Zobrazeno 1 - 10
of 250
pro vyhledávání: '"John R. Engen"'
Autor:
Anne‐Lise Marie, Florian Georgescauld, Kendall R. Johnson, Somak Ray, John R. Engen, Alexander R. Ivanov
Publikováno v:
Advanced Science, Vol 11, Iss 11, Pp n/a-n/a (2024)
Abstract Protein complexes are essential for proteins' folding and biological function. Currently, native analysis of large multimeric protein complexes remains challenging. Structural biology techniques are time‐consuming and often cannot monitor
Externí odkaz:
https://doaj.org/article/64b628a454f04f858ff2c3bef4508bbf
Autor:
Pelin Ayaz, Agatha Lyczek, YiTing Paung, Victoria R. Mingione, Roxana E. Iacob, Parker W. de Waal, John R. Engen, Markus A. Seeliger, Yibing Shan, David E. Shaw
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-15 (2023)
Atomic-level descriptions of protein–small molecule binding processes that involve a large conformational change of the protein have been elusive. Here, the authors report unguided molecular dynamics simulations of such a process—Abl kinase bindi
Externí odkaz:
https://doaj.org/article/e9aae3578aa946d8ba5c8a7f929b7cf9
Autor:
Michelle S. Prew, Christina M. Camara, Thomas Botzanowski, Jamie A. Moroco, Noah B. Bloch, Hannah R. Levy, Hyuk-Soo Seo, Sirano Dhe-Paganon, Gregory H. Bird, Henry D. Herce, Micah A. Gygi, Silvia Escudero, Thomas E. Wales, John R. Engen, Loren D. Walensky
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-12 (2022)
Prew et al. uncovered a structural basis for human VLCAD deficiency that arises from point mutations within the enzyme’s membrane-binding region, which was shown to fold as a putative α-helical hairpin. Helix-breaking mutations selectively disrupt
Externí odkaz:
https://doaj.org/article/e862c131a10741b096477d28809d47d0
Autor:
Ka Ying Sharon Hung, Sven Klumpe, Markus R. Eisele, Suzanne Elsasser, Geng Tian, Shuangwu Sun, Jamie A. Moroco, Tat Cheung Cheng, Tapan Joshi, Timo Seibel, Duco Van Dalen, Xin-Hua Feng, Ying Lu, Huib Ovaa, John R. Engen, Byung-Hoon Lee, Till Rudack, Eri Sakata, Daniel Finley
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-13 (2022)
The interplay of the proteasome and deubiquitinase Ubp6 is crucial for the degradation of ubiquitylated substrates. Here, the authors provide structural insights into the allosteric mechanism by which the activities of both Ubp6 and the proteasome ar
Externí odkaz:
https://doaj.org/article/0db17aeb4b8c4a309992d0d564111f7b
Autor:
Noah B. Bloch, Thomas E. Wales, Michelle S. Prew, Hannah R. Levy, John R. Engen, Loren D. Walensky
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
The pro-apoptotic BAX protein is a monomer under homeostatic conditions and, in response to stress, transforms into oligomers that induce apoptosis. Here, the authors characterize structural features of BAX that individually stabilize the monomer whi
Externí odkaz:
https://doaj.org/article/6094840e65e043afbdbb1d1b24daacd6
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-13 (2019)
The activation mechanism of integrin αVβ8 differs from other integrins. Combining X-ray crystallography, hydrogen deuterium exchange mass spectrometry and mutation, the authors reveal structural features responsible for these differences and provid
Externí odkaz:
https://doaj.org/article/43de20468235470690fca07f6b07b53e
Publikováno v:
Cell Reports, Vol 30, Iss 10, Pp 3229-3239.e6 (2020)
Summary: BCL-2 family proteins converge at the mitochondrial outer membrane to regulate apoptosis and maintain the critical balance between cellular life and death. This physiologic process is essential to organism homeostasis and relies on protein-p
Externí odkaz:
https://doaj.org/article/d674418a0a83428c96204962babe54c6
Autor:
Nina Kerres, Steffen Steurer, Stefanie Schlager, Gerd Bader, Helmut Berger, Maureen Caligiuri, Christian Dank, John R. Engen, Peter Ettmayer, Bernhard Fischerauer, Gerlinde Flotzinger, Daniel Gerlach, Thomas Gerstberger, Teresa Gmaschitz, Peter Greb, Bingsong Han, Elizabeth Heyes, Roxana E. Iacob, Dirk Kessler, Heike Kölle, Lyne Lamarre, David R. Lancia, Simon Lucas, Moriz Mayer, Katharina Mayr, Nikolai Mischerikow, Katja Mück, Christoph Peinsipp, Oliver Petermann, Ulrich Reiser, Dorothea Rudolph, Klaus Rumpel, Carina Salomon, Dirk Scharn, Renate Schnitzer, Andreas Schrenk, Norbert Schweifer, Diane Thompson, Elisabeth Traxler, Roland Varecka, Tilman Voss, Alexander Weiss-Puxbaum, Sandra Winkler, Xiaozhang Zheng, Andreas Zoephel, Norbert Kraut, Darryl McConnell, Mark Pearson, Manfred Koegl
Publikováno v:
Cell Reports, Vol 20, Iss 12, Pp 2860-2875 (2017)
The transcription factor BCL6 is a known driver of oncogenesis in lymphoid malignancies, including diffuse large B cell lymphoma (DLBCL). Disruption of its interaction with transcriptional repressors interferes with the oncogenic effects of BCL6. We
Externí odkaz:
https://doaj.org/article/43ac770ae3294c078849cf3143253f8a
Autor:
Klaus Bonazza, Roxana E Iacob, Nathan E Hudson, Jing Li, Chafen Lu, John R Engen, Timothy A Springer
Publikováno v:
eLife, Vol 11 (2022)
Hemostasis in the arterial circulation is mediated by binding of the A1 domain of the ultralong protein von Willebrand factor (VWF) to GPIbα on platelets to form a platelet plug. A1 is activated by tensile force on VWF concatemers imparted by hydrod
Externí odkaz:
https://doaj.org/article/b17ab643965e4aac956079f5db2b0c9f
Publikováno v:
eLife, Vol 9 (2020)
Bruton’s tyrosine kinase (BTK) is targeted in the treatment of B-cell disorders including leukemias and lymphomas. Currently approved BTK inhibitors, including Ibrutinib, a first-in-class covalent inhibitor of BTK, bind directly to the kinase activ
Externí odkaz:
https://doaj.org/article/a1e7c59bd7424b1ea7e5693fd82af544