Amyloid-Journal of Protein Folding Disorders最新文献_第2页

Susceptibility and screening approaches in systemic amyloidosis: expert perspectives from the International Society of Amyloidosis (ISA). 系统性淀粉样变性的易感性和筛查方法：来自国际淀粉样变性学会（ISA）的专家观点。

IF 5.1 2区医学

Amyloid-Journal of Protein Folding Disorders Pub Date : 2026-09-04 DOI: 10.1080/13506129.2026.2718204

Taxiarchis Kourelis, Raymond Comenzo, Andrea Cortese, Justin L Grodin, Martha Grogan, Paolo Milani, Frederick L Ruberg, Yoshiki Sekijima, Lukas D Weberling, Efstathios Kastritis, Kevin M Alexander

{"title":"Susceptibility and screening approaches in systemic amyloidosis: expert perspectives from the International Society of Amyloidosis (ISA).","authors":"Taxiarchis Kourelis, Raymond Comenzo, Andrea Cortese, Justin L Grodin, Martha Grogan, Paolo Milani, Frederick L Ruberg, Yoshiki Sekijima, Lukas D Weberling, Efstathios Kastritis, Kevin M Alexander","doi":"10.1080/13506129.2026.2718204","DOIUrl":"https://doi.org/10.1080/13506129.2026.2718204","url":null,"abstract":"Background: Systemic amyloidosis is a progressive disease in which misfolded protein toxicity and deposition lead to organ dysfunction. Early diagnosis is essential to enable timely treatment and prevent irreversible organ damage, yet the disease remains underrecognized. Although advances in imaging and biomarkers have raised suspicion in appropriate contexts, a major barrier is the absence of clearly defined factors identifying individuals at high risk who warrant timely screening.Methods: On behalf of the International Society of Amyloidosis (ISA), experts in the field reviewed the diagnostic landscape and identified unmet needs in the early detection of systemic amyloidosis.Results: The experts highlighted a lack of risk-adapted screening strategies capable of improving detection while avoiding inefficient population-level screening. They identified parameters that may help define high-risk populations, including biomarkers, susceptibility factors, demographic variables, and clinical 'red flags'. They further discussed how artificial intelligence (AI)-driven tools may support identification of at-risk individuals and accelerate diagnosis in suspected amyloidosis.Conclusions: Defining high-risk populations and integrating AI-based tools may enable risk-adapted screening that improves early diagnosis while avoiding indiscriminate population-level testing.","PeriodicalId":50964,"journal":{"name":"Amyloid-Journal of Protein Folding Disorders","volume":" ","pages":"1-14"},"PeriodicalIF":5.1,"publicationDate":"2026-09-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148892879","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

Proline-rich, polybasic peptides are a structurally distinct class of amyloid-reactive peptides. 富含脯氨酸的多碱肽是一类结构独特的淀粉样蛋白反应肽。

IF 5.1 2区医学

Amyloid-Journal of Protein Folding Disorders Pub Date : 2026-09-01 Epub Date: 2026-05-25 DOI: 10.1080/13506129.2026.2671950

Trevor J Hancock, Manasi Balachandran, Angela Williams, James Foster, Anna Sparks, Joseph Jackson, Nic Angell, Ashlyn Wilson, Sallie Macy, Craig Wooliver, Jonathan Wall

{"title":"Proline-rich, polybasic peptides are a structurally distinct class of amyloid-reactive peptides.","authors":"Trevor J Hancock, Manasi Balachandran, Angela Williams, James Foster, Anna Sparks, Joseph Jackson, Nic Angell, Ashlyn Wilson, Sallie Macy, Craig Wooliver, Jonathan Wall","doi":"10.1080/13506129.2026.2671950","DOIUrl":"10.1080/13506129.2026.2671950","url":null,"abstract":"Background: Systemic amyloidosis is a chronic, devastating illness caused by the build-up of misfolded proteins, leading to abdominothoracic organ dysfunction. Currently approved treatment options focus on preventing further amyloid accumulation. As such, there is a clinically unmet need for therapeutics that can opsonize tissue-deposited amyloid for clearance by phagocytic cells. We have developed a class of polybasic peptides that bind conserved properties of amyloid and amyloid-associated hypersulfated heparan sulfate, with high specificity. We have generated a novel structural class of polybasic peptides (termed PxR peptides) based on a proline-rich repeat strategy that demonstrates potency against amyloid.Methods: Amyloid-reactivity and specificity were probed using amyloid-laden and control tissue sections from mice and humans. Amyloid binding to synthetic fibrils and human patient-derived amyloid extracts was quantified using immunosorbent assays. PxR peptide stability in mouse and human serum was quantified using a bioactivity assay.Results: PxR peptides were predicted to form a linear face of positive charges, which can bind with high specificity and potency to synthetic fibrils and amyloid extracts, and are resistant to serum proteases.Conclusions: Polybasic PxR peptides offer additional resources as pan-amyloid binding peptides for effective delivery of bioactive and amyloid-clearing therapeutics to amyloid.","PeriodicalId":50964,"journal":{"name":"Amyloid-Journal of Protein Folding Disorders","volume":" ","pages":"410-420"},"PeriodicalIF":5.1,"publicationDate":"2026-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148018667","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

