Fausto De Andrés-Cardelle, Gonzalo Barge-Caballero, Manuel López-Pérez, Andrea López-López, Eva González-Babarro, Mario Gutiérrez-Feijoo, Raquel Bilbao-Quesada, Inés Gómez-Otero, Alfonso Varela-Román, Alberto Bouzas-Mosquera, María G Crespo-Leiro, Eduardo Barge-Caballero
{"title":"Usefulness of the Columbia score for predicting outcomes in patients with transthyretin amyloid cardiomyopathy. Analysis of the Galician registry of cardiac amyloidosis.","authors":"Fausto De Andrés-Cardelle, Gonzalo Barge-Caballero, Manuel López-Pérez, Andrea López-López, Eva González-Babarro, Mario Gutiérrez-Feijoo, Raquel Bilbao-Quesada, Inés Gómez-Otero, Alfonso Varela-Román, Alberto Bouzas-Mosquera, María G Crespo-Leiro, Eduardo Barge-Caballero","doi":"10.1080/13506129.2025.2453231","DOIUrl":"10.1080/13506129.2025.2453231","url":null,"abstract":"<p><strong>Aims: </strong>To evaluate the predictive value of the Columbia score in patients with transthyretin amyloid cardiomyopathy (ATTR-CM).</p><p><strong>Methods: </strong>Observational study based in a prospective, multi-centre registry of patients with ATTR-CM recruited between January-2018 and December-2023 in 7 Spanish hospitals. The Baseline Columbia score was correlated by means of multivariable Cox's regression with study endpoints all-cause death and all-cause death or heart failure (HF) hospitalisation. Discriminative capacity was evaluated by means of Harrell's <i>C</i> statistics and area under 2-year time-dependent receiver-operator curves.</p><p><strong>Results: </strong>We studied 374 patients with ATTR-CM. Columbia score was independently associated with increased risk of all-cause death (adjusted HR per 1 point = 1.30, 95% CI 1.17-1.45) and all-cause death or HF hospitalisation (adjusted HR per 1 point = 1.38, 95% 1.26-1.50). The score showed moderate discriminative capacity for all-cause death (Harrell's <i>C</i> = 0.653) and all-cause death or HF hospitalisation (Harrell's <i>C</i> = 0.697). The area under the 2-year time-dependent receiver-operator curve was 0.594 for all-cause death and 0.669 for all-cause death or HF hospitalisation. Columbia's score was adequately calibrated for both outcomes.</p><p><strong>Conclusions: </strong>We studied the prognostic performance of the Columbia score in a Spanish prospective cohort of patients with ATTR-CM. The score showed adequate calibration and moderate discriminative capacity for predicting death and HF hospitalisations.</p>","PeriodicalId":50964,"journal":{"name":"Amyloid-Journal of Protein Folding Disorders","volume":" ","pages":"145-153"},"PeriodicalIF":5.2,"publicationDate":"2025-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143015624","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}
Hironobu Naiki, Mona Johnson, Kaylee Walters, Alexander Carpinteiro, M Teresa Cibeira, Anita D'Souza, Efstathios Kastritis, Mathew S Maurer, Lisa Mendelson, Giampaolo Merlini, Eli Muchtar, Giovanni Palladini, Eloisa Riva, Yoshiki Sekijima, Per Westermark, Shaji Kumar, Stefan Olaf Schönland
{"title":"Global patterns of amyloid typing: results of a survey by the International Society of Amyloidosis (ISA).","authors":"Hironobu Naiki, Mona Johnson, Kaylee Walters, Alexander Carpinteiro, M Teresa Cibeira, Anita D'Souza, Efstathios Kastritis, Mathew S Maurer, Lisa Mendelson, Giampaolo Merlini, Eli Muchtar, Giovanni Palladini, Eloisa Riva, Yoshiki Sekijima, Per Westermark, Shaji Kumar, Stefan Olaf Schönland","doi":"10.1080/13506129.2025.2462992","DOIUrl":"10.1080/13506129.2025.2462992","url":null,"abstract":"<p><strong>Background: </strong>Accurate tissue typing in amyloidosis is essential to provide appropriate therapy for individual patients.</p><p><strong>Objective: </strong>To get a real-life overview of typing strategies worldwide.</p><p><strong>Methods: </strong>The International Society of Amyloidosis (ISA) performed an online questionnaire survey among ISA members. We prepared questionnaire sheets for referral institutions (Category 1; C1), institutions performing amyloid typing for internal requests only (C2), and institutions outsourcing amyloid typing to referral institutions (C3), respectively.