Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Jil A. Daw"'
Autor:
Andrew R. Findlay, May M. Paing, Jil A. Daw, Meade Haller, Rocio Bengoechea, Sara K. Pittman, Shan Li, Feng Wang, Timothy M. Miller, Heather L. True, Tsui-Fen Chou, Conrad C. Weihl
Publikováno v:
Molecular Therapy: Nucleic Acids, Vol 32, Iss , Pp 937-948 (2023)
Dominant missense mutations in DNAJB6, a co-chaperone of HSP70, cause limb girdle muscular dystrophy (LGMD) D1. No treatments are currently available. Two isoforms exist, DNAJB6a and DNAJB6b, each with distinct localizations in muscle. Mutations resi
Externí odkaz:
https://doaj.org/article/98875bfcbb0241d7a450adbfdbc2b0b5
Autor:
Ankan K. Bhadra, Michael J. Rau, Jil A. Daw, James A. J. Fitzpatrick, Conrad C. Weihl, Heather L. True
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-14 (2022)
Here the authors describe mechanisms through which analogous LGMDD1 (Limb-Girdle Muscular Dystrophy Type D1) mutations affect Sis1 (a yeast functional homolog of human DNAJB6) chaperone activity and poison the function of wild-type protein; potential
Externí odkaz:
https://doaj.org/article/9cfc3a8ff8664c45baa7d3b4ce06d2f6
Autor:
Andrew R. Findlay, May M. Paing, Jil A. Daw, Rocio Bengoechea, Sara K. Pittman, Shan Li, Feng Wang, Timothy M. Miller, Heather L. True, Tsui-Fen Chou, Conrad C. Weihl
Dominant missense mutations in DNAJB6, an HSP40 co-chaperone, cause limb girdle muscular dystrophy (LGMD) D1. No treatments are currently available. Two isoforms exist, DNAJB6a and DNAJB6b, each with distinct localizations in muscle. Mutations reside
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::456b308c6f7fd816e0e1cc8af0a89474
https://doi.org/10.1101/2022.11.17.516920
https://doi.org/10.1101/2022.11.17.516920
Autor:
Ankan K. Bhadra, Michael J. Rau, Jil A. Daw, James A.J. Fitzpatrick, Conrad C. Weihl, Heather L. True
Molecular chaperones, or heat shock proteins (HSPs), protect against the toxic misfolding and aggregation of proteins. As such, mutations or deficiencies within the chaperone network can lead to disease. In fact, dominant mutations in DNAJB6 (Hsp40/S
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::379f30bbe1e3f165c4ba4201d561302d
https://doi.org/10.1101/2021.12.22.473881
https://doi.org/10.1101/2021.12.22.473881
Autor:
Ankan K. Bhadra, Michael J. Rau, Jil A. Daw, James A. J. Fitzpatrick, Conrad C. Weihl, Heather L. True
Publikováno v:
Nature communications. 13(1)
Molecular chaperones, or heat shock proteins (HSPs), protect against the toxic misfolding and aggregation of proteins. As such, mutations or deficiencies within the chaperone network can lead to disease. Dominant mutations within DNAJB6 (Hsp40)—an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b2dee85b3fc0c4bf6d527fc44f0001cb
https://pubmed.ncbi.nlm.nih.gov/35931773
https://pubmed.ncbi.nlm.nih.gov/35931773