Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Andrew L, Hellewell"'
Publikováno v:
Hellewell, A L, Heesom, K J, Jepson, M A & Adams, J C 2022, ' PDIA3/ERp57 promotes a matrix-rich secretome that stimulates fibroblast adhesion through CCN2 ', American journal of physiology. Cell physiology, vol. 322, no. 4, pp. C624–C644 . https://doi.org/10.1152/ajpcell.00258.2021
The matricellular glycoprotein thrombospondin-1 (TSP1) has complex roles in the extracellular matrix (ECM) and at cell surfaces, but relatively little is known about its intracellular associations prior to secretion. To search for novel intracellular
Publikováno v:
PLoS ONE, Vol 9, Iss 6, p e98900 (2014)
Natural killer (NK) cell secretory lysosome exocytosis and cytotoxicity are impaired in familial hemophagocytic lymphohistiocytosis type 4 (FHL-4), a disorder caused by mutations in the gene encoding the SNARE protein syntaxin 11. We show that syntax
Externí odkaz:
https://doaj.org/article/d84c2a0f3340464e836f669a068d5f60
Autor:
Mark, Lommel, Jennifer, Strompen, Andrew L, Hellewell, Gnana Prakash, Balasubramanian, Elena D, Christofidou, Andrew R, Thomson, Aimee L, Boyle, Derek N, Woolfson, Kane, Puglisi, Markus, Hartl, Thomas W, Holstein, Josephine C, Adams, Suat, Özbek
Publikováno v:
Scientific Reports
Thrombospondins (TSPs) are multidomain glycoproteins with complex matricellular functions in tissue homeostasis and remodeling. We describe a novel role of TSP as a Wnt signaling target in the basal eumetazoan Hydra. Proteome analysis identified Hydr
Publikováno v:
Adams, J C & Hellewell, A L 2016, ' Insider Trading : Extracellular Matrix Proteins and their Non-Canonical Intracellular Roles ', BioEssays, vol. 38, no. 1, pp. 77-88 . https://doi.org/10.1002/bies.201500103
In metazoans, the extracellular matrix (ECM) provides a dynamic, heterogeneousmicroenvironment that has important supportive and instructive roles. Although the primary site of action of ECM proteins is extracellular, evidence is emerging for noncano
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::24b3ac8f7cbc5a8d1fe07aae5bd5a59a
https://research-information.bris.ac.uk/ws/files/53679989/AcceptedPaperHellewellandAdamsBioEssays2015.pdf
https://research-information.bris.ac.uk/ws/files/53679989/AcceptedPaperHellewellandAdamsBioEssays2015.pdf
Autor:
Sheena E. Radford, Walraj S. Gosal, Andrew L. Hellewell, Eric W. Hewitt, Wei-Feng Xue, Steve W. Homans
Publikováno v:
The Journal of Biological Chemistry
Fibrils associated with amyloid disease are molecular assemblies of key biological importance, yet how cells respond to the presence of amyloid remains unclear. Cellular responses may not only depend on the chemical composition or molecular propertie
Autor:
Toral, Jakhria, Andrew L, Hellewell, Morwenna Y, Porter, Matthew P, Jackson, Kevin W, Tipping, Wei-Feng, Xue, Sheena E, Radford, Eric W, Hewitt
Publikováno v:
The Journal of Biological Chemistry
Background: The causative agents and pathological mechanisms of amyloid disease are poorly understood. Results: β2-Microglobulin amyloid fibrils display length-dependent internalization, alter trafficking of lysosomal membrane proteins, and inhibit
Autor:
Lilia Milanesi, Tania Sheynis, Andrew L. Hellewell, Helen R. Saibil, Eric W. Hewitt, Wei-Feng Xue, Sheena E. Radford, Raz Jelinek, Elena V. Orlova
Protein misfolding and aggregation cause serious degenerative conditions such as Alzheimer’s, Parkinson, and prion diseases. Damage to membranes is thought to be one of the mechanisms underlying cellular toxicity of a range of amyloid assemblies. P
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fb57e5dabb940c25a01ff1d02f8b8a48
Autor:
Sheena E. Radford, Geoffrey W. Platt, Steve W. Homans, Lucy A. Woods, Andrew L. Hellewell, Alison E. Ashcroft, Eric W. Hewitt
Publikováno v:
Nature chemical biology
Although small molecules that modulate amyloid formation in vitro have been identified, significant challenges remain in determining precisely how these species act. Here we describe the identification of rifamycin SV as a potent inhibitor of β(2) m
Amyloid assemblies are associated with several debilitating human disorders. Understanding the intra- and extracellular assembly of normally soluble proteins and peptides into amyloid aggregates and how they disrupt normal cellular functions is there
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::551d840c8b20a019b61a68eabbf7f7cd
Autor:
Eric W. Hewitt, Andrew L. Hellewell, Wei-Feng Xue, Tania Sheynis, Anat Friediger, Kevin W. Tipping, Sheena E. Radford, Raz Jelinek
Publikováno v:
Biophysical Journal. (3):745-755
Amyloid fibril accumulation is a pathological hallmark of several devastating disorders, including Alzheimer’s disease, prion diseases, type II diabetes, and others. Although the molecular factors responsible for amyloid pathologies have not been d