Fat aspiration for amyloidosis screening of 2830 patients from 2013 to 2020: compelling sensitivity for AL and better sensitivity in females for all major subtypes. 2013 - 2020年2830例淀粉样变患者的脂肪抽吸筛查：AL的敏感性令人注目，女性对所有主要亚型的敏感性更高。

IF 5.1 2区医学

Amyloid-Journal of Protein Folding Disorders Pub Date : 2026-09-01 Epub Date: 2026-06-26 DOI: 10.1080/13506129.2026.2685673

Christoph Richard Kimmich, Stefan O Schönland, Norbert Blank, Tobias Dittrich, Kaya Veelken, Carsten Müller-Tidow, Johan Bijzet, Hans LA Nienhuis, Bouke P Hazenberg, Ute Hegenbart

{"title":"Fat aspiration for amyloidosis screening of 2830 patients from 2013 to 2020: compelling sensitivity for AL and better sensitivity in females for all major subtypes.","authors":"Christoph Richard Kimmich, Stefan O Schönland, Norbert Blank, Tobias Dittrich, Kaya Veelken, Carsten Müller-Tidow, Johan Bijzet, Hans LA Nienhuis, Bouke P Hazenberg, Ute Hegenbart","doi":"10.1080/13506129.2026.2685673","DOIUrl":"10.1080/13506129.2026.2685673","url":null,"abstract":"Introduction: Subcutaneous fat aspiration is a minimally-invasive screening tool for systemic amyloidosis (SA) with high variability in reported sensitivities.Methods: Sensitivity and specificity were studied for consecutive Congo red-stained fat aspirates for amyloidosis screening performed between 2013 and 2020. For sensitivity analysis patients with symptomatic SA proven by either histopathology or scintigraphy and for specificity analysis patients with clinically certain exclusion of SA were chosen. Deposits were classified as substantial when >10% of analyzed tissue stained positive.Results: 1320/2830 probes were positive of which 617 were graded as substantial.Overall sensitivity was 70.0% (1190/1701) according to gold-standard and specificity was 99.4% (613/617). Additionally, in 110/114 patients with clinically certain SA and in 16/398 probes from patients with nonspecific findings amyloid was detected. For subtypes, sensitivities were: systemic light-chain (AL) 90.1% (922/1023), transthyretin wild-type (ATTRwt) 18.8% (69/368), AA 72.3% (107/148) and transthyretin variant (ATTRv) amyloidosis 71% (63/89). Sensitivity overall and in AL, ATTRwt, AA and ATTRv was higher in females. Substantial deposits were more common in females overall and in AL.Summary: Fat aspiration for symptomatic SA yielded excellent specificity. Sensitivity was very good in AL and fair in ATTRv and AA amyloidosis. Sensitivity was higher in females than in males.","PeriodicalId":50964,"journal":{"name":"Amyloid-Journal of Protein Folding Disorders","volume":" ","pages":"368-380"},"PeriodicalIF":5.1,"publicationDate":"2026-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148341052","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

Transthyretin stabilizer therapy increases naturally-occurring antibodies in ATTR cardiomyopathy. 经甲状腺素稳定剂治疗可增加ATTR心肌病患者的天然抗体。

IF 5.1 2区医学

Amyloid-Journal of Protein Folding Disorders Pub Date : 2026-09-01 Epub Date: 2026-04-06 DOI: 10.1080/13506129.2026.2651299

Stephan Settelmeier, Daniel Agranovski, Maximilian Steinhardt, Sarah Waydhas, Ian Gering, Vladimir Cejka, Caroline Morbach, Stefan Störk, Dieter Willbold, Ralf Küppers, Julia Vogel, Lars Michel, Alexander Carpinteiro, H Christian Reinhardt, Richard Dodel, Tienush Rassaf, Alexander J Ross, Ulrike B Hendgen-Cotta

