarkers Improves Disease Diagnosis Classification: An Application to Multiple Sclerosis.Journal of personalized medicine · 2023Article
- Hyperspectral Raman Imaging for Automated Recognition of Human Renal Amyloid.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2023Article
- Recombinant protein embedded liposome on gold nanoparticle based on LSPR method to detect Corona virus.Nano convergence · 2023Article
- Non-Perturbative Identification and Subtyping of Amyloidosis in Human Kidney Tissue with Raman Spectroscopy and Machine Learning.Biosensors · 2023Article
- ATR-FTIR spectroscopy of plasma supported by multivariate analysis discriminates multiple sclerosis disease.Scientific reports · 2023Article
- Consideration of a new approach to clarify the mechanism formation of AgNPs, AgNCl and AgNPs@AgNCl synthesized by biological method.Discover nano · 2023Article
- The UCMD-CausingHuman mutation · 2023Article
- Role of the mechanisms for antibody repertoire diversification in monoclonal light chain deposition disorders: when a friend becomes foe.Frontiers in immunology · 2023Review
- Methodological advances and strategies for high resolution structure determination of cellular protein aggregates.The Journal of biological chemistry · 2022Review
- Pathophysiological Response to SARS-CoV-2 Infection Detected by Infrared Spectroscopy Enables Rapid and Robust Saliva Screening for COVID-19.Biomedicines · 2022Article
- Characterization of the Conformational Properties of Soluble and Insoluble Proteins by Fourier Transform Infrared Spectroscopy.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Contribution of Infrared Spectroscopy to the Understanding of Amyloid Protein Aggregation in Complex Systems.Frontiers in molecular biosciences · 2022Review
- Article
- Dissecting the Molecular Features of Systemic Light Chain (AL) Amyloidosis: Contributions from Proteomics.Medicina (Kaunas, Lithuania) · 2021Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Light chain (AL) amyloidosis, caused by deposition of amyloidogenic immunoglobulin light chains (LCs), is the most common systemic form in industrialized countries. Still open questions, and premises for developing targeted therapies, concern the mechanisms of amyloid formation in vivo and the bases of organ targeting and dysfunction. Investigating amyloid material in its natural environment is crucial to obtain new insights on the molecular features of fibrillar deposits at individual level. To this aim, we used Fourier transform infrared (FTIR) microspectroscopy for studying in situ unfixed tissues (heart and subcutaneous abdominal fat) from patients affected by AL amyloidosis. We compared the infrared response of affected tissues with that of ex vivo and in vitro fibrils obtained from the pathogenic LC derived from one patient, as well as with that of non amyloid-affected tissues. We demonstrated that the IR marker band of intermolecular β-sheets, typical of protein aggregates, can be detected in situ in LC amyloid-affected tissues, and that FTIR microspectroscopy allows exploring the inter- and intra-sample heterogeneity. We extended the infrared analysis to the characterization of other biomolecules embedded within the amyloid deposits, finding an IR pattern that discloses a possible role of lipids, collagen and glycosaminoglycans in amyloid deposition in vivo.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.