Zobrazeno 1 - 10
of 23
pro vyhledávání: '"Srisathiyanarayanan Dharmaiah"'
Autor:
Fa-An Chao, Albert H. Chan, Srisathiyanarayanan Dharmaiah, Charles D. Schwieters, Timothy H. Tran, Troy Taylor, Nitya Ramakrishnan, Dominic Esposito, Dwight V. Nissley, Frank McCormick, Dhirendra K. Simanshu, Gabriel Cornilescu
Publikováno v:
Communications Biology, Vol 6, Iss 1, Pp 1-12 (2023)
Abstract Localized dynamics of RAS, including regions distal to the nucleotide-binding site, is of high interest for elucidating the mechanisms by which RAS proteins interact with effectors and regulators and for designing inhibitors. Among several o
Externí odkaz:
https://doaj.org/article/69321b8535d54b5689b2d175700764dc
Autor:
Timothy H. Tran, Albert H. Chan, Lucy C. Young, Lakshman Bindu, Chris Neale, Simon Messing, Srisathiyanarayanan Dharmaiah, Troy Taylor, John-Paul Denson, Dominic Esposito, Dwight V. Nissley, Andrew G. Stephen, Frank McCormick, Dhirendra K. Simanshu
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-16 (2021)
The molecular details of the RAS-RAF interaction are still not fully understood. Here, the authors present crystal structures of wild-type and mutant KRAS in complex with the RAS-binding and membrane-interacting cysteine-rich domains of RAF1, and pro
Externí odkaz:
https://doaj.org/article/8075c5993bfb4f61bc8bb5d453321337
Autor:
Fa-An Chao, Srisathiyanarayanan Dharmaiah, Troy Taylor, Simon Messing, William Gillette, Dominic Esposito, Dwight V. Nissley, Frank McCormick, R. Andrew Byrd, Dhirendra K. Simanshu, Gabriel Cornilescu
Publikováno v:
Journal of the American Chemical Society. 144:4196-4205
KRAS is the most frequently mutated RAS protein in cancer patients, and it is estimated that about 20% of the cancer patients in the United States carried mutant RAS proteins. To accelerate therapeutic development, structures and dynamics of RAS prot
Autor:
Dominic Esposito, Dhirendra K. Simanshu, Simon Messing, Anatoly Urisman, Matthew J. Sale, Frank McCormick, Pau Castel, Gabrielle Rizzuto, Alice Cheng, Michael J. Trnka, Antonio Cuevas-Navarro, Srisathiyanarayanan Dharmaiah
Publikováno v:
Proc Natl Acad Sci U S A
Proceedings of the National Academy of Sciences of the United States of America, vol 118, iss 33
Proceedings of the National Academy of Sciences of the United States of America, vol 118, iss 33
RAS proteins are molecular switches that interact with effector proteins when bound to guanosine triphosphate, stimulating downstream signaling in response to multiple stimuli. Although several canonical downstream effectors have been extensively stu
Autor:
Rendong Yang, Dwight V. Nissley, Troy Taylor, Getiria Onsongo, Ting-You Wang, Megan Rigby, Anne E. Sarver, Emil Lou, Srisathiyanarayanan Dharmaiah, Subbaya Subramanian, Dhirendra K. Simanshu, John Columbus, Robert M. Stephens, Andrew C. Nelson, Drew Sciacca, Thomas J. Turbyville
Publikováno v:
J Biol Chem
The oncogene RAS is one of the most widely studied proteins in cancer biology, and mutant active RAS is a driver in many types of solid tumors and hematological malignancies. Yet the biological effects of different RAS mutations and the tissue-specif
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8b0b6081537e879b415dc450509538ed
https://europepmc.org/articles/PMC7363148/
https://europepmc.org/articles/PMC7363148/
Autor:
Patrick Alexander, Dominic Esposito, Andrew G. Stephen, Dwight V. Nissley, Frank McCormick, Trent E. Balius, Timothy H. Tran, Srisathiyanarayanan Dharmaiah, Dhirendra K. Simanshu, Constance Agamasu
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
In Kessler et al. (1), the small molecule BI-2852 is shown to bind—at nanomolar affinity—to KRAS between switch I and II, inhibiting interactions with effectors. Here, we identify an alternative explanation for the inhibitory activity. While inve
Autor:
Dana Rabara, Dhirendra K. Simanshu, Robert M. Stephens, Timothy H. Tran, Srisathiyanarayanan Dharmaiah, Frank McCormick, Matthew Holderfield
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America, vol 116, iss 44
KRAS mutations occur in ∼35% of colorectal cancers and promote tumor growth by constitutively activating the mitogen-activated protein kinase (MAPK) pathway. KRAS mutations at codons 12, 13, or 61 are thought to prevent GAP protein-stimulated GTP h
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8ec02e93f0d96648d67a46767cf4d8eb
https://europepmc.org/articles/PMC6825300/
https://europepmc.org/articles/PMC6825300/
Autor:
Megan Rigby, Emil Lou, Andrew C. Nelson, Drew Sciacca, Thomas J. Turbyville, Subbaya Subramanian, Anne E. Sarver, Srisathiyanarayanan Dharmaiah, Dwight V. Nissley, Getiria Onsongo, Rendong Yang, John Columbus, Robert M. Stephens, Dhirendra K. Simanshu
Molecular testing of oncogenicRASmutations in colorectal cancer (CRC) have led to increased identification of mutations in patients with CRC.NRAS-mutated CRC has not been well characterized because it is less common (KRASmutations. Here, we report a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::18fa9570df402c2f58208fa128cacb4b
Autor:
Dwight V. Nissley, Dhirendra K. Simanshu, Frank McCormick, Matthew Drew, Wupeng Yan, Anatoly Urisman, Evan Markegard, Dominic Esposito, Srisathiyanarayanan Dharmaiah, Klaus Scheffzek
Publikováno v:
Cell reports, vol 32, iss 3
Cell reports
Cell reports
SUMMARY Sprouty-related, EVH1 domain-containing (SPRED) proteins negatively regulate RAS/mitogen-activated protein kinase (MAPK) signaling following growth factor stimulation. This inhibition of RAS is thought to occur primarily through SPRED1 bindin
Autor:
Timothy H. Tran, Srisathiyanarayanan Dharmaiah, Dhirendra K. Simanshu, Dwight V. Nissley, Albert H. Chan
Publikováno v:
Molecular Cancer Research. 18:PR01-PR01
The RAS family proteins alternate between active GTP-bound and inactive GDP-bound states. Due to the high affinity of GDP and GTP, and low intrinsic GTPase activity of RAS, switching between the two states is assisted by guanine nucleotide exchange f