{"title":"Transthyretin stabilizer therapy increases naturally-occurring antibodies in ATTR cardiomyopathy.","authors":"Stephan Settelmeier, Daniel Agranovski, Maximilian Steinhardt, Sarah Waydhas, Ian Gering, Vladimir Cejka, Caroline Morbach, Stefan Störk, Dieter Willbold, Ralf Küppers, Julia Vogel, Lars Michel, Alexander Carpinteiro, H Christian Reinhardt, Richard Dodel, Tienush Rassaf, Alexander J Ross, Ulrike B Hendgen-Cotta","doi":"10.1080/13506129.2026.2651299","DOIUrl":"10.1080/13506129.2026.2651299","url":null,"abstract":"Background: Amyloid transthyretin cardiomyopathy (ATTR-CM) results from extracellular deposition of misfolded transthyretin (TTR), causing progressive heart failure. Naturally-occurring antibodies (nAbs) targeting misfolded proteins exist in neurodegenerative disease, but their presence in ATTR-CM is unknown. The objective of this study is to determine whether nAbs against TTR (nAbsTTR) exist in humans and whether they are influenced by disease or its treatment.Methods: Serum from healthy donors, umbilical cord blood (UCB), and patients with ATTR-CM - both untreated and receiving TTR-stabilizing therapy - was analyzed for nAbsTTR using immunoassays, blotting, and binding studies. Functional activity was evaluated in a fibril formation assay.Results: nAbsTTR binding both native and amyloid TTR (ATTR) with high affinity (KD 30 nM/7 nM) were detected in healthy serum and UCB. NAbsTTR levels were significantly altered in ATTR-CM compared to controls: nAbsTTR (IgG) were higher while nAbsTTR (IgM) were lower. nAbsTTR of both subtypes significantly increased by 22% (p ≤ 0.05) in patients receiving TTR-stabilizing therapy. In vitro, nAbsTTR suppressed TTR fibril aggregation.Conclusions: Naturally-occurring TTR-targeting antibodies are present from birth, modulated by disease and therapy, and inhibit fibril formation. These findings reveal an unrecognized immune mechanism with potential relevance for ATTR-CM pathogenesis and treatment.","PeriodicalId":50964,"journal":{"name":"Amyloid-Journal of Protein Folding Disorders","volume":" ","pages":"320-336"},"PeriodicalIF":5.1,"publicationDate":"2026-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147624552","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

Article commentary on: 'Serum peripherin as a disease biomarker in hereditary transthyretin amyloidosis: a multicenter cohort study'. 文章评论：“血清外周蛋白作为遗传性甲状腺转蛋白淀粉样变的疾病生物标志物：一项多中心队列研究”。

IF 5.1 2区医学

Amyloid-Journal of Protein Folding Disorders Pub Date : 2026-09-01 Epub Date: 2026-09-02 DOI: 10.1080/13506129.2026.2726463

Christian Messina

引用次数: 0

The prognostic value of red blood cell distribution width in AL amyloidosis. 红细胞分布宽度对AL淀粉样变的预后价值。

IF 5.1 2区医学

Amyloid-Journal of Protein Folding Disorders Pub Date : 2026-09-01 Epub Date: 2026-05-16 DOI: 10.1080/13506129.2026.2671953

Despina Fotiou, Erasmia Boutakoglou, Konstantinos Giannakas, Foteini Theodorakakou, Eirini Solia, Magdalini Migkou, Panagiotis Malandrakis, Ioannis Ntanasis-Stathopoulos, Vasiliki Spiliopoulou, Nikolaos Kanellias, Evangelos Eleutherakis-Papaiakovou, Maria Gavriatopoulou, Evangelos Terpos, Meletios A Dimopoulos, Efstathios Kastritis

引用次数: 0

Serum peripherin as a disease biomarker in hereditary transthyretin amyloidosis: a multicenter cohort study. 血清外周蛋白作为遗传性甲状腺转蛋白淀粉样变的疾病生物标志物：一项多中心队列研究

IF 5.1 2区医学

Amyloid-Journal of Protein Folding Disorders Pub Date : 2026-09-01 Epub Date: 2026-03-16 DOI: 10.1080/13506129.2026.2640984

Domenico Plantone, Delia Righi, Angela Romano, Luca Leonardi, Valeria Guglielmino, Francesca Forcina, Marco Ceccanti, Maurizio Inghilleri, Fiore Manganelli, Stefano Tozza, Maria Ausilia Sciarrone, Francesca Vitali, Andrea Sabino, Carlo Manco, Angela Stufano, Maria Laura Stromillo, Nicola De Stefano, Paolo Calabresi, Guido Primiano, Marco Luigetti

