Zobrazeno 1 - 10
of 27
pro vyhledávání: '"Ismail Moarefi"'
Autor:
Ismail, Moarefi
Publikováno v:
Advances in experimental medicine and biology. 896
Small molecule drug discovery critically depends on the availability of meaningful in vitro assays to guide medicinal chemistry programs that are aimed at optimizing drug potency and selectivity. As it becomes increasingly evident, most disease relev
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::a4129db21a2e54adc74b26eb85016cfc
https://pubmed.ncbi.nlm.nih.gov/27165315
https://pubmed.ncbi.nlm.nih.gov/27165315
Autor:
Ismail Moarefi
Publikováno v:
Advanced Technologies for Protein Complex Production and Characterization ISBN: 9783319272146
Small molecule drug discovery critically depends on the availability of meaningful in vitro assays to guide medicinal chemistry programs that are aimed at optimizing drug potency and selectivity. As it becomes increasingly evident, most disease relev
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d509831fd035d4b27758c729b1912b76
https://doi.org/10.1007/978-3-319-27216-0_1
https://doi.org/10.1007/978-3-319-27216-0_1
Autor:
Katrin Meissl, Gabriele Maurer, Florian Kern, Ismail Moarefi, Izabela Sobczak, Daniela Piazzolla, Oliviero Carugo, Karin Ehrenreiter, Matthias Hamerl, Tony Ng, Thomas Leung, Manuela Baccarini, Gregory Weitsman, Theodora Niault
Publikováno v:
The Journal of Cell Biology
The mechanism by which Raf-1 antagonizes Rok-α to promote migration and tumorigenesis is revealed.
The activity of Raf-1 and Rok-α kinases is regulated by intramolecular binding of the regulatory region to the kinase domain. Autoinhibition is
The activity of Raf-1 and Rok-α kinases is regulated by intramolecular binding of the regulatory region to the kinase domain. Autoinhibition is
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::89a46358fbb3b387fb224f8cbdf96000
http://europepmc.org/articles/PMC2779248
http://europepmc.org/articles/PMC2779248
Autor:
Stephan M. Feller, EYvonne Jones, Ismail Moarefi, Robert J.C. Gilbert, Roland P. Bourette, Guy Mouchiroud, Maria Harkiolaki, Marc Lewitzky, Holger Sondermann
Publikováno v:
The EMBO Journal. 22:2571-2582
SH3 domains are protein recognition modules within many adaptors and enzymes. With more than 500 SH3 domains in the human genome, binding selectivity is a key issue in understanding the molecular basis of SH3 domain interactions. The Grb2-like adapto
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f9b7affb014754d9f17e31e1f432a605
https://doi.org/10.1093/emboj/cdg258
https://doi.org/10.1093/emboj/cdg258
Autor:
Konstanze F. Winklhofer, Anja Reintjes, Ulrich Heller, Ismail Moarefi, Johanna Heske, Walter Muranyi, Jörg Tatzelt
Publikováno v:
Journal of Biological Chemistry. 278:14961-14970
Misfolding of the mammalian prion protein (PrP) is implicated in the pathogenesis of prion diseases. We analyzed wild type PrP in comparison with different PrP mutants and identified determinants of the in vivo folding pathway of PrP. The complete N
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1f349b61b0795207408c15472f2830ea
https://doi.org/10.1074/jbc.m209942200
https://doi.org/10.1074/jbc.m209942200
Autor:
Achim Brinker, Günther Jung, Clemens Scheufler, Burkhard Fleckenstein, Christian Herrmann, Ismail Moarefi, Florian von der Mülbe, F. Ulrich Hartl
Publikováno v:
Journal of Biological Chemistry. 277:19265-19275
Protein-protein interaction modules containing so-called tetratricopeptide repeats (TPRs) mediate the assembly of Hsp70/Hsp90 multi-chaperone complexes. The TPR1 and TPR2A domains of the Hsp70/Hsp90 adapter protein p60/Hop specifically bind to short
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::001444b54d27efbf4d2fc9dce905beb1
https://doi.org/10.1074/jbc.m109002200
https://doi.org/10.1074/jbc.m109002200
Publikováno v:
Journal of Cell Biology. 154:267-274
Hsp90 is unique among molecular chaperones. The majority of its known substrates are signal transduction proteins, and recent work indicates that it uses a novel protein-folding strategy.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1479ae3212e9a3fbaac42a4e6579c32b
https://doi.org/10.1083/jcb.200104079
https://doi.org/10.1083/jcb.200104079
Autor:
Ismail Moarefi, Clemens Scheufler, Jörg Höhfeld, F. Ulrich Hartl, Holger Sondermann, Christine Schneider
Publikováno v:
Science. 291:1553-1557
Bag (Bcl2-associated athanogene) domains occur in a class of cofactors of the eukaryotic chaperone 70-kilodalton heat shock protein (Hsp70) family. Binding of the Bag domain to the Hsp70 adenosine triphosphatase (ATPase) domain promotes adenosine 5
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5fa8836ee3bc0cd167d4d34b311eab00
https://doi.org/10.1126/science.1057268
https://doi.org/10.1126/science.1057268
Publikováno v:
Cell. 103(4):621-632
Prefoldin (GimC) is a hexameric molecular chaperone complex built from two related classes of subunits and present in all eukaryotes and archaea. Prefoldin interacts with nascent polypeptide chains and, in vitro, can functionally substitute for the H
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::644c7d8680eecf203d4e761cbaacf895
Autor:
Ismail Moarefi, F. Ulrich Hartl, Gleb Bourenkov, Clemens Scheufler, Luis Moroder, Achim Brinker, Hans D. Bartunik, Stefano Pegoraro
Publikováno v:
Cell. 101:199-210
The adaptor protein Hop mediates the association of the molecular chaperones Hsp70 and Hsp90. The TPR1 domain of Hop specifically recognizes the C-terminal heptapeptide of Hsp70 while the TPR2A domain binds the C-terminal pentapeptide of Hsp90. Both
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a116d825cd92f6cc7ce0832ba502d966
https://doi.org/10.1016/s0092-8674(00)80830-2
https://doi.org/10.1016/s0092-8674(00)80830-2