</p><p><strong>Results: </strong>Seventy-six institutions participated in this survey, including C1 (<i>n</i> = 33), C2 (<i>n</i> = 20) and C3 (<i>n</i> = 23) institutions. Multiple typing methods were available across the responding institutions, including immunohistochemistry (85% of C1/C2 institutions), immunofluorescence microscopy (43%), genetic analysis (77%) and mass spectrometric analysis (42%). Commercial antibodies were used worldwide for immunohistochemistry. C1 institutions in Europe and Asia also used various in-house antibodies. Ninety-three percent of institutions performed genetic analysis of <i>TTR gene</i>, followed by <i>APOA1</i> (43%), <i>FGA</i>, <i>GSN</i>, <i>LYZ</i> (33%) and <i>APOA2</i> (31%). Hierarchical referral flows of mass spectrometric analysis, immunohistochemistry and genetic analysis were observed regionally and internationally. Globalization and centralization of referral flows were more prominent for mass spectrometric analysis.</p><p><strong>Conclusion: </strong>These data provide an assessment of the current state, enabling improvement in capabilities of amyloid typing worldwide and enhancing regional/international networks.</p>","PeriodicalId":50964,"journal":{"name":"Amyloid-Journal of Protein Folding Disorders","volume":" ","pages":"139-144"},"PeriodicalIF":5.2,"publicationDate":"2025-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143384048","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}
Milou Berends, Hendrea S A Tingen, Johan Bijzet, Henny H Lemmink, Friso L H Muntinghe, Ewout J Houwerzijl, Peter van der Meer, Riemer H J A Slart, Janet A Gilbertson, Reinold O B Gans, Bouke P C Hazenberg, Hans L A Nienhuis, Paul A van der Zwaag
{"title":"Multigene panel analysis has limited additional value compared to transthyretin gene analysis in Dutch patients with suspected cardiac amyloidosis.","authors":"Milou Berends, Hendrea S A Tingen, Johan Bijzet, Henny H Lemmink, Friso L H Muntinghe, Ewout J Houwerzijl, Peter van der Meer, Riemer H J A Slart, Janet A Gilbertson, Reinold O B Gans, Bouke P C Hazenberg, Hans L A Nienhuis, Paul A van der Zwaag","doi":"10.1080/13506129.2025.2469609","DOIUrl":"10.1080/13506129.2025.2469609","url":null,"abstract":"","PeriodicalId":50964,"journal":{"name":"Amyloid-Journal of Protein Folding Disorders","volume":" ","pages":"203-206"},"PeriodicalIF":5.2,"publicationDate":"2025-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143598214","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}
Valentina Moccia, Claudia Maria Tucciarone, Silvia Garutti, Melissa Milazzo, Filippo Ferri, Carlo Palizzotto, Maria Mazza, Marco Basset, Eric Zini, Stefano Ricagno, Silvia Ferro
{"title":"AA amyloidosis in vertebrates: epidemiology, pathology and molecular aspects.","authors":"Valentina Moccia, Claudia Maria Tucciarone, Silvia Garutti, Melissa Milazzo, Filippo Ferri, Carlo Palizzotto, Maria Mazza, Marco Basset, Eric Zini, Stefano Ricagno, Silvia Ferro","doi":"10.1080/13506129.2024.2417219","DOIUrl":"10.1080/13506129.2024.2417219","url":null,"abstract":"<p><p>AA amyloidosis is a prototypic example of systemic amyloidosis: it results from the prolonged overproduction of SAA protein produced in response to chronic inflammation. AA amyloidosis primarily affects the kidneys, liver, spleen, gastrointestinal tract, leading to a variety of symptoms. First, this review examines AA amyloidosis in humans, focusing on pathogenesis, clinical presentation, and diagnosis and then in animals. In fact AA amyloidosis is the only systemic amyloidosis that has been largely documented in a remarkable number of vertebrate species: mammals, birds, and fishes, especially in individuals with comorbidities, chronic stress, or held in captivity. Secondly, here, we summarise independent sets of evidence obtained on different animal species, exploring the possible transmissibility of AA amyloidosis especially in crowded or confined populations. Finally, biochemical and structural data on native SAA and on AA amyloid fibrils from human, murine, and cat ex vivo samples are discussed. The available structural data depict a complex scenario, where SAA can misfold forming highly different amyloid assemblies. This review highlights the complexity of AA amyloidosis, emphasising the need for further research into its spread in the animal kingdom, its structural aspects, and pathogenetic mechanisms to evaluate its impact on human and animal health.