Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Mentor Mulaj"'
Autor:
Romany Abskharon, Johnny Dang, Ameer Elfarash, Zerui Wang, Pingping Shen, Lewis S. Zou, Sedky Hassan, Fei Wang, Hisashi Fujioka, Jan Steyaert, Mentor Mulaj, Witold K. Surewicz, Joaquín Castilla, Alexandre Wohlkonig, Wen-Quan Zou
Publikováno v:
Microbial Cell Factories, Vol 16, Iss 1, Pp 1-11 (2017)
Abstract Background The infectious prion protein (PrPSc or prion) is derived from its cellular form (PrPC) through a conformational transition in animal and human prion diseases. Studies have shown that the interspecies conversion of PrPC to PrPSc is
Externí odkaz:
https://doaj.org/article/b627b0d2329d44528d6e772788104f61
Autor:
Martin Muschol, Lixin Wan, Shengchen Lin, Shuang Lu, Tyler Keeley, Shengyu Yang, Mentor Mulaj, Bin Fang, Jihui Hao, Jianwei Sun
Publikováno v:
Journal of Biological Chemistry. 291:27323-27333
Fascin is an actin bundling protein that cross-links individual actin filaments into straight, compact, and stiff bundles, which are crucial for the formation of filopodia, stereocillia, and other finger-like membrane protrusions. The dysregulation o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::20b162933401afcd041f854d216189b6
https://doi.org/10.1074/jbc.m116.767640
https://doi.org/10.1074/jbc.m116.767640
Publikováno v:
Biomacromolecules
Self-assembly of proteins into amyloid fibrils plays a key role in a multitude of human disorders that range from Alzheimer's disease to type II diabetes. Compact oligomeric species, observed early during amyloid formation, are reported as the molecu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::adbd44709272e4af91b6206a00e5bd8a
http://europepmc.org/articles/PMC4294590
http://europepmc.org/articles/PMC4294590
Autor:
Alexandre Wohlkonig, Lewis S. Zou, Johnny Dang, Hisashi Fujioka, Jan Steyaert, Romany Abskharon, Joaquín Castilla, Wen-Quan Zou, Sedky H.A. Hassan, Pingping Shen, Mentor Mulaj, Zerui Wang, Ameer Elfarash, Fei Wang, Witold K. Surewicz
Publikováno v:
Microbial Cell Factories, Vol 16, Iss 1, Pp 1-11 (2017)
Microbial Cell Factories
Microbial Cell Factories
BACKGROUND: The infectious prion protein (PrP(Sc) or prion) is derived from its cellular form (PrP(C)) through a conformational transition in animal and human prion diseases. Studies have shown that the interspecies conversion of PrP(C) to PrP(Sc) is
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8893c2052bdee2def51af5ee3d1b4487
https://doi.org/10.1186/s12934-017-0782-x
https://doi.org/10.1186/s12934-017-0782-x
Publikováno v:
Biophysical Journal. 108(2)
Deposition of protein plaques, rich in long rigid fibrils with a characteristic cross-beta sheet structure, is the pathological marker for human disorders ranging from Alzheimer's disease to type II diabetes and rheumatoid arthritis. Significant evid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8ed78034a4b4d642cefa518d6e5591ad
Autor:
Tyler Keeley, Mentor Mulaj, Lixin Wan, Shengchen Lin, Jianwei Sun, Martin Muschol, Shengyu Yang, Jihui Hao, Bin Fang, Shuang Lu
Publikováno v:
Cancer Research. 77:5333-5333
Fascin is the most frequently upregulated actin regulatory protein in metastatic tumors. The elevated expression levels of fascin universally correlate with poor clinical course and shorter survival across different cancer types. It is believed that
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4af7c0ea3667b63bdb9621333537a335
https://doi.org/10.1158/1538-7445.am2017-5333
https://doi.org/10.1158/1538-7445.am2017-5333
Amyloid fibril formation of lysozyme in vitro will proceed along two distinctly different assembly pathways under different solution conditions. We describe the use of atomic force microscopy (AFM) and dynamic light scattering (DLS) in characterizing
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::229de009ac1a371755c268f70cd88384
