Results 211 to 220 of about 16,862 (246)

Neointimal Hyperplasia and Restenosis: Epidemiology, Pathophysiology, Animal Models, Clinical Features, Diagnosis, and Management

MedComm, Volume 7, Issue 11, November 2026.
The overall graphical diagram to summarize the pathological characteristics, pathogenesis, clinical manifestation, preclinical animal models, diagnostic methods, and intervention strategies for neointimal hyperplasia. Neointimal hyperplasia results from excessive proliferation and intimal migration of vascular smooth muscle cells (VSMCs) in the ...
Kaixu Wang, Daiyu Zhang, Yu Hu, Yixin Zhao, Xinling Wang, Long Jiang, Meixiu Jiang   +6 more
wiley   +1 more source

Exosomes in Cancer: The Biology, Function, Diagnosis, and Therapy

MedComm, Volume 7, Issue 11, November 2026.
Tumor‐derived exosomes and nonmembranous extracellular nanoparticles (exomeres/supermeres) constitute a heterogeneous communication network that drives cancer progression. By shuttling functional biomolecules across tissue‐specific barriers, these nanoparticles orchestrate local microenvironmental remodeling, immune suppression, premetastatic niche ...
Jun Wu, Lei Wu, Kang Yang, Kang Xie, Tao Lu, Tiangxiang Huang, Dengfeng Wan, Tao Song, Longbo Zhang   +8 more
wiley   +1 more source

A Pharmacological Chaperone Therapy for Acute Intermittent Porphyria [PDF]

Molecular Therapy, 2020
Mutations in hydroxymethylbilane synthase (HMBS) cause acute intermittent porphyria (AIP), an autosomal dominant disease where typically only one HMBS allele is mutated. In AIP, the accumulation of porphyrin precursors triggers life-threatening neurovisceral attacks and at long-term, entails an increased risk of hepatocellular carcinoma, kidney failure,
Caroline Schmitt, Sverre Sandberg, Helene J Bustad   +2 more
exaly   +5 more sources

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Pharmacological Chaperones: Beyond Conformational Disorders

Handbook of Experimental Pharmacology, 2017
Pharmacological chaperones (PCs) are small molecules that bind to nascent protein targets to facilitate their biogenesis. The ability of PCs to assist in the folding and subsequent forward trafficking of disease-causative protein misfolding mutants has opened new avenues for the treatment of conformational diseases such as cystic fibrosis and lysosomal
Nancy J Leidenheimer
exaly   +3 more sources

Screening methods for identifying pharmacological chaperones

Molecular BioSystems, 2017
Abstract Protein folding is crucial for most proteins to achieve their correct three-dimensional conformations and function properly. Defects in protein folding frequently caused by mutations lead to a range of protein misfolding diseases, including Alzheimer’s disease, Parkinson’s disease, cystic fibrosis, amyloidosis, Gaucher ...
Min Hyeon Shin, Hyun-Suk Lim
openaire   +3 more sources

Pharmacological Chaperone Therapy for Lysosomal Storage Diseases

Future Medicinal Chemistry, 2014
Pharmacological chaperone therapy is an emerging approach to treat lysosomal storage diseases. Small-molecule chaperones interact with mutant enzymes, favor their correct conformation and enhance their stability. This approach shows significant advantages when compared with existing therapies, particularly in terms of the bioavailability of drugs, oral
PARENTI, GIANCARLO, MORACCI, Marco, FECAROTTA, SIMONA, ANDRIA, GENEROSO   +3 more
openaire   +6 more sources

Pharmacological Chaperones as Therapeutics for Lysosomal Storage Diseases

Journal of Medicinal Chemistry, 2013
Lysosomal enzymes are responsible for the degradation of a wide variety of glycolipids, oligosaccharides, proteins, and glycoproteins. Inherited mutations in the genes that encode these proteins can lead to reduced stability of newly synthesized lysosomal enzymes.
Robert E, Boyd, Gary, Lee, Philip, Rybczynski, Elfrida R, Benjamin, Richie, Khanna, Brandon A, Wustman, Kenneth J, Valenzano   +6 more
openaire   +2 more sources

Pharmacological chaperones: potential treatment for conformational diseases

Trends in Endocrinology & Metabolism, 2004
Increasing numbers of inherited diseases are found to result from mutations that lead to misfolded proteins. In many cases, the changes in conformation are relatively modest and the function of the protein would not be predicted to be affected. Yet, these proteins are recognized as "misfolded" and degraded prematurely.
Virginie, Bernier, Monique, Lagacé, Daniel G, Bichet, Michel, Bouvier   +3 more
openaire   +2 more sources

Chemical and pharmacological chaperones as new therapeutic agents

Expert Reviews in Molecular Medicine, 2007
Proteins that are exported from the cell, or targeted to the cell surface or other organelles, are synthesised and assembled in the endoplasmic reticulum and then delivered to their destinations. Point mutations – the most common cause of human genetic diseases – can inhibit folding and assembly of the protein in the endoplasmic reticulum. The unstable
Tip W, Loo, David M, Clarke
openaire   +2 more sources

Pharmacological chaperones: a new twist on receptor folding

Trends in Pharmacological Sciences, 2000
Protein misfolding is at the root of several genetic human diseases. These diseases do not stem from mutations within the active domain of the proteins, but from mutations that disrupt their three-dimensional conformation, which leads to their intracellular retention by the quality control apparatus of the cell.
J P, Morello, U E, Petäjä-Repo, D G, Bichet, M, Bouvier   +3 more
openaire   +2 more sources