Results 231 to 240 of about 3,403,581 (279)

Sestrin2 drives ER-phagy in response to protein misfolding.

Dev Cell
De Leonibus C, Maddaluno M, Ferriero R, Besio R, Cinque L, Lim PJ, Palma A, De Cegli R, Gagliotta S, Montefusco S, Iavazzo M, Rohrbach M, Giunta C, Polishchuk E, Medina DL, Di Bernardo D, Forlino A, Piccolo P, Settembre C.   +18 more
europepmc   +1 more source

GLUT1 Deficiency Syndrome with Coexistent Movement Disorder and Anemia

Movement Disorders Clinical Practice, Volume 13, Issue 9, Page 2281-2283, September 2026.
Sangeetha Yoganathan, Haya S AlFaris, Anika Menetrey, Sayoni Roy Chowdhury, Lindsey Vogt, Jolynn Dickson, Karen Owusu, Pradeep Krishnan, Suvasini Sharma, Liali Aljouda, Reena Pabari, Grace Yoon, Carolina Gorodetsky   +12 more
wiley   +1 more source

Fitness defects due to cytosolic protein misfolding in S. cerevisiae can be alleviated by decreasing mitochondrial protein import capacity

Zaidi Z, Dash DP, Sharma A, Kundu S, Bhatt S, Rao S, Padia K, Rai M, Chakraborty K.   +8 more
europepmc   +1 more source

Protein misfolding in neurodegenerative diseases

Neuropathology and Applied Neurobiology, 2004
A common pathogenic mechanism shared by diverse neurodegenerative disorders, like Alzheimer's disease, Parkinson's disease, Huntington's disease and transmissible spongiform encephalopathies, may be altered protein homeostasis leading to protein misfolding and aggregation of a wide variety of different proteins in the form of insoluble fibrils ...
E I, Agorogiannis, G I, Agorogiannis, A, Papadimitriou, G M, Hadjigeorgiou   +3 more
openaire   +3 more sources

Protein Misfolding Cyclic Amplification

, 2012
Prion diseases are caused by a conformational conversion of the cellular prion protein (PrPC) to a pathological conformer (PrPSc). The “prion-only” hypothesis suggests that PrPSc is the infectious agent that propagates the disease acting as a template for the conversion of PrPC.
Moda F., Pritzkow S., Soto C.
openaire   +4 more sources

Mechanisms of protein misfolding: Novel therapeutic approaches to protein-misfolding diseases [PDF]

Journal of Molecular Structure, 2016
In protein misfolding, protein molecule acquires wrong tertiary structure, thereby induces protein misfolding diseases. Protein misfolding can occur through various mechanisms. For instance, changes in environmental conditions, oxidative stress, dominant
Ali Saber Abdelhameed, Mohammad Khursheed Siddiqi, Rizwan Hasan Khan   +2 more
exaly   +2 more sources

Cell death: protein misfolding and neurodegenerative diseases [PDF]

Apoptosis: an International Journal on Programmed Cell Death, 2009
Several chronic neurodegenerative disorders manifest deposits of misfolded or aggregated proteins. Genetic mutations are the root cause for protein misfolding in rare families, but the majority of patients have sporadic forms possibly related to ...
Stuart Lipton, Tomohiro Nakamura
exaly   +2 more sources

Protein Misfolding Diseases and Therapeutic Approaches

Current Protein and Peptide Science, 2019
Protein folding is the process by which a polypeptide chain acquires its functional, native 3D structure. Protein misfolding, on the other hand, is a process in which proteins fails to fold into its native functional conformation.
Anurag Yadav, Kusum Yadav, Upendra Nath Dwivedi   +2 more
exaly   +2 more sources

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Protein Misfolding and Aggregation

Biotechnology Progress, 2008
Interest in the problem of protein misfolding and aggregation has exploded in recent years for two reasons: (1) the sharp rise in the number and volume of therapeutic proteins produced commercially and (2) the recognition of the central role of protein aggregates in degenerative diseases.
Regina M, Murphy, Brent S, Kendrick
openaire   +2 more sources

Protein misfolding and disease; protein refolding and therapy [PDF]

FEBS Letters, 2001
Diverse human disorders, including several neurodegenerative diseases and systemic amyloidosis, are thought to arise from the misfolding and aggregation of an underlying protein.
Claudio Soto
exaly   +2 more sources