</p>","PeriodicalId":50964,"journal":{"name":"Amyloid-Journal of Protein Folding Disorders","volume":" ","pages":"3-13"},"PeriodicalIF":5.2,"publicationDate":"2025-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142480034","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}
Brian C Netzel, M Cristine Charlesworth, Kenneth L Johnson, Amy J French, Angela Dispenzieri, Joseph J Maleszewski, Ellen D McPhail, Martha Grogan, Margaret M Redfield, Megan Weivoda, Eli Muchtar, Morie A Gertz, Shaji K Kumar, Pinaki Misra, Julie Vrana, Jason Theis, Suzanne R Hayman, Marina Ramirez-Alvarado, Surendra Dasari, Taxiarchis Kourelis
{"title":"Whole tissue proteomic analyses of cardiac ATTR and AL unveil mechanisms of tissue damage.","authors":"Brian C Netzel, M Cristine Charlesworth, Kenneth L Johnson, Amy J French, Angela Dispenzieri, Joseph J Maleszewski, Ellen D McPhail, Martha Grogan, Margaret M Redfield, Megan Weivoda, Eli Muchtar, Morie A Gertz, Shaji K Kumar, Pinaki Misra, Julie Vrana, Jason Theis, Suzanne R Hayman, Marina Ramirez-Alvarado, Surendra Dasari, Taxiarchis Kourelis","doi":"10.1080/13506129.2024.2448440","DOIUrl":"10.1080/13506129.2024.2448440","url":null,"abstract":"<p><strong>Background: </strong>Cardiac AL and ATTR are potentially fatal cardiomyopathies. Current therapies do not address mechanisms of tissue dysfunction because these remain unknown. Our prior work focused on the amyloid plaque proteome, which may not capture tissue-wide proteomic alterations.</p><p><strong>Objectives: </strong>To evaluate mechanisms of tissue dysfunction in cardiac AL and ATTR using a full biopsy tissue proteomics approach.</p><p><strong>Methods: </strong>We performed proteomics analysis on 76 ATTR and 27 AL diagnostic endomyocardial biopsies.</p><p><strong>Results: </strong>Stage-3 AL patients exhibited increased coagulation, extracellular matrix remodelling (ECM), epithelial-to-mesenchymal transition (EMT), complement activation, hypoxia, and clathrin-mediated endocytosis pathways <i>vs.</i> stages-1/2, with decreased healthy cardiac metabolism. In stages-2 and 3 ATTR, immunoglobulin proteins, complement, and keratinisation pathways were increased compared to stage-1. Unsupervised analyses identified an ATTR group with worse survival characterised by upregulated complement and downregulated metabolic pathways. Compared to ATTR, AL had higher clathrin-mediated endocytosis, mRNA splicing, and ribosomal proteins, while ATTR had higher complement levels.</p><p><strong>Conclusions: </strong>This study identifies known processes dysregulated in heart failure with preserved ejection fraction as well as novel pathways responsible for tissue damage. Our results support an immune-mediated mechanism of tissue toxicity in cardiac amyloidosis, especially among patients with worse outcomes.</p>","PeriodicalId":50964,"journal":{"name":"Amyloid-Journal of Protein Folding Disorders","volume":" ","pages":"72-80"},"PeriodicalIF":5.2,"publicationDate":"2025-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11825277/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142958446","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
A Roldán-Sevilla, M Gallego-Delgado, M T Lista-Araujo, J Torres-Pérez, A M Merino-Merino, C Gil-Polo, D Cantero-Lozano, S M Lorenzo-Hernandez, R Eiros-Bachiller
