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amyloid PhD Projects, Programs & Scholarships

We have 22 amyloid PhD Projects, Programs & Scholarships

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  An integrated approach to the study of cellular interactions with amyloid
  Research Group: Astbury Centre for Structural Molecular Biology
  Dr E W Hewitt, Prof S E Radford
Applications accepted all year round

Funding Type

PhD Type

The formation of insoluble amyloid fibrils is associated with a spectrum of human disorders, the amyloidoses, which include Alzheimer’s, Parkinson’s, type 2 diabetes and dialysis related amyloidosis (DRA).
  Mass spectrometry analysis of human tissue to characterise cleavage events resulting in amyloid deposition associated with aortic aneurysm and dissection
  Dr J Madine, Prof C E Eyers
Applications accepted all year round

Funding Type

PhD Type

The most common form of localised amyloid occurs in the aorta (aortic medial amyloid; AMA) and is estimated to occur in 97% of Caucasian people over 50.
  Computer simulation of metal-amyloid interaction and its role in plaque formation
  Dr J Platts
Applications accepted all year round

Funding Type

PhD Type

Alzheimer’s disease is one of the greatest healthcare challenges facing 21st century society. AD is associated with formation of fibrils and plaques in brain tissue that impair proper functioning of neurons.
  Investigating the links between osteoporosis & Alzheimer’s disease – effects of β-amyloid upon the mechanical set-point in bone
  Dr S McArthur, Dr SCF Rawlinson
Applications accepted all year round

Funding Type

PhD Type

Background. Individuals with Alzheimer’s disease are more likely to suffer from osteoporosis (the loss of bone mass and strength) than age-matched individuals; significantly contributing to the frailty associated with dementia.
  Investigating the link between amyloid-β oligomers, neuroinflammation and cognitive deficits in preclinical models for Alzheimer’s Disease
  Dr M Harte, Prof J Neill
Applications accepted all year round

Funding Type

PhD Type

Currently four out of the five pharmacological treatments used for Alzheimer’s disease (AD) are acetylcholinesterase inhibitors aimed at boosting the amount of acetylcholine in the brain, with the fifth being an N-methyl-D-aspartate (NMDA) receptor antagonist.
  Cryo-EM structural analysis of amyloid fibrils
  Prof M Fändrich, Dr M Schmidt
Applications accepted all year round

Funding Type

PhD Type

The Institute of Protein Biochemistry at Ulm University, Germany, investigates the molecular basis of amyloid diseases, such as Alzheimer’s disease and systemic amyloidosis.
  Protein Misfolding and the Molecular Basis of Alzheimer’s Disease
  Dr J Viles
Applications accepted all year round

Funding Type

PhD Type

Background. World-wide one in three people over the age of 65 will die with Alzheimer’s Disease (AD). The disease is characterised by deposits of amyloid plaques and fibrils of amyloid-beta peptide (Ab) are their main constituent.
  Characterisation of the neuronal receptor for soluble amyloid precursor protein: a route to new therapeutic targets for Alzheimer’s disease
  Prof N Hooper, Prof M J Humphries
Applications accepted all year round

Funding Type

PhD Type

Alzheimer’s disease (AD) is the commonest form of dementia for which currently there is no means of stopping or even slowing the disease.
  Inhibiting amyloid development using natural compounds: a molecular dynamics study
  Dr P Mulheran, Dr V A Ferro
Applications accepted all year round

Funding Type

PhD Type

Amyloid fibrils are highly ordered protein aggregates associated with many neurodegenerative diseases such as Alzheimer’s. Flavanoids, which are polyphenols such as curcumin present in the human diet, have been shown to inhibit fibril formation in tau protein which is abundant in neurons.
  Screening of chemical libraries using iPS models for investigating the role of prion protein in Alzheimer’s disease
  Prof B Chen
Applications accepted all year round

Funding Type

PhD Type

Background. AD has been identified as a protein misfolding disease (proteopathy). The disease is caused by accumulation of two major amyloids.
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