Zobrazeno 1 - 10
of 78
pro vyhledávání: '"James S Foster"'
Autor:
Stephen J Kennel, Joseph W Jackson, Alan Stuckey, Tina Richey, James S Foster, Jonathan S Wall
Publikováno v:
PLoS ONE, Vol 19, Iss 4, p e0301756 (2024)
IntroductionAmyloid deposition is a cause of restrictive cardiomyopathy. Patients who present with cardiac disease can be evaluated for transthyretin (TTR)-associated cardiac amyloidosis using nuclear imaging with 99mTc-labeled pyrophosphate (PYP); h
Externí odkaz:
https://doaj.org/article/ae00333921e540a68f07fb68eada90da
Autor:
Helen P McWilliams-Koeppen, James S Foster, Nicole Hackenbrack, Marina Ramirez-Alvarado, Dallas Donohoe, Angela Williams, Sallie Macy, Craig Wooliver, Dale Wortham, Jennifer Morrell-Falvey, Carmen M Foster, Stephen J Kennel, Jonathan S Wall
Publikováno v:
PLoS ONE, Vol 10, Iss 9, p e0137716 (2015)
Light chain (AL) amyloidosis is the most common form of systemic amyloid disease, and cardiomyopathy is a dire consequence, resulting in an extremely poor prognosis. AL is characterized by the production of monoclonal free light chains that deposit a
Externí odkaz:
https://doaj.org/article/7182f06f22c546f9ac3476127cafd2be
Autor:
Pranay Dogra, Emily B Martin, Angela Williams, Raphael L Richardson, James S Foster, Nicole Hackenback, Stephen J Kennel, Tim E Sparer, Jonathan S Wall
Publikováno v:
PLoS ONE, Vol 10, Iss 5, p e0126239 (2015)
Human cytomegalovirus (HCMV) infection can lead to congenital hearing loss and mental retardation. Upon immune suppression, reactivation of latent HCMV or primary infection increases morbidity in cancer, transplantation, and late stage AIDS patients.
Externí odkaz:
https://doaj.org/article/02856b0633474fbfa83ccefa93f6dfdf
Autor:
James S. Foster, Manasi Balachandran, Trevor J. Hancock, Emily B. Martin, Sallie Macy, Craig Wooliver, Tina Richey, Alan Stuckey, Angela D. Williams, Joseph W. Jackson, Stephen J. Kennel, Jonathan S. Wall
Publikováno v:
Frontiers in Immunology, Vol 14 (2023)
IntroductionSystemic amyloidosis is a progressive disorder characterized by the extracellular deposition of amyloid fibrils and accessory proteins in visceral organs and tissues. Amyloid accumulation causes organ dysfunction and is not generally clea
Externí odkaz:
https://doaj.org/article/3ce636148a204e3aafd0f0efaec0fd54
Autor:
Emily B. Martin, Alan Stuckey, Dustin Powell, Ronald Lands, Bryan Whittle, Craig Wooliver, Sallie Macy, James S. Foster, Spencer Guthrie, Stephen J. Kennel, Jonathan S. Wall
Publikováno v:
Pharmaceuticals, Vol 16, Iss 4, p 629 (2023)
There are at least 20 distinct types of systemic amyloidosis, all of which result in the organ-compromising accumulation of extracellular amyloid deposits. Amyloidosis is challenging to diagnose due to the heterogeneity of the clinical presentation,
Externí odkaz:
https://doaj.org/article/0c7a66e5b85e4db4a58eeeaf99099fad
Autor:
Joseph W. Jackson, James S. Foster, Emily B. Martin, Sallie Macy, Craig Wooliver, Manasi Balachandran, Tina Richey, R. Eric Heidel, Angela D. Williams, Stephen J. Kennel, Jonathan S. Wall
Publikováno v:
Amyloid. :1-12
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bd06c6460612ca06556a2071d6bbb6f9
https://doi.org/10.1080/13506129.2022.2155133
https://doi.org/10.1080/13506129.2022.2155133
Autor:
James S. Foster, Anna B. Williams, Dianne J. Trent, Tina Richey, Emily B. Martin, Siva Karthik Varanasi, Alexa Stroh, Stephen A. Kania, Jonathan S. Wall, Craig Wooliver, Sallie Macy, Elizabeth N. Ergen, Stephen J. Kennel, Angela Williams, R. Eric Heidel
Publikováno v:
Am J Pathol
Light chain–associated amyloidosis is characterized by the extracellular deposition of amyloid fibrils in abdominothoracic organs, skin, soft tissue, and peripheral nerves. Phagocytic cells of the innate immune system appear to be ineffective at cl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::264c1f99489876c1c8a39db2c41244c5
https://doi.org/10.1016/j.ajpath.2019.01.011
https://doi.org/10.1016/j.ajpath.2019.01.011
Autor:
Tina Richey, Alan Stuckey, Emily B. Martin, Angela Williams, James S. Foster, Craig Wooliver, Jonathan S. Wall, Stephen J. Kennel
Publikováno v:
Journal of Translational Medicine, Vol 15, Iss 1, Pp 1-11 (2017)
Journal of Translational Medicine
Journal of Translational Medicine
Background Systemic amyloidoses comprise diseases characterized by the deposition of proteinaceous material known as amyloid. Currently, without performing multiple biopsies, there is no way to ascertain the extent of amyloid deposition in patients
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9323e925034fdb7f8db19e05584f8987
http://link.springer.com/article/10.1186/s12967-017-1351-0
http://link.springer.com/article/10.1186/s12967-017-1351-0
Autor:
James S. Foster, Spencer D. Guthrie, Sébastien Bender, Frank Bridoux, Suganya Selvarajah, Jonathan S. Wall, Arnaud Jaccard, Angela Williams, Christophe Sirac, Gemma Martinez-Rivas, Gregory D Bell, Stephen J. Kennel, Roussine Codo
Publikováno v:
Blood. 138:1207-1207
Background: Amyloidosis is characterized by extracellular deposition of protein fibrils that can involve any organ or tissue in the body. It is a severe, progressive and often lethal disorder. There are approximately seventeen different systemic amyl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::79c7533d24aaf402a718cf62efa88e21
https://doi.org/10.1182/blood-2021-151908
https://doi.org/10.1182/blood-2021-151908
Autor:
Yitong Fu, James S. Foster, Alan Stuckey, Angela Williams, Dustin Powell, Tina Richey, Bryan Whittle, Emily B. Martin, Spencer D. Guthrie, Jonathan S. Wall, Ronald H. Lands, R. Eric Heidel, Stephen J. Kennel
Publikováno v:
Blood. 136:17-18
Background: Systemic immunoglobulin light chain-associated amyloidosis (AL) is a rare disorder associated with the production of monoclonal free light chain proteins. The aggregation of misfolded light chains leads to the extracellular deposition of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::49036d5ed89cae1c33c34f633f90751a
https://doi.org/10.1182/blood-2020-143307
https://doi.org/10.1182/blood-2020-143307