Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Aaron, Moulin"'
Autor:
Cécile Capdevila, Christophe Loux, Catherine Lawrence, Jean-Piere Marquette, Magali Mathieu, Jacques Dumas, Paul Ferrari, Huawei Qiu, Bruno Dumas, Josiane Le Parc, Clark Pan, Ronnie Wei, Mark Levine, Russell Bigelow, Tim Edmunds, Aaron Moulin, Alexey Rak, Christine Hamel, Julie Bird
Publikováno v:
Protein Science. 23:1698-1707
Various important biological pathways are modulated by TGFβ isoforms; as such they are potential targets for therapeutic intervention. Fresolimumab, also known as GC1008, is a pan-TGFβ neutralizing antibody that has been tested clinically for sever
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::59d962602ccf8d97b943d8b22a97f36a
https://doi.org/10.1002/pro.2548
https://doi.org/10.1002/pro.2548
Autor:
Dagmar Ringe, Gregory A. Petsko, Aaron Moulin, Andrey Kovalevsky, S. Zoë Fisher, Louis M. Lazar, Paul Langan, Walter R. P. Novak
Publikováno v:
Acta Crystallographica Section F Structural Biology and Crystallization Communications. 67:587-590
The overarching goal of this research project is to determine, for a subset of proteins, exact hydrogen positions using neutron diffraction, thereby improving H-atom placement in proteins so that they may be better used in various computational metho
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fbd390948e597809b9a111b659f2eb4e
https://doi.org/10.1107/s1744309111009341
https://doi.org/10.1107/s1744309111009341
Autor:
Gregory A. Petsko, Mark A. Wilson, Dagmar Ringe, Zoë Fisher, Cheryl A. Kreinbring, Louis M. Lazar, Aaron Moulin, Michael Blakeley, Andrey Kovalevsky, Walter R. P. Novak
Publikováno v:
Acta Crystallographica Section A Foundations and Advances. 74:a30-a30
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::644a9fe5fe4deaa5cb0e165967f884d4
https://doi.org/10.1107/s0108767318099695
https://doi.org/10.1107/s0108767318099695
Autor:
Dagmar Ringe, Aaron Moulin, Katharine E. D’Aquino, Andrew R. Denninger, J. Alejandro D’Aquino
Publikováno v:
Journal of Molecular Biology. 390:112-123
The metal-ion-activated diphtheria toxin repressor (DtxR) is responsible for the regulation of virulence and other genes in Corynebacterium diphtheriae. A single point mutation in DtxR, DtxR(E175K), causes this mutant repressor to have a hyperactive
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::98ef61351d658dce943db69e9bd37dd1
https://doi.org/10.1016/j.jmb.2009.05.003
https://doi.org/10.1016/j.jmb.2009.05.003
Autor:
Aaron, Moulin, Magali, Mathieu, Catherine, Lawrence, Russell, Bigelow, Mark, Levine, Christine, Hamel, Jean-Piere, Marquette, Josiane, Le Parc, Christophe, Loux, Paul, Ferrari, Cecile, Capdevila, Jacques, Dumas, Bruno, Dumas, Alexey, Rak, Julie, Bird, Huawei, Qiu, Clark Q, Pan, Tim, Edmunds, Ronnie R, Wei
Publikováno v:
Protein science : a publication of the Protein Society. 23(12)
Various important biological pathways are modulated by TGFβ isoforms; as such they are potential targets for therapeutic intervention. Fresolimumab, also known as GC1008, is a pan-TGFβ neutralizing antibody that has been tested clinically for sever
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::6a6fb54f6d50902c599a15854fab52c3
https://pubmed.ncbi.nlm.nih.gov/25209176
https://pubmed.ncbi.nlm.nih.gov/25209176
Autor:
Alexandra Kaganovich, John DeSilva, Margarita Kamenetsky, Pak P. Poon, Gerald C. Johnston, Hong Sun, Bradford Maynes, Ludmilla Berenfeld, Jennifer L. Collins, Irina Ratskovskaya, Jennifer Heymont, JoAnne Engebrecht, Aaron Moulin, Gregory A. Petsko
Publikováno v:
Proceedings of the National Academy of Sciences. 97:12672-12677
PTEN/MMAC1/TEP1 (PTEN, phosphatase deleted on chromosome ten; MMAC1, mutated in multiple advanced cancers; TEP1, tensin-like phosphatase) is a major human tumor suppressor gene whose suppressive activity operates on the phosphatidylinositol pathway.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5b4a99a6d2f12d84549f5eb03a7c3c85
https://doi.org/10.1073/pnas.97.23.12672
https://doi.org/10.1073/pnas.97.23.12672
Malonate: a versatile cryoprotectant and stabilizing solution for salt-grown macromolecular crystals
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 59:2356-2358
Collection of quality data on high-energy synchrotron sources requires the selection of a cryoprotectant that allows protein crystals to be cryocooled without damage to the crystal and with suppression of ice formation. The use of sodium malonate as
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::107aee65efa29eaad92bfd63c3445e1e
https://doi.org/10.1107/s0907444903021784
https://doi.org/10.1107/s0907444903021784
The study of enzymes has regularly been informed by the discovery of new inhibitors. With respect to insight into events at the active site of enzymes, related to catalysis, the most informative inhibitors have generally been substrate or product ana
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f4c4089c3427d29a1a4d59db522deb5d
https://europepmc.org/articles/PMC2512255/
https://europepmc.org/articles/PMC2512255/
Autor:
Aaron Moulin, Carin C. Stamper, Petra Munih, Gregory A. Petsko, Dagmar Ringe, Richard C. Holz, Brian Bennett
Publikováno v:
Journal of inorganic biochemistry. 101(8)
The X-ray crystal structure of the Co(II)-loaded form of the aminopeptidase from Aeromonas proteolytica ([CoCo(AAP)]) was solved to 2.2A resolution. [CoCo(AAP)] folds into an alpha/beta globular domain with a twisted beta-sheet hydrophobic core sandw
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ebc460cddb6d6a9d984b3e8a48484427
https://pubmed.ncbi.nlm.nih.gov/17574677
https://pubmed.ncbi.nlm.nih.gov/17574677
Autor:
Dagmar Ringe, Gregory A. Petsko, Richard C. Holz, Aaron Moulin, Brian Bennett, Krzysztof P. Bzymek, Sabina I. Swierczek
Publikováno v:
Biochemistry. 44(36)
Glutamate151 (E151) has been shown to be catalytically essential for the aminopeptidase from Vibrio proteolyticus (AAP). E151 acts as the general acid/base during the catalytic mechanism of peptide hydrolysis. However, a glutamate residue is not the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5144304973650cd83884e5a4828b59bb
https://pubmed.ncbi.nlm.nih.gov/16142900
https://pubmed.ncbi.nlm.nih.gov/16142900