Zobrazeno 1 - 10
of 26
pro vyhledávání: '"Pamela, Osenkowski"'
Autor:
Elisabeth Ormandy, Janella C. Schwab, Samantha Suiter, Nicole Green, Janice Oakley, Pamela Osenkowski, Christine Sumner
Publikováno v:
The American Biology Teacher. 84:399-404
Animal dissection is practiced to varying degrees around the world and is particularly prevalent in North America throughout all levels of education. However, a growing number of studies suggest that non-animal teaching methods (NAMs) (e.g., virtual
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::da88dfe739c3190e00607f6dbd86ad29
https://doi.org/10.1525/abt.2022.84.7.399
https://doi.org/10.1525/abt.2022.84.7.399
Educators’ Views on the Use of Dissection and Dissection Alternatives in American Biology Classrooms
Publikováno v:
Alternatives to Laboratory Animals. 50:235-243
Animal dissection remains a common practice in American biology classrooms, despite the availability of dissection alternatives to study anatomy and physiology. Indeed, there is a growing body of evidence in the literature suggesting that the use of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7d44df8203cf9a67ed37d615663bb068
https://doi.org/10.1177/02611929221096578
https://doi.org/10.1177/02611929221096578
Publikováno v:
The American Biology Teacher. 83:498-503
When the COVID-19 pandemic struck in 2020, many schools made the decision to cancel face-to-face classes and move instruction online. To better understand how the pandemic affected science educators’ plans to conduct classroom animal dissection exe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::65a7b500349cfa077b4b2492960adf55
https://doi.org/10.1525/abt.2021.83.8.498
https://doi.org/10.1525/abt.2021.83.8.498
Autor:
Sherry L, Ward, Pamela, Osenkowski
Publikováno v:
Sherry L. Ward
Dogs are the experimental model in many types of biomedical research. Each year, hundreds of publications report the use of dogs in invasive biomedical procedures, often without sufficient explanation of the purpose and justification for selecting do
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d7240e010c88e413a0c276999b085aa
https://pubmed.ncbi.nlm.nih.gov/35502626
https://pubmed.ncbi.nlm.nih.gov/35502626
Autor:
Jing Zhang, Dennis J. Selkoe, Michael S. Wolfe, Wenjuan Ye, Han-Xun Wei, Dai Lu, Yongli Gu, Pamela Osenkowski, Corinne E. Augelli-Szafran, Vivien Sun
Publikováno v:
Bioorg Med Chem Lett
One therapeutic approach for Alzheimer's disease is to inhibit the cleavage of the amyloid precursor protein (APP) by γ-secretase. At the beginning of a series of studies from our laboratories, a series of novel γ-amino alcohols (1) were found to p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a7871e2efb9ec024eb8ebe67104c6219
https://doi.org/10.1016/j.bmcl.2016.03.042
https://doi.org/10.1016/j.bmcl.2016.03.042
Autor:
Corinne E. Augelli-Szafran, Michael S. Wolfe, Yongli Gu, Dennis J. Selkoe, Jing Zhang, Han-Xun Wei, Dai Lu, Wenjuan Ye, Pamela Osenkowski
Publikováno v:
Bioorg Med Chem Lett
γ-Secretase is one of two proteases directly involved in the production of the amyloid β-peptide, (Aβ) which is pathogenic in Alzheimer’s disease. Inhibition of γ-secretase to suppress the production of Aβ should not block processing of one of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4b031aeca784f22889539ebb4c372988
https://europepmc.org/articles/PMC8317589/
https://europepmc.org/articles/PMC8317589/
Publikováno v:
Journal of Biological Chemistry. 283:22529-22540
gamma-Secretase is an unusual and ubiquitous aspartyl protease with an intramembrane catalytic site that cleaves many type-I integral membrane proteins, most notably APP and Notch. Several reports suggest that cleavage of APP to produce the Abeta pep
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::86da22aad73c42765855d1b365378e0d
https://doi.org/10.1074/jbc.m801925200
https://doi.org/10.1074/jbc.m801925200
Autor:
Allen Saliganan, Pamela Osenkowski, Lucia Schuger, Seaho Kim, Amro Aboukameel, Marta Toth, Huiren Zhao, Rafael Fridman, Jin Ah Cho, Kristina Cole, R. Daniel Bonfil
Publikováno v:
Journal of Biological Chemistry. 283:17391-17405
Membrane type 1 (MT1) matrix metalloproteinase (MMP-14) is a membrane-tethered MMP considered to be a major mediator of pericellular proteolysis. MT1-MMP is regulated by a complex array of mechanisms, including processing and endocytosis that determi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d3eaad5b505a01c188d3bb9bf47270d8
https://doi.org/10.1074/jbc.m708943200
https://doi.org/10.1074/jbc.m708943200
Autor:
Pamela Osenkowski, Sreenivasa R. Chinni, Shahriar Mobashery, J. Carlos Trindade Filho, Sanaa Nabha, Hamilto Akihissa Yamamoto, R. Daniel Bonfil, Aaron Sabbota, Robert L. Vessella, Huiren Zhao, Michael L. Cher, Zhong Dong, Rafael Fridman
Publikováno v:
The American Journal of Pathology. 170:2100-2111
Membrane type 1-matrix metalloproteinase (MT1-MMP) is a major mediator of collagen I degradation. In human samples, we show that prostate cancer cells in skeletal metastases consistently express abundant MT1-MMP protein. Because prostate cancer bone
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4a1e457d76c5c06760bcd348c32a4015
https://doi.org/10.2353/ajpath.2007.060720
https://doi.org/10.2353/ajpath.2007.060720
Autor:
Marta Toth, Pamela Osenkowski, Stephen L. Brown, Rafael Fridman, Dusan Hesek, Samy O. Meroueh, Wael Sakr, Shahriar Mobashery
Publikováno v:
Biochemical Journal. 387:497-506
MT1-MMP (membrane type 1 matrix metalloproteinase) is a membrane-anchored MMP that can be shed to the extracellular milieu. In the present study we report the primary structure and activity of the major soluble form of MT1-MMP. MS analysis of the pur
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c45731eebd4fb82886b714c6c61240f4
https://doi.org/10.1042/bj20041324
https://doi.org/10.1042/bj20041324