Combining nano-physical and computational investigations to understand the nature of “aging” in dermal collagen

Autor: Ahmed T, Nash A, Clark KEN, Ghibaudo M, de Leeuw NH, Potter A, Stratton R, Birch HL, Enea Casse R, Bozec L

Publikováno v: International Journal of Nanomedicine, Vol Volume 12, Pp 3303-3314 (2017)

Tarek Ahmed,1 Anthony Nash,2 Kristina EN Clark,3 Marion Ghibaudo,4 Nora H de Leeuw,2 Anne Potter,4 Richard Stratton,3 Helen L Birch,5 Ramona Enea Casse,4 Laurent Bozec1 1Division of Biomaterials and Tissue Engineering, Eastman Dental Institute, Unive

Externí odkaz: https://doaj.org/article/8c3822cab3d34291976c29951fc49176

Chemical Markers of Human Tendon Health Identified Using Raman Spectroscopy: Potential for In Vivo Assessment.

Autor: Yin NH; Department of Orthopaedics and Musculoskeletal Science, University College London, UCL Stanmore Campus, RNOH, Brockley Hill, London HA7 4LP, UK., Parker AW; Central Laser Facility, Research Complex at Harwell, Science and Technology Facilities Council, Rutherford Appleton Laboratory, UKRI, Harwell Campus, Didcot OX11 0QX, UK., Matousek P; Central Laser Facility, Research Complex at Harwell, Science and Technology Facilities Council, Rutherford Appleton Laboratory, UKRI, Harwell Campus, Didcot OX11 0QX, UK., Birch HL; Department of Orthopaedics and Musculoskeletal Science, University College London, UCL Stanmore Campus, RNOH, Brockley Hill, London HA7 4LP, UK.

Publikováno v: International journal of molecular sciences [Int J Mol Sci] 2022 Nov 27; Vol. 23 (23). Date of Electronic Publication: 2022 Nov 27.

Effect on the mechanical properties of type I collagen of intra-molecular lysine-arginine derived advanced glycation end-product cross-linking

Autor: Collier, TA, Nash, A, Birch, HL, de Leeuw, NH

Publikováno v: Journal of Biomechanics

Non-enzymatic advanced glycation end product (AGE) cross-linking of collagen molecules has been hypothesised to result in significant changes to the mechanical properties of the connective tissues within the body, potentially resulting in a number of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::b86029bf79b92daaed41841d5a052c72
https://orca.cardiff.ac.uk/id/eprint/107407/8/1-s2.0-S0021929017306723-main.pdf

Structure-function specialisation of the interfascicular matrix in the human achilles tendon.

Autor: Patel D; Institute of Bioengineering, School of Engineering and Materials Science, Queen Mary University of London, Mile End Road, London E1 4NS, UK., Zamboulis DE; Department of Musculoskeletal and Ageing Science, Institute of Life Course and Medical Sciences, University of Liverpool, West Derby Street, Liverpool L7 8TX, UK., Spiesz EM; Department of Bionanoscience, Delft University of Technology, Building 58, Van der Maasweg 9, 2629 HZ Delft, the Netherlands., Birch HL; Institute of Orthopaedics and Musculoskeletal Science, UCL, Stanmore Campus, Brockley Hill, Stanmore, Middlesex, HA7 4LP, UK., Clegg PD; Department of Musculoskeletal and Ageing Science, Institute of Life Course and Medical Sciences, University of Liverpool, West Derby Street, Liverpool L7 8TX, UK; The Medical Research Council Versus Arthritis Centre for Integrated Research into Musculoskeletal Ageing (CIMA), University of Liverpool, West Derby Street, Liverpool L7 8TX, UK., Thorpe CT; Department of Comparative Biomedical Sciences, Royal Veterinary College, Royal College Street, London NW1 0TU, UK., Screen HRC; Institute of Bioengineering, School of Engineering and Materials Science, Queen Mary University of London, Mile End Road, London E1 4NS, UK. Electronic address: h.r.c.screen@qmul.ac.uk.

Publikováno v: Acta biomaterialia [Acta Biomater] 2021 Sep 01; Vol. 131, pp. 381-390. Date of Electronic Publication: 2021 Jul 13.

Computational study of glucosepane-water and hydrogen bond formation: an electron topology and orbital analysis

Autor: Nash, A, Saßmannshausen, J, Bozec, L, Birch, HL, de Leeuw, NH

The collagen protein provides tensile strength to the extracellular matrix in addition to localising cells, proteins and protein cofactors. Collagen is susceptible to a build up of glycation modifications as a result of an exceptionally long half-lif

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::0b30a1fe24cd7952148328d6e96fd800