https://doi.org/10.1016/b978-0-12-394431-3.00035-3
https://doi.org/10.1016/b978-0-12-394431-3.00035-3
Autor:
Marie-Isabel Aguilar, Maria Andreasen, Neil R. Anthony, Fernando Teran Arce, Florian Arnhold, Shruti Arya, Aida Attar, Silvia Barbosa, Manja A. Behrens, Innocent B. Bekard, Georges Belfort, Martin L. Bennink, Magdalena Bereza, Keith M. Berland, Gal Bitan, Mischa Bonn, Hugo M. Botelho, Joana Branco dos Santos, Leonid Breydo, Yi Cao, Roberto Cappai, Isabel Cardoso, Mariano Carrión-Vázquez, Sofia B. Carvalho, John A. Carver, Fiona T.S. Chan, W. Seth Childers, Jason C. Collins, Laura Connelly, Cyril Curtain, Vijit Dalal, Alfonso De Simone, Athene M. Donald, Dave E. Dunstan, Heath Ecroyd, Jan Johannes Enghild, Laura Esther Abelleira, Marcus Fändrich, María del Carmen Fernández-Ramírez, Vito Foderà, Günter Fritz, Yoshiaki Furukawa, Shirin D. Ghodke, Stefano Gianni, Armin Giese, Cláudio M. Gomes, Susana Gonçalves, Lesley H. Greene, Michael D.W. Griffin, Amy M. Griggs, Christian Haass, Per Hammarström, J. Robin Harris, Federico Herrera, Rubén Hervás, Shannon E. Hill, Xu Hou, Geoffrey J. Howlett, Tsuneya Ikezu, Hyunbum Jang, Grethe V. Jensen, Bruce L. Kagan, Clemens F. Kaminski, Shigeko Kawai-Noma, Alexei Klechikov, Gijsje H. Koenderink, Ratnesh Lal, Douglas V. Laurents, Chi Le Lan Pham, Harry LeVine, Dusan Losic, David G. Lynn, Kirsten G. Malmos, Lisandra L. Martin, Adam I. Mechler, Anil K. Mehta, Derya Meral, Nathaniel G.N. Milton, Yee-Foong Mok, Ludmilla A. Morozova-Roche, Víctor Mosquera, Samrat Mukhopadhyay, Mentor Mulaj, Martin Muschol, Niels Chr Nielsen, R. Nilsson, Georg Nübling, Ruth Nussinov, Daniel E. Otzen, Tiago Fleming Outeiro, Jan Skov Pedersen, Jesper Søndergaard Pedersen, K. Peter, Dorothea Pinotsi, Meng Qin, Srinivasan Ramachandran, Agata Rekas, Annalisa Relini, Jean-Christophe Rochet, Sophie Rothhämel, Nikita Rudinskiy, Markus Sauer, Gabriele S. Kaminski Schierle, Michael Schleeger, Bettina Schmid, David H. Small, Anne Søndergaard, Mirco Sorci, Tara L. Spires-Jones, Marcel Stenvang, Martin Stöckl, Katrin Strecker, Vinod Subramaniam, Anna S.P. Svane, Kim K.M. Sweers, Pablo Taboada, Hideki Taguchi, Chai Lean Teoh, David C. Thorn, Kiyotaka Tokuraku, Robert Tycko, Brigita Urbanc, Vladimir N. Uversky, Corianne C. van den Akker, Michele Vendruscolo, Anna von Mikecz, Vladana Vukojević, Wei Wang, Katrin Weise, Roland Winter, Jessica W. Wu, Wei-Feng Xue, Kiran Yanamandra, Daniel Ysselstein, Eva Žerovnik, Dawei Zou
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3c175a1f0ef43b7e6a7630800263015e
https://doi.org/10.1016/b978-0-12-394431-3.01002-6
https://doi.org/10.1016/b978-0-12-394431-3.01002-6
Autor:
Christopher Persichilli, Mentor Mulaj, Shannon E. Hill, Marissa Ciesla, Joseph Foley, Sandy D. Westerheide, Rhonda Robeel, Martin Muschol, Rachel Raynes, Tatiana Miti
Publikováno v:
The Journal of chemical physics. 139(12)
Deposits of fibrils formed by disease-specific proteins are the molecular hallmark of such diverse human disorders as Alzheimer's disease, type II diabetes, or rheumatoid arthritis. Amyloid fibril formation by structurally and functionally unrelated
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::46757ae4995325d01ba3e7699ee0142b
https://pubmed.ncbi.nlm.nih.gov/24089713
https://pubmed.ncbi.nlm.nih.gov/24089713
Publikováno v:
Intrinsically Disordered Proteins. 3:e1056905
Self-assembly of proteins and peptides into amyloid fibrils involves multiple distinct intermediates and late-stage fibrillar polymorphs. Understanding the conditions and mechanisms that promote the formation of one type of intermediate and polymorph
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2cd3905f3efa8ee04bace569df00df65
https://doi.org/10.1080/21690707.2015.1056905
https://doi.org/10.1080/21690707.2015.1056905