{"title":"Clinical and genetic features of AGel amyloidosis caused by novel gelsolin variant and its impact on cardiac function and conduction disorders.","authors":"A Roldán-Sevilla, M Gallego-Delgado, M T Lista-Araujo, J Torres-Pérez, A M Merino-Merino, C Gil-Polo, D Cantero-Lozano, S M Lorenzo-Hernandez, R Eiros-Bachiller","doi":"10.1080/13506129.2024.2441784","DOIUrl":"10.1080/13506129.2024.2441784","url":null,"abstract":"","PeriodicalId":50964,"journal":{"name":"Amyloid-Journal of Protein Folding Disorders","volume":" ","pages":"90-92"},"PeriodicalIF":5.2,"publicationDate":"2025-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142856388","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}
Ole B Suhr, Martha Grogan, Ana Martins da Silva, Chafic Karam, Pablo Garcia-Pavia, Brian Drachman, Wagner Zago, Radhika Tripuraneni, Gene G Kinney
{"title":"PRX004 in variant amyloid transthyretin (ATTRv) amyloidosis: results of a phase 1, open-label, dose-escalation study.","authors":"Ole B Suhr, Martha Grogan, Ana Martins da Silva, Chafic Karam, Pablo Garcia-Pavia, Brian Drachman, Wagner Zago, Radhika Tripuraneni, Gene G Kinney","doi":"10.1080/13506129.2024.2420809","DOIUrl":"10.1080/13506129.2024.2420809","url":null,"abstract":"<p><strong>Background: </strong>The investigational monoclonal antibody PRX004 is designed to specifically target and deplete TTR amyloid. Here, we report on the safety, tolerability, pharmacokinetics, pharmacodynamics and preliminary clinical activity of PRX004 in patients with ATTRv amyloidosis.</p><p><strong>Methods: </strong>This global, multicentre, phase 1 trial comprised a 3 + 3 dose-escalation phase and a long-term extension (LTE) phase (NCT03336580). In the dose-escalation phase, patients received PRX004 (0.1, 0.3, 1, 3, 10 or 30 mg/kg), administered intravenously every 28 days for 3 months. In the LTE, eligible patients could receive up to 15 additional doses. Patients who received doses of ≥3 mg/kg for ≥9 months were assessed for Global Longitudinal Strain (GLS) and Neuropathy Impairment Score (NIS). The primary objective was to determine the maximum tolerated dose (MTD) of PRX004.</p><p><strong>Results: </strong>Overall, 21 patients with ATTRv amyloidosis completed the dose-escalation phase; 17 subsequently enrolled in the LTE. The MTD was not reached. PRX004 was well tolerated at all doses, with dose-proportional exposure. GLS and NIS were improved or maintained over 9 months (<i>n</i> = 7).</p><p><strong>Conclusions: </strong>PRX004 was well tolerated in patients with ATTRv amyloidosis and demonstrated potential clinical activity. A phase 2 randomised controlled trial in ATTR cardiomyopathy is ongoing (NCT05442047).</p>","PeriodicalId":50964,"journal":{"name":"Amyloid-Journal of Protein Folding Disorders","volume":" ","pages":"14-21"},"PeriodicalIF":5.2,"publicationDate":"2025-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142548803","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}
Jonas Wixner, John L Berk, David Adams, Michael Polydefkis, Isabel Conceição, Shahram Attarian, Julian D Gillmore, P James B Dyck, Folke Folkvaljon, Wunan Zhou, Jersey Chen, Nicholas J Viney, T Jesse Kwoh, Teresa Coelho, Márcia Waddington-Cruz
{"title":"Effects of eplontersen on symptoms of autonomic neuropathy in hereditary transthyretin-mediated amyloidosis: secondary analysis from the NEURO-TTRansform trial.","authors":"Jonas Wixner, John L Berk, David Adams, Michael Polydefkis, Isabel Conceição, Shahram Attarian, Julian D Gillmore, P James B Dyck, Folke Folkvaljon, Wunan Zhou, Jersey Chen, Nicholas J Viney, T Jesse Kwoh, Teresa Coelho, Márcia Waddington-Cruz","doi":"10.1080/13506129.2024.2427290","DOIUrl":"10.1080/13506129.2024.2427290","url":null,"abstract":"<p><strong>Background: </strong>The NEURO-TTRansform trial showed that after 66 weeks of treatment, eplontersen significantly reduced neuropathic impairment and improved quality of life (QoL) in patients with hereditary transthyretin-mediated amyloidosis with polyneuropathy (ATTRv-PN). In this secondary analysis from NEURO-TTRansform, autonomic impairment, and the impact of eplontersen on autonomic impairment progression was evaluated through 85 weeks in patients randomised to eplontersen (<i>n</i> = 144) versus external placebo (<i>n</i> = 60; through Week 66 from the NEURO-TTR trial).