Protein aggregation is typical of neurodegenerative diseases such as Alzheimer's, Parkinson's and prion diseases such as ...

A lipid anchor on nerve cell membranes stabilizes prion proteins (PrPC) and prevents their pathological aggregation into forms linked to prion diseases.

Researchers at Ruhr University Bochum discovered that a lipid anchor on nerve cell membranes stabilizes prion protein folding ...

Protein aggregation is typical of various neurodegenerative diseases such as Alzheimer's, Parkinson's and prion diseases such as Creutzfeld-Jakob disease. A research team has now used new in vitro and ...

Protein aggregation is typical of various neurodegenerative diseases such as Alzheimer’s, Parkinson’s and prion diseases such ...

Researchers have gained valuable insight into the development of prion diseases of the brain.Protein aggregation is typical of various ...

Do "prions" exist? The word "prion" is used ... a protein molecule folded in an abnormal way can alter the folding of another protein molecule and thereby change its biological properties.

Protein folding is the process by which proteins achieve their mature functional (native) tertiary structure, and often begins co-translationally. Protein folding requires chaperones and often ...

[3,4,5,6,7,8,9] They appear to be constituted by proteins ... in folding abnormalities, and that different conformations have been detected by Western blot analysis in prion proteins.

How proteins achieve their correct shape is the subject of this special Focus. For those who practice the traditional Japanese art of paper folding, or origami, a sheet of paper can be used to ...

Protein folding has been an ongoing problem for researchers since 1972. Christian Anfinsen speculated in his Nobel Prize acceptance speech in that year that the three-dimensional structure of a ...

The biomarker development pipeline is generally composed of three stages: biomarker discovery, verification and clinical validation (Figure 1). The process begins with biomarker discovery where ...