Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Mohona Sarkar"'
Publikováno v:
Pediatric Critical Care Medicine. 22:103-104
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cfbda6353cfa13c780a20fde30d111e1
https://doi.org/10.1097/01.pcc.0000738968.40017.7c
https://doi.org/10.1097/01.pcc.0000738968.40017.7c
Autor:
Per Harald Jonson, Mridul Johari, Stuart H. Ralston, Sini Penttilä, YouJin Lee, Jaakko Sarparanta, Carolyn M. Sue, Conrad C. Weihl, Asim Azfer, Paul Maddison, David Hilton-Jones, Peter Hackman, Stephan Zierz, Patrick F. Chinnery, J. Paul Taylor, Bjarne Udd, Hans H. Goebel, Cornelia Kornblum, Mohona Sarkar, Anna Vihola, Robert C. Bucelli, Marco Savarese, Tiina Suominen, Jens Reimann, Anni Evilä, Johanna Palmio, Marie-Christine Minot, Torsten Kraya
Publikováno v:
The Journal of clinical investigation. 128(3)
Multisystem proteinopathy (MSP) involves disturbances of stress granule (SG) dynamics and autophagic protein degradation that underlie the pathogenesis of a spectrum of degenerative diseases that affect muscle, brain, and bone. Specifically, identica
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::81af572a16ac661fe0367cc4a2c94aca
https://pubmed.ncbi.nlm.nih.gov/29457785
https://pubmed.ncbi.nlm.nih.gov/29457785
Autor:
Mohona Sarkar, Gary J. Pielak
Publikováno v:
Protein Science. 23:1161-1164
Most theories predict that macromolecular crowding stabilizes globular proteins, but recent studies show that weak attractive interactions can result in crowding-induced destabilization. Osmolytes are ubiquitous in biology and help protect cells agai
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e1bf33934eb9bc08bf81744075934350
https://doi.org/10.1002/pro.2510
https://doi.org/10.1002/pro.2510
Publikováno v:
Protein Science. 22:1313-1319
Intrinsic rates of exchange are essential parameters for obtaining protein stabilities from amide 1H exchange data. To understand the influence of the intracellular environment on stability, one must know the effect of the cytoplasm on these rates. W
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::348872b49689d022440278c5b262b6af
https://doi.org/10.1002/pro.2318
https://doi.org/10.1002/pro.2318
Publikováno v:
Biophysical Reviews. 5:187-194
The intracellular milieu is complex, heterogeneous and crowded—an environment vastly different from dilute solutions in which most biophysical studies are performed. The crowded cytoplasm excludes about a third of the volume available to macromolec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d9a716a0d0549f03ebfbfd044cb047e9
https://doi.org/10.1007/s12551-013-0104-4
https://doi.org/10.1007/s12551-013-0104-4
Autor:
Hong Joo Kim, Junmin Peng, Regina-Maria Kolaitis, Diana M. Mitrea, Nam Chul Kim, Jaclyn A Cika, Jennifer Moore, Timothy I. Shaw, James Messing, Peipei Zhang, J. Paul Taylor, Maura Coughlin, Richard W. Kriwacki, Brian A. Maxwell, Jamshid Temirov, Bing Bai, Kyung-Ha Lee, Brian D. Freibaum, Amandine Molliex, Mohona Sarkar
Expansion of a hexanucleotide repeat GGGGCC (G4C2) in C9ORF72 is the most common cause of amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD). Transcripts carrying (G4C2) expansions undergo unconventional, non-ATG-dependent translat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4e2d2c40828e82773e97513484507e19
https://europepmc.org/articles/PMC5079111/
https://europepmc.org/articles/PMC5079111/
Publikováno v:
Journal of the American Chemical Society. 133:7116-7120
Thirty percent of a cell's volume is filled with macromolecules, and protein chemistry in a crowded environment is predicted to differ from that in dilute solution. We quantified the effect of crowding by globular proteins on the equilibrium thermody
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d3fb0d7e96e7ffecafeb28e2aa6db3be
https://doi.org/10.1021/ja200067p
https://doi.org/10.1021/ja200067p
Publikováno v:
The Journal of Physical Chemistry C. 113:6839-6844
Highly ordered 3D-hexagonal mesoporous silica HMS-3 has been synthesized under alkaline condition at 277 K using tetraethyl orthosilicate as the silica source and cetyltrimethylammonium bromide as the structure-directing agent. Powder X-ray diffracti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3e7d44d6522c632f203d001590af35cd
https://doi.org/10.1021/jp8114034
https://doi.org/10.1021/jp8114034
Autor:
Lorne Zinman, Carol F. Lippa, Ralph B. Perkerson, David Lacomis, Aishe Kurti, Billie J. Matchett, Cyril Pottier, J. Paul Taylor, Hong Joo Kim, Eileen H. Bigio, Heather Stewart, Zbigniew K. Wszolek, Leonard Petrucelli, M.-Marsel Mesulam, Elizabeth Finger, Kavya Annu, Ronald C. Petersen, Jamshid Temirov, Tanja Mittag, Charles Krieger, Rosa Rademakers, James Messing, Veronica Hirsch-Reinshagen, Ian R. A. Mackenzie, Sasha Zivkovic, Stephan Züchner, Alexandra M. Nicholson, Julia Keith, Ekaterina Rogaeva, Dennis W. Dickson, Neill R. Graff-Radford, Richard J. Caselli, Matt Baker, Melissa E. Murray, Kevin B. Boylan, Sandra Weintraub, Ging-Yuek Robin Hsiung, Masato Kato, Raymond P. Roos, John D. Fryer, Maria D. Purice, Mohona Sarkar
Publikováno v:
Neuron
Summary Amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD) are age-related neurodegenerative disorders with shared genetic etiologies and overlapping clinical and pathological features. Here we studied a novel ALS/FTD family and id
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b24545e056391b536f1d854718beeba0
https://doi.org/10.1016/j.neuron.2017.07.025
https://doi.org/10.1016/j.neuron.2017.07.025
Autor:
Lila M. Gierasch, Andres Binolfi, Peter B. Crowley, Francois Xavier Theillet, Anne Gershenson, Tamara Frembgen-Kesner, Gary J. Pielak, Adrian H. Elcock, Karan S. Hingorani, Philipp Selenko, Conggang Li, Mohona Sarkar, Ciara Kyne
Publikováno v:
Chemical Reviews
Chemical reviews, 114(13): 6661–6714
Chemical reviews, 114(13): 6661–6714
It has long been axiomatic that a protein’s structure determines its function. Intrinsically disordered proteins (IDPs) and disordered protein regions (IDRs) defy this structure–function paradigm. They do not exhibit stable secondary and/or terti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5bbdcaaf7f55f0577c1593d21b7b069e
http://hdl.handle.net/10379/14144
http://hdl.handle.net/10379/14144