Amyloid-Journal of Protein Folding Disorders最新文献_第6页

Lysozyme as an amyloid fibril protein together with transthyretin in the ligamentum flavum in association with lumbar spinal stenosis. 溶菌酶作为淀粉样纤维蛋白与转甲状腺素在黄韧带中与腰椎管狭窄相关。

IF 5.1 2区医学

Amyloid-Journal of Protein Folding Disorders Pub Date : 2026-06-01 Epub Date: 2026-02-26 DOI: 10.1080/13506129.2026.2635090

Gunilla Westermark, Svante Berg, Per Eldhagen, Justina Damjanovic Vesterlund, Ulrika Thelander, Elin Persson, Jonas Bergquist, Per Westermark

{"title":"Lysozyme as an amyloid fibril protein together with transthyretin in the ligamentum flavum in association with lumbar spinal stenosis.","authors":"Gunilla Westermark, Svante Berg, Per Eldhagen, Justina Damjanovic Vesterlund, Ulrika Thelander, Elin Persson, Jonas Bergquist, Per Westermark","doi":"10.1080/13506129.2026.2635090","DOIUrl":"10.1080/13506129.2026.2635090","url":null,"abstract":"Background: Transthyretin amyloid (ATTR) is frequently found in aging ligaments and may represent an early sign of systemic ATTR amyloidosis, particularly of wild-type origin. Amyloid deposits of other compositions are commonly observed alongside ATTR deposits.Methods: Ligamentum flavum samples obtained during surgery for lumbar spinal stenosis, containing distinct ATTR amyloid deposits as well as amyloid of unknown composition, were analyzed using high-performance liquid chromatography-tandem mass spectrometry (HPLC-MS/MS), electron microscopy, immunohistochemistry, and immunofluorescence confocal microscopy. In vitro fibril formation and potential cross-seeding by the two major proteins, transthyretin and lysozyme, were assessed with the thioflavin-T assay.Results: A close topographic association between ATTR deposits and elastic material was evident. Distinct ATTR amyloid was intermingled with non-ATTR amyloid. HPLC-MS/MS identified three major amyloid fibril proteins with high score: transthyretin (TTR), apolipoprotein AI, and lysozyme. Congo red positivity combined with immunoreactivity for TTR and lysozyme demonstrated that ATTR predominated, though distinct lysozyme amyloid deposits were also present. Only minimal apolipoprotein AI-positive amyloid was detected. In vitro, cross-seeding between TTR and lysozyme was not observed; however, lysozyme inhibited TTR fibrillation.Conclusion: In lumbar spinal stenosis, ATTR amyloid deposits are predominant but are often intermixed with other amyloid deposits, notably those of lysozyme origin.","PeriodicalId":50964,"journal":{"name":"Amyloid-Journal of Protein Folding Disorders","volume":" ","pages":"125-134"},"PeriodicalIF":5.1,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147292028","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Incidence of second primary malignancies in patients with AL amyloidosis and the impact of disease stage and therapies. AL淀粉样变性患者第二原发恶性肿瘤的发病率及疾病分期和治疗的影响。

IF 5.1 2区医学

Amyloid-Journal of Protein Folding Disorders Pub Date : 2026-06-01 Epub Date: 2026-04-01 DOI: 10.1080/13506129.2026.2648188

Efstathios Kastritis, Vassiliki Spiliopoulou, Foteini Theodorakakou, Magdalini Migkou, Panagiotis Malandrakis, Evangelos Terpos, Maria Gavriatopoulou, Meletios Athanasios Dimopoulos

引用次数: 0

Long-term outcome of acquired transthyretin amyloidosis. 获得性甲状腺转蛋白淀粉样变的长期预后。

IF 5.1 2区医学

Amyloid-Journal of Protein Folding Disorders Pub Date : 2026-06-01 Epub Date: 2026-01-06 DOI: 10.1080/13506129.2025.2611257

Yohei Misumi, Toshiya Nomura, Shiori Yamakawa, Tomoaki Taguchi, Masayoshi Tasaki, Konen Obayashi, Taro Yamashita, Yukio Ando, Mitsuharu Ueda

{"title":"Long-term outcome of acquired transthyretin amyloidosis.","authors":"Yohei Misumi, Toshiya Nomura, Shiori Yamakawa, Tomoaki Taguchi, Masayoshi Tasaki, Konen Obayashi, Taro Yamashita, Yukio Ando, Mitsuharu Ueda","doi":"10.1080/13506129.2025.2611257","DOIUrl":"10.1080/13506129.2025.2611257","url":null,"abstract":"Background: Acquired transthyretin (ATTR) amyloidosis is increasingly reported among domino liver transplantation (DLT) recipients who receive livers from patients with hereditary variant TTR (ATTRv) amyloidosis. However, its long-term outcomes and the effects of disease-modifying drugs remain unclear.Methods: We retrospectively analyzed 30 DLT recipients who received liver grafts from ATTRv amyloidosis patients. Longitudinal evaluations included clinical scores, nerve conduction studies (NCS),123I-metaiodobenzylguanidine scintigraphy, echocardiography, electrocardiography,99mTc-pyrophosphate scintigraphy, and serum biomarkers.Results: Overall survival at 1, 3, and 10 years after DLT was 86.7%, 76.7%, and 57.7%, respectively. Amyloid deposition occurred in 17 recipients, with a median time from DLT to deposition of 7.7 years (range, 3.1-9.0 years). Among the 12 patients followed for >3 years after amyloid detection, tafamidis clinically stabilized neuropathy in most cases, however, NCSs revealed progressive subclinical axonal degeneration. Two patients experienced clinically significant neuropathy progression during tafamidis treatment, which was stabilized after switching to siRNA therapy. Clinically significant cardiac amyloidosis developed in only one patient.Conclusions: Acquired ATTR amyloidosis frequently develops in long-term DLT recipients. Although tafamidis stabilizes clinical manifestations in most patients, it may not completely prevent disease progression in some cases. Further long-term evaluation is needed to determine optimal treatment strategies, including siRNA therapy.","PeriodicalId":50964,"journal":{"name":"Amyloid-Journal of Protein Folding Disorders","volume":" ","pages":"189-195"},"PeriodicalIF":5.1,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145913824","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Proteolysis reconciles inconsistencies found in proteomic and cryo-EM studies of ATTR. 蛋白质水解调和了蛋白质组学和低温电镜研究中发现的ATTR的不一致性。

IF 5.1 2区医学

Amyloid-Journal of Protein Folding Disorders Pub Date : 2026-06-01 Epub Date: 2026-02-01 DOI: 10.1080/13506129.2026.2622969

Avi Chakrabartty

引用次数: 0

Endothelial glycocalyx disruption and early renal tubular injury in hereditary transthyretin Amyloidosis with dysautonomia. 遗传性甲状腺转蛋白淀粉样变性伴自主神经异常的内皮糖萼破坏和早期肾小管损伤。

IF 5.1 2区医学

Amyloid-Journal of Protein Folding Disorders Pub Date : 2026-06-01 Epub Date: 2025-12-18 DOI: 10.1080/13506129.2025.2603258

Lara Albuquerque de Brito, Cleonisio Leite Rodrigues, Alexandre Braga Libório, Raynrich Kevin Assis Lima, Hermany Capistrano Freitas, Fernanda Martins Maia Carvalho

引用次数: 0

Electric field-induced destabilization and surface modulation of Aβ42 fibrils in molecular simulations: theoretical implications for direct current stimulation in Alzheimer's disease. 在分子模拟中电场诱导的Aβ42原纤维的不稳定和表面调节：对阿尔茨海默病的直流电刺激的理论意义。

IF 5.1 2区医学

Amyloid-Journal of Protein Folding Disorders Pub Date : 2026-06-01 Epub Date: 2026-01-19 DOI: 10.1080/13506129.2026.2616753

Fran Bačić Toplek, Natale Vincenzo Maiorana, Matteo Guidetti, Sara Marceglia, Riccardo Capelli, Alberto Priori, Carlo Camilloni

{"title":"Electric field-induced destabilization and surface modulation of Aβ42 fibrils in molecular simulations: theoretical implications for direct current stimulation in Alzheimer's disease.","authors":"Fran Bačić Toplek, Natale Vincenzo Maiorana, Matteo Guidetti, Sara Marceglia, Riccardo Capelli, Alberto Priori, Carlo Camilloni","doi":"10.1080/13506129.2026.2616753","DOIUrl":"10.1080/13506129.2026.2616753","url":null,"abstract":"Background: The amyloid-β peptide 42 (Aβ42) forms fibrillar aggregates that are a hallmark of Alzheimer's disease. While recent therapeutic strategies targeting Aβ42 fibrils and oligomers have shown promise, safer and more effective interventions are still needed. Noninvasive brain stimulation (NIBS) techniques such as repetitive transcranial magnetic stimulation (rTMS) and transcranial direct current stimulation (tDCS) have emerged as potential complementary approaches, yet the molecular mechanisms by which electric fields influence amyloid aggregation remain poorly understood.Methods: We performed atomistic molecular dynamics simulations to investigate the response of Aβ42 fibrils to static electric fields of increasing strength. Simulations were based on an ex vivo fibril structure with reconstructed N-terminal regions, and different structural restraint conditions were used to disentangle surface and core effects.Results: Electric fields perturb the disordered N-terminal 'fuzzy coat', altering its conformational dynamics and weakening its interactions with the fibril core, thereby modifying the fibril surface properties. Simulations with unrestrained fibril ends further reveal increased fluctuations in core residues, indicating field-induced destabilization that may hinder elongation.Conclusions: These findings provide molecular-level insight into how static electric fields can modulate amyloid fibril formation and propagation, offering a possible mechanistic basis for the effects of tDCS and related brain stimulation techniques.","PeriodicalId":50964,"journal":{"name":"Amyloid-Journal of Protein Folding Disorders","volume":" ","pages":"216-223"},"PeriodicalIF":5.1,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145999638","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

ALyzer3D.AI: a more generalizable deep learning predictor of light chain amyloidogenicity powered by structural and evolutionary Artificial Intelligence. ALyzer3D。人工智能：由结构和进化人工智能驱动的更通用的轻链淀粉样变性深度学习预测器。

IF 5.1 2区医学

Amyloid-Journal of Protein Folding Disorders Pub Date : 2026-06-01 Epub Date: 2025-12-25 DOI: 10.1080/13506129.2025.2605534

Peter May, Johannes Jung, Marion Högner, Florian Bassermann

{"title":"ALyzer3D.AI: a more generalizable deep learning predictor of light chain amyloidogenicity powered by structural and evolutionary Artificial Intelligence.","authors":"Peter May, Johannes Jung, Marion Högner, Florian Bassermann","doi":"10.1080/13506129.2025.2605534","DOIUrl":"10.1080/13506129.2025.2605534","url":null,"abstract":"Background: Predicting amyloidogenic risk of immunoglobulin light chains in amyloid light-chain (AL) amyloidosis is a major challenge, and existing computational models fail to generalize to new patient data.Methods: We developed ALyzer3D.AI, a multi-modal deep learning architecture that integrates evolutionary features from the ESM-2 Protein Language Model, structural metrics from ColabFold and engineered biophysical features. Generalizability was evaluated on published and independent datasets, and model interpretability was assessed using IMGT-aligned SHapley Additive exPlanations (SHAP).Results: While existing models dropped in performance on new data (accuracy 0.42-0.56), ALyzer3D.AI maintained an accuracy of 0.65 when trained and tested on the same datasets. A final model built on the full combined cohort of 5261 sequences achieved stable performance across repeated splits, with independent test AUC of 0.86 and accuracy of 0.84 at an optimized decision threshold. Performance arose from synergistic integration of PLM, structural and scalar features. PLM attributions were broadly distributed and slightly enriched in framework regions, whereas structural SHAP values were concentrated in CDRs and FR4. The most informative positions had intermediate sequence entropy.Conclusions: ALyzer3D.AI provides a robust, interpretable tool for predicting light-chain amyloidogenicity that generalizes better to independent datasets than existing methods. It is publicly available via https://colab.research.google.com/github/pcmay/ALyzer3D.AI/blob/main/ALyzer3DAI.ipynb.","PeriodicalId":50964,"journal":{"name":"Amyloid-Journal of Protein Folding Disorders","volume":" ","pages":"155-167"},"PeriodicalIF":5.1,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145835232","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Detection yield of surrogate tissue biopsies across amyloidosis classes: a large-scale analysis of 4,027 patients. 淀粉样变分类中替代组织活检的检出率：4027例患者的大规模分析。