{"title":"Serum peripherin as a disease biomarker in hereditary transthyretin amyloidosis: a multicenter cohort study.","authors":"Domenico Plantone, Delia Righi, Angela Romano, Luca Leonardi, Valeria Guglielmino, Francesca Forcina, Marco Ceccanti, Maurizio Inghilleri, Fiore Manganelli, Stefano Tozza, Maria Ausilia Sciarrone, Francesca Vitali, Andrea Sabino, Carlo Manco, Angela Stufano, Maria Laura Stromillo, Nicola De Stefano, Paolo Calabresi, Guido Primiano, Marco Luigetti","doi":"10.1080/13506129.2026.2640984","DOIUrl":"10.1080/13506129.2026.2640984","url":null,"abstract":"Background: Hereditary transthyretin amyloidosis (ATTRv, v for variant) is a rare, progressive, and fatal multisystemic disease. Peripherin represents a promising biomarker for axonal damage in the peripheral nervous system (PNS). This study aims to investigate serum peripherin levels in symptomatic and presymptomatic ATTRv subjects, alongside serum neurofilament light chain (sNfL) levels, and their correlations with disease progression and severity.Methods: This multicenter, cross-sectional cohort study included 96 individuals with TTR gene variants (49 presymptomatic and 47 symptomatic ATTRv subjects) and 42 healthy controls (HCs). Serum peripherin levels were measured using a highly sensitive homebrew immunoassay, whereas sNfL levels were determined using a commercially available Simoa Neurology 2-Plex B assay. Statistical analyses included non-parametric Spearman correlations, Kruskal-Wallis ANOVA, ANCOVA, and binomial logistic regression.Results: Serum peripherin levels were elevated in both presymptomatic (p < 0.001) and symptomatic ATTRv groups (p < 0.001) compared to HCs. Peripherin levels did not correlate with age, sNfL levels, or clinical severity, but showed a strong discriminative ability between ATTRv and HCs (AUC = 0.83, sensitivity = 76%, specificity = 76%, p < 0.001).Conclusions: This study demonstrates that serum peripherin represents a promising biomarker for early detection of PNS damage in ATTRv, with elevated levels detectable even in presymptomatic stages.","PeriodicalId":50964,"journal":{"name":"Amyloid-Journal of Protein Folding Disorders","volume":" ","pages":"276-285"},"PeriodicalIF":5.1,"publicationDate":"2026-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147470225","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

Artificial intelligence-enhanced electrocardiogram findings before and after heart transplantation in cardiac amyloidosis. 人工智能增强心肌淀粉样变性患者心脏移植前后心电图表现。

IF 5.1 2区医学

Amyloid-Journal of Protein Folding Disorders Pub Date : 2026-09-01 Epub Date: 2026-05-18 DOI: 10.1080/13506129.2026.2669753

Kamal Awad, Juan M Farina, Jose N Nativi Nicolau, Melissa A Lyle, Andrew N Rosenbaum, Barry A Boilson, Omar F Abou Ezzeddine, Francisco Lopez-Jimenez, Angela Dispenzieri, Martha Grogan, D Eric Steidley, Reza Arsanjani, Julie L Rosenthal

引用次数: 0

RNA-based full length immunoglobulin light chain sequencing reveals lambda constant domain mutations with potential implications for thermodynamic stability in light chain amyloidosis. 基于rna的全长免疫球蛋白轻链测序揭示了lambda恒定结构域突变与轻链淀粉样变性的热力学稳定性的潜在影响。

IF 5.1 2区医学

Amyloid-Journal of Protein Folding Disorders Pub Date : 2026-09-01 Epub Date: 2026-06-04 DOI: 10.1080/13506129.2026.2679153

Eyad Naser, Sara Oubari, Josefine Jakob, Björn Häupl, Bettina Budeus, Bernd Walkenfort, Melanie Nowakowski, Gabriele Hessler, Claudine Kühn, Mike Hasenberg, Thomas Oellerich, Hans Christian Reinhardt, Alexander Carpinteiro