</p><p><strong>Methods: </strong>Change from baseline in modified Neuropathy Impairment Score +7 (mNIS+7) composite score, Norfolk Quality of Life-Diabetic Neuropathy (Norfolk QoL-DN) total score, and the Neuropathy Symptoms and Change (NSC) total score was evaluated. Exploratory assessments were change in autonomic components of these instruments, Composite Autonomic Symptom Score-31 (COMPASS-31) total score, and nutritional status (modified body mass index [mBMI]).</p><p><strong>Results: </strong>Patients reported profound autonomic dysfunction at baseline. Improvements with eplontersen versus placebo were observed up to Week 66 in autonomic components of mNIS+7, Norfolk QoL-DN, NSC, and mBMI; eplontersen results were sustained up to Week 85, including improvements in COMPASS-31 (Week 81).</p><p><strong>Conclusions: </strong>Eplontersen demonstrated benefit across multiple measures of autonomic impairment known to progress rapidly and negatively impact QoL without treatment, without deterioration in nutritional status.</p>","PeriodicalId":50964,"journal":{"name":"Amyloid-Journal of Protein Folding Disorders","volume":" ","pages":"29-38"},"PeriodicalIF":5.2,"publicationDate":"2025-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142649726","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}
Simran Raheja, Guglielmo Verona, Paolo Florent, Nigel B Rendell, Paola Nocerino, Stephan Ellemerich, Raizel Fernandes, Nicola Botcher, Dorota Rowczenio, Janet A Gilbertson, J Paul Simons, Julian D Gillmore, Vittorio Bellotti, Graham W Taylor, Diana Canetti
{"title":"Oxidative conversion of transthyretin in formalin-fixed clinical amyloid samples results in the formation of the His90Asp and His90Asn variants.","authors":"Simran Raheja, Guglielmo Verona, Paolo Florent, Nigel B Rendell, Paola Nocerino, Stephan Ellemerich, Raizel Fernandes, Nicola Botcher, Dorota Rowczenio, Janet A Gilbertson, J Paul Simons, Julian D Gillmore, Vittorio Bellotti, Graham W Taylor, Diana Canetti","doi":"10.1080/13506129.2024.2436990","DOIUrl":"10.1080/13506129.2024.2436990","url":null,"abstract":"<p><strong>Background: </strong>Proteomics is routinely used to type clinical amyloid deposits, and offers additional benefit of identifying genetic variants, which can be diagnostically useful. Reviewing the proteomics data for ATTR patients attending our Centre revealed an unusually large number of samples containing a rare pathogenic H90D TTR variant alongside the more common H90N variant.</p><p><strong>Methods: </strong>These findings raised questions to their source. Proteomics was used to monitor the generation of H90D/H90N variants in fresh, frozen, stored samples during extraction and digestion, and also following Cu<sup>2+</sup>-mediated oxidation.</p><p><strong>Results: </strong>There was no evidence that the variants were present in the circulation, except in one patient with genetically confirmed H90D TTR, in fresh fat aspirates or tissues from an ATTR amyloid mouse model. The variant could be generated <i>in vitro</i> from both wild-type TTR and <i>ex vivo</i> ATTR fibrils by non-enzymic oxidation of histidine at position 90. These data suggest that the H90D variant can be generated artefactually from wild-type 90H TTR through a radical-mediated oxidation of histidine, followed by its conversion to asparagine and aspartic acid. This probably occurs during storage.</p><p><strong>Conclusions: </strong>In the absence of genetic data, the identification of H90D TTR in stored tissue by proteomics should be treated with caution.</p>","PeriodicalId":50964,"journal":{"name":"Amyloid-Journal of Protein Folding Disorders","volume":" ","pages":"46-53"},"PeriodicalIF":5.2,"publicationDate":"2025-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142830790","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}
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