Zobrazeno 1 - 10
of 23
pro vyhledávání: '"Natalia Kozlyuk"'
Autor:
Lauren E. Boucher, Elisabeth Geyer Prinslow, Michael Feldkamp, Fang Yi, Rupesh Nanjunda, Sheng-Jiun Wu, Tun Liu, Eilyn R. Lacy, Steven Jacobs, Natalia Kozlyuk, Brian Del Rosario, Bingyuan Wu, Patricia Aquino, Robert C. Davidson, Samantha Heyne, Nicholas Mazzanti, James Testa, Michael D. Diem, Elsa Gorre, Andrew Mahan, Hirsh Nanda, Harsha P. Gunawardena, Alexis Gervais, Anthony A. Armstrong, Alexey Teplyakov, Chichi Huang, Adam Zwolak, Partha Chowdhury, Wan Cheung Cheung, Jinquan Luo
Publikováno v:
mAbs, Vol 15, Iss 1 (2023)
ABSTRACTSingle-chain fragment variable (scFv) domains play an important role in antibody-based therapeutic modalities, such as bispecifics, multispecifics and chimeric antigen receptor T cells or natural killer cells. However, scFv domains exhibit lo
Externí odkaz:
https://doaj.org/article/07a49e5767d741f0bc24b50e3af689e1
Autor:
Marc A. Sprague-Piercy, Jan C. Bierma, Marquise G. Crosby, Brooke P. Carpenter, Gemma R. Takahashi, Joana Paulino, Ivan Hung, Rongfu Zhang, John E. Kelly, Natalia Kozlyuk, Xi Chen, Carter T. Butts, Rachel W. Martin
Publikováno v:
Biