نتایج جستجو برای: hspb1

تعداد نتایج: 443  

2014
André-Patrick Arrigo Benjamin Gibert

Human small heat shock proteins are molecular chaperones that regulate fundamental cellular processes in normal unstressed cells as well as in many cancer cells where they are over-expressed. These proteins are characterized by cell physiology dependent changes in their oligomerization and phosphorylation status. These structural changes allow them to interact with many different client protein...

Journal: :Environmental Health Perspectives 1996
D L Ashley M A Bonin F L Cardinali J M McCraw J V Wooten

Mutations of human αB-crystallin cause congenital cataract and cardio-myopathy by protein aggregation and cell death. How mutations of αB-crystallin become pathogenic is poorly understood. To better understand the cellular events related to protein aggregation and cell death, we transfected cataract and cardio-myopathy causing mutants, R11H, P20S, R56W, D109H, R120G, D140N, G154S, R157H and A17...

2016
Mitsuru Okuno Seiji Adachi Osamu Kozawa Masahito Shimizu Ichiro Yasuda William Chi-shing Cho

Pancreatic cancer is one of most aggressive forms of cancer. After clinical detection it exhibits fast metastatic growth. Heat shock protein 27 (HSP27; HSPB1) has been characterized as a molecular chaperone which modifies the structures and functions of other proteins in cells when they are exposed to various stresses, such as chemotherapy. While the administration of gemcitabine, an anti-tumor...

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