{"title":"RNA-based full length immunoglobulin light chain sequencing reveals lambda constant domain mutations with potential implications for thermodynamic stability in light chain amyloidosis.","authors":"Eyad Naser, Sara Oubari, Josefine Jakob, Björn Häupl, Bettina Budeus, Bernd Walkenfort, Melanie Nowakowski, Gabriele Hessler, Claudine Kühn, Mike Hasenberg, Thomas Oellerich, Hans Christian Reinhardt, Alexander Carpinteiro","doi":"10.1080/13506129.2026.2679153","DOIUrl":"10.1080/13506129.2026.2679153","url":null,"abstract":"Background: Systemic light chain amyloidosis is a protein misfolding disorder characterized by deposition of clonal immunoglobulin light chains in vital organs. To date, little is known about the contribution of light chain constant domain mutations in thermodynamic stability and amyloidogenicity.Methods: In 89 patients, RNA-based full-length light chain repertoire sequencing with Oxford Nanopore was performed, in addition to Illumina sequencing and mass spectrometric detection of light chain protein in serum and amyloid deposits. Computational methods for conservation, free energy calculation and molecular dynamics simulations were applied to investigate the thermodynamic stability.Results: Monoclonal light chain detection rate was 95.4%, and sequences showed 100% identity with Illumina in all patients. Light chain protein was specifically detectable by mass spectrometry in serum and amyloid deposits. Lambda constant domain mutations were present in 10%, while no kappa constant domain mutations were detected. Fold free energy change and molecular dynamics simulations indicate potential light chain stabilizing or destabilizing effects of detected constant domain mutations.Conclusion: Current findings highlight the importance of routinely implementing full-length light chain sequencing in plasma cell dyscrasias, particularly light chain amyloidosis to account for the potential impact of constant domain mutations on light chain stability and amyloidogenicity.","PeriodicalId":50964,"journal":{"name":"Amyloid-Journal of Protein Folding Disorders","volume":" ","pages":"381-395"},"PeriodicalIF":5.1,"publicationDate":"2026-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148165353","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

Long-term efficacy and safety of vutrisiran in hereditary transthyretin amyloidosis with polyneuropathy: final analysis of the HELIOS-A randomized treatment extension. 乌崔西兰治疗遗传性甲状腺转蛋白淀粉样变性合并多发性神经病变的长期疗效和安全性：HELIOS-A随机扩展治疗的最终分析。

IF 5.1 2区医学

Amyloid-Journal of Protein Folding Disorders Pub Date : 2026-09-01 Epub Date: 2026-06-15 DOI: 10.1080/13506129.2026.2685666

Cécile Cauquil, David Adams, Julian Gillmore, Alejandra Gonzalez-Duarte, Michelle Mezei, Laura Obici, Yoshiki Sekijima, Weizhi Zhao, Katherine Boyle, Prajakta Badri, Marianne Sweetser, Colleen Moffitt, Márcia Waddington-Cruz

{"title":"Long-term efficacy and safety of vutrisiran in hereditary transthyretin amyloidosis with polyneuropathy: final analysis of the HELIOS-A randomized treatment extension.","authors":"Cécile Cauquil, David Adams, Julian Gillmore, Alejandra Gonzalez-Duarte, Michelle Mezei, Laura Obici, Yoshiki Sekijima, Weizhi Zhao, Katherine Boyle, Prajakta Badri, Marianne Sweetser, Colleen Moffitt, Márcia Waddington-Cruz","doi":"10.1080/13506129.2026.2685666","DOIUrl":"10.1080/13506129.2026.2685666","url":null,"abstract":"Background: The long-term efficacy and safety of vutrisiran in hereditary transthyretin amyloidosis with polyneuropathy (ATTRv-PN) were assessed in the HELIOS-A randomized treatment extension (RTE).Methods: Patients who completed the 18-month, phase 3, open-label HELIOS-A study could enter an open-label RTE with re-randomization 1:1 to vutrisiran 25 mg every 3 months (Q3M) or 50 mg every 6 months (Q6M; transitioned to 25 mg Q3M following an amendment) for up to 42 months (RTE M18 efficacy assessment; RTE M42 safety and transthyretin (TTR) levels).Results: In the RTE, 149 patients were re-randomized to vutrisiran (25 mg Q3M [n = 76]; 50 mg Q6M [n = 73]). Mean serum TTR reduction from study baseline at RTE M42 for the total vutrisiran group was 84.5%. Efficacy was sustained from RTE baseline through RTE M18 in modified Neuropathy Impairment Score +7, Norfolk Quality of Life-Diabetic Neuropathy score, 10-meter walk test, Rasch-built Overall Disability Scale and modified body mass index (mBMI); most patients (67.8%) had stable polyneuropathy disability scores. Most AEs were mild/moderate in severity with no new safety concerns.Conclusions: Results from the HELIOS-A RTE demonstrate relative stability with only modest changes in disease activity, sustained serum TTR reductions, and an acceptable safety profile with long-term vutrisiran treatment in patients with ATTRv-PN.ClinicalTrials.gov: NCT03759379.","PeriodicalId":50964,"journal":{"name":"Amyloid-Journal of Protein Folding Disorders","volume":" ","pages":"356-367"},"PeriodicalIF":5.1,"publicationDate":"2026-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148254339","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