Results 61 to 70 of about 19,748 (182)

Light-Chain (AL) Amyloidosis [PDF]

Clinical Journal of the American Society of Nephrology, 2006
Light-chain (AL) amyloidosis is the most common form of systemic amyloidosis and is associated with an underlying plasma cell dyscrasia. The disease often is difficult to recognize because of its broad range of manifestations and what often are vague symptoms.
openaire   +2 more sources

Chemistry Underlying the Behavior of Food and Agricultural Components During Industrial Manufacturing Processes and Its Implications in Quality Assurance, Food Quality, and Food Safety Management: A Systematic Review

Food Safety and Health, EarlyView.
Industrial manufacturing processes have transformative effects on the components of food matrix. These transformations in food matrix and components have direct implications for quality assurance (QA), food quality (e.g., nutritional profile and texture), and food safety management (e.g., pathogen control and toxin mitigation). ABSTRACT This systematic
Chinaza Godswill Awuchi
wiley   +1 more source

Subcutaneous scalp nodule as the presenting symptom of systemic light-chain amyloidosis

Dermatology Practical & Conceptual, 2018
We present a case of subcutaneous nodular amyloidosis mimicking a pilar cyst. Further evaluation led to the diagnosis of malignant systemic light-chain amyloidosis. The epidemiology and histopathological features of light-chain amyloidosis with cutaneous
Joseph Tadros, Stacey Goodman, Eric R. Tkaczyk   +2 more
doaj  

Mesenchymal stromal cell therapy for rheumatoid arthritis: Long‐term efficacy, safety, and mechanistic insights

Rheumatology &Autoimmunity, EarlyView.
Graphical abstract summarizing the multifactorial pathogenesis of rheumatoid arthritis (RA) and the therapeutic potential of mesenchymal stromal cell (MSC) therapy. MSCs provide promising benefits through their immunomodulatory properties, low immunogenicity, ability to promote tissue repair, and multi‐lineage differentiation, presenting a potential ...
Yingjia Chen, Ruiyu Gao, Xing Guo, Genhong Yao, Xiaojun Tang, Yile E. Liu, Lingyun Sun   +6 more
wiley   +1 more source

Amyloid‐Like Protein Assembly‐Driven Functional Materials for Enabling the Sustainable Development of Light Industry

SusMat, EarlyView.
This article covers the basic theory and regulation strategies of amyloid‐like protein assembly, reviews the research progress of amyloid‐like protein assembly‐driven functional materials in light industry fields such as food, packaging, textiles, and biocatalysis, analyzes their sustainable advantages and challenges in these applications, and offers ...
Ruirui Liu, Zuying Chen, Jian Zhao, Fengjian Wang, Changli Zeng, Peng Yang   +5 more
wiley   +1 more source

Light-chain amyloidosis with dysphagia as the main symptom: a case report

Journal of Medical Case Reports
Background Immunoglobulin light-chain amyloidosis is a relatively rare condition with a worldwide incidence of 5.1–12.8 cases per million person-years (Baker, 2022).
Maomao Ai, Tao Lin, Ruoyu Guo, Haiyao Zheng, Haiyan Deng, Feng Yu   +5 more
doaj   +1 more source

Update on treatment of light chain amyloidosis

Haematologica, 2014
Light chain amyloidosis is the most common type of amyloidosis as a consequence of protein misfolding of aggregates composed of amyloid fibrils. The clinical features are dependent on the organs involved, typically cardiac, renal, hepatic, peripheral and autonomic neuropathy and soft tissue.
S. Mahmood, V. Sanchorawala, A. Wechalekar, PALLADINI, GIOVANNI   +3 more
openaire   +4 more sources

Helical reconstruction of amyloids in cryoSPARC

Acta Crystallographica Section F, EarlyView.
We present practical guidelines for helical reconstruction of amyloid filaments in cryoSPARC, benchmarked against publicly available datasets. Our analysis defines current capabilities and limitations, and outlines optimization strategies to enable high‐throughput structural studies and therapeutic discovery.Amyloid‐mediated proteotoxicity underlies ...
Jan-Hannes Schaefer, Robert T. O'Neill, Joseph P. Donnelly, Evan T. Powers, Jeffery W. Kelly, Gabriel C. Lander   +5 more
wiley   +1 more source

Investigating transthyretin variants H88R and I107V in amyloid priming: From destabilization to complete dissociation

The FEBS Journal, EarlyView.
Investigated mutations in transthyretin (TTR) disrupt the F87‐centered hydrophobic core that stabilizes its tetrameric structure. The mild I107V mutation weakens inter‐chain packing, while H88R fully abolishes tetramer formation, yielding a monomeric, aggregation‐prone form. Structural, biophysical, and computational analyses reveal that both mutations
István L. Bódy, Zsolt Fazekas, Nóra Wágner, Anna J. Kiss‐Szemán, Veronika Harmat, Zoltán Pozsonyi, Dóra K. Menyhárd, András Perczel   +7 more
wiley   +1 more source

Utilization and Prognosis of Cardiac Device Implantation in AL Versus ATTR Amyloidosis

Pacing and Clinical Electrophysiology, EarlyView.
ABSTRACT Introduction Cardiac amyloidosis can cause congestive heart failure, arrhythmias, and heart blocks, which frequently require cardiac device implantation (CDI). However, the differences between light chain (AL) amyloidosis and transthyretin (ATTR) amyloidosis CDI requirements are unknown. Methods A retrospective analysis was conducted using the
Bilal Hussain, Sanchit Duhan, Khawaja Hassan Akhtar, Amith Reddy Seri, Krittapoom Akrawinthawong, Janardhana Gorthi, Bijeta Keisham, Tarun Dasari   +7 more
wiley   +1 more source