Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Howard Doong"'
Autor:
Teh Ying Chou, Howard Doong, Hsiang Ling Ho, Mei Yu Chen, Chun-Ming Tsai, Yi Chen Yeh, Chao Hua Chiu
Publikováno v:
Oncotarget
A significant fraction of patients with lung adenocarcinomas harboring activating epidermal growth factor receptor (EGFR) mutations do not experience clinical benefits from EGFR tyrosine kinase inhibitor (TKI) therapy. Using next-generation sequencin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1ff1d3338b9fffcc13f04eea8008df71
https://doi.org/10.18632/oncotarget.3511
https://doi.org/10.18632/oncotarget.3511
Autor:
Hongmin Wang, Deepa Srinivasan, Shengyun Fang, Precious J. Lim, Jing Liang, Yihong Ye, Mervyn J. Monteiro, Rebecca Danner, Howard Doong, Cara Rothenberg, Christine A. Harman
Publikováno v:
The Journal of Cell Biology
Loss of ubiquilin or erasin activates ER stress, increases accumulation of polyubiquitinated proteins, and shortens lifespan in worms.
Unwanted proteins in the endoplasmic reticulum (ER) are exported into the cytoplasm and degraded by the protea
Unwanted proteins in the endoplasmic reticulum (ER) are exported into the cytoplasm and degraded by the protea
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::af52d0fdeeadc4d2cc063bc82077b219
https://doi.org/10.1083/jcb.200903024
https://doi.org/10.1083/jcb.200903024
Characterization of erasin (UBXD2): a new ER protein that promotes ER-associated protein degradation
Autor:
Corrine Peterhoff, Ralph A. Nixon, Chaobo Yin, Howard Doong, Mervyn J. Monteiro, Shengyun Fang, Jing Liang
Publikováno v:
Journal of Cell Science. 119:4011-4024
Ubiquitin regulator-X (UBX) is a discrete protein domain that binds p97/valosin-containing protein (VCP), a molecular chaperone involved in diverse cell processes, including endoplasmic-reticulum-associated protein degradation (ERAD). Here we charact
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0a6333f1c467592f4a0cee6bf013ea94
https://doi.org/10.1242/jcs.03163
https://doi.org/10.1242/jcs.03163
Autor:
Howard Doong, Jaime Miller, Jing Liang, Leann K. Massey, Mervyn J. Monteiro, Diana L. Ford, Alex L. Mah
Publikováno v:
Journal of Alzheimer's Disease. 6:79-92
Mutations in presenilin proteins (PS1 and PS2) are associated with most cases of early-onset Alzheimer's disease. Several proteins appear to regulate accumulation of PS proteins in cells. One such protein is ubiquilin-1, which increases levels of coe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ca07ee6dcfd024f1e2fb836b8493de85
https://doi.org/10.3233/jad-2004-6109
https://doi.org/10.3233/jad-2004-6109
Publikováno v:
Journal of Biological Chemistry. 278:28490-28500
BAG family proteins are regulatory co-chaperones for heat shock protein (Hsp) 70. Hsp70 facilitates the removal of injured proteins by ubiquitin-mediated proteasomal degradation. This process can be driven by geldanamycin, an irreversible blocker of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9c9f363b76d1c2523826990e2249016a
https://doi.org/10.1074/jbc.m209682200
https://doi.org/10.1074/jbc.m209682200
Publikováno v:
Journal of the American College of Surgeons. 225:S160
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::eeefc5521e1a308ecd98c5b1e70deb24
https://doi.org/10.1016/j.jamcollsurg.2017.07.359
https://doi.org/10.1016/j.jamcollsurg.2017.07.359
Publikováno v:
Biochemical and biophysical research communications. 352(4)
Endoplasmic reticulum (ER) stress-induced accumulation of misfolded proteins in the ER stimulates the ER-associated degradation (ERAD) process. ERAD in turn eliminates those misfolded proteins. Upregulation of ubiquitination enzymes is an essential m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8b27f87a4c4aa5404672d86d7b365e82
https://pubmed.ncbi.nlm.nih.gov/17157811
https://pubmed.ncbi.nlm.nih.gov/17157811
Publikováno v:
Experimental cell research. 312(15)
CAIR-1/BAG-3 is a stress and survival protein that has been shown to bind SH3 domain-containing proteins through its proline-rich (PXXP) domain. Because stress and survival pathways are active during invasion and metastasis, we hypothesized that CAIR
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::518c82e9a3ee9319a367d140d7622877
https://pubmed.ncbi.nlm.nih.gov/16859681
https://pubmed.ncbi.nlm.nih.gov/16859681
Publikováno v:
The Journal of biological chemistry. 278(31)
BAG family proteins are regulatory co-chaperones for heat shock protein (Hsp) 70. Hsp70 facilitates the removal of injured proteins by ubiquitin-mediated proteasomal degradation. This process can be driven by geldanamycin, an irreversible blocker of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::f976b3a4b3bbf0c5f17ba1bce38b92cb
https://pubmed.ncbi.nlm.nih.gov/12750378
https://pubmed.ncbi.nlm.nih.gov/12750378