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amyloid PhD Projects, Programs & Scholarships

We have 26 amyloid PhD Projects, Programs & Scholarships

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  Mapping the molecular mechanisms of chaperone-catalysed division of amyloid fibrils
  Dr W-F Xue, Prof M F Tuite
Application Deadline: 4 February 2019
PhD STUDENTSHIP STARTING Sept 2019. LOCATION. Kent Fungal Group, School of Biosciences, University of Kent, Canterbury. How do molecular chaperones interact and fragment amyloid fibrils in cells? This is the central question that this PhD project will address.
  Nanoinjection: a single molecule platform for the quantitative and targeted delivery of amyloid oligomers and fibrils into cells for functional analysis
  Dr E W Hewitt, Dr P Actis, Prof S E Radford
Application Deadline: 7 January 2019
Interested in amyloid disorders such as Parkinson’s and Huntington’s. Want to work with cutting edge technology in a multidisciplinary team.
  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
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).
  MRC DiMeN Doctoral Training Partnership: 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 Eyers
Application Deadline: 21 January 2019
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
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
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.
  Chemical tools as modulators of amyloid formation
  Research Group: BBSRC White Rose DTP
  Dr R Foster, Prof S E Radford
Application Deadline: 7 January 2019
The inherent ability of proteins to aggregate into amyloid fibrils underlies more than fifty human diseases. The misassembly of soluble proteins into toxic aggregates underlies a variety of conditions including AD and Type-2 diabetes.
  Capturing how Hsp90 prevents the formation of cell-disruptive toxic amyloid species by Cryo-EM in a C. elegans model for Alzheimer’s Disease
  Research Group: BBSRC White Rose DTP
  Dr P van Oosten-Hawle, Prof N A Ranson, Dr E W Hewitt
Application Deadline: 7 January 2019
Stress and aging challenge the health of a proteome and increase susceptibility to protein conformational diseases, a hallmark of many neurodegenerative diseases, including Alzheimer’s Disease.
  Cryo-EM studies of amyloid fibrils and their mechanisms of formation in vitro and in vivo
  Research Group: BBSRC White Rose DTP
  Prof S E Radford, Prof N A Ranson
Application Deadline: 7 January 2019
Amyloidosis is a pathological condition associated with the aggregation of proteins into fibrils, and is the underlying pathology in diseases such as Alzheimer’s and Parkinsons diseases.
  Inhibiting protein-protein interactions in the early stages of amyloid formation
  Research Group: BBSRC White Rose DTP
  Prof F. Sobott, Prof S E Radford
Application Deadline: 7 February 2019
Amyloidosis is a pathological condition associated with the aggregation of proteins into fibrils. Despite the importance of amyloid diseases in today’s society, therapies remain remote, due to a lack of understanding of some of the fundamental molecular processes involved.
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