IF 5.1 2区医学

Amyloid-Journal of Protein Folding Disorders Pub Date : 2026-06-01 Epub Date: 2025-12-29 DOI: 10.1080/13506129.2025.2606847

Natasha J Burke, Lisa M Mendelson, Tracy Joshi, Caryn Libbey, Eric J Burks, Tatiana Prokaeva, Brian Spencer, Luke Zheng, Gheorghe Doros, Vaishali Sanchorawala, Andrew Staron

{"title":"Detection yield of surrogate tissue biopsies across amyloidosis classes: a large-scale analysis of 4,027 patients.","authors":"Natasha J Burke, Lisa M Mendelson, Tracy Joshi, Caryn Libbey, Eric J Burks, Tatiana Prokaeva, Brian Spencer, Luke Zheng, Gheorghe Doros, Vaishali Sanchorawala, Andrew Staron","doi":"10.1080/13506129.2025.2606847","DOIUrl":"10.1080/13506129.2025.2606847","url":null,"abstract":"Background: Congo red (CR) staining of surrogate tissues, such as the abdominal fat pad (FP) or bone marrow (BM), provides a minimally invasive approach to diagnosing systemic amyloidosis. This study evaluated the diagnostic yield of surrogate tissue biopsies across amyloidosis classes.Methods: We retrospectively analyzed 4,027 patients with systemic amyloidosis (1968-2023) who underwent CR staining of FP aspirates (n = 3,873) and/or BM core biopsies (n = 2,598). Detection rates were compared by amyloidosis class and biopsy site.Results: AL amyloidosis had the highest CR positivity rates (FP: 73%; BM: 53%), whereas ATTRwt amyloidosis had the lowest (FP: 22%; BM: 26%). CR positivity in BM was not exclusive to AL amyloidosis; 74 CR-positive BM biopsies were in non-AL cases. Among 2,213 patients with AL amyloidosis who underwent both FP and BM sampling, combined testing increased detection to 85% (40% positive in both; 32% FP-only; 13% BM-only). Higher CR positivity grades in FP aspirates correlated with shorter survival in AL amyloidosis but not in other amyloidosis classes.Conclusions: The diagnostic yield of CR-stained surrogate tissue biopsies varies by amyloidosis class and biopsy site. In AL amyloidosis, combining FP and BM sampling enhances detection, and FP CR positivity grade offers prognostic insight.","PeriodicalId":50964,"journal":{"name":"Amyloid-Journal of Protein Folding Disorders","volume":" ","pages":"146-154"},"PeriodicalIF":5.1,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145851428","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Ongoing or halted amyloid deposition in systemic amyloidosis: essential to know early, but which tools may give early insight? 系统性淀粉样变性中持续或停止的淀粉样沉积：早期了解至关重要，但哪些工具可以提供早期洞察？

IF 5.1 2区医学

Amyloid-Journal of Protein Folding Disorders Pub Date : 2026-06-01 Epub Date: 2026-02-19 DOI: 10.1080/13506129.2026.2633507

Bouke P C Hazenberg, Bart-Jan Kroesen, Johan Bijzet, Hans L A Nienhuis

引用次数: 0

Correction. 修正。

IF 5.1 2区医学

Amyloid-Journal of Protein Folding Disorders Pub Date : 2026-05-28 DOI: 10.1080/13506129.2026.2680374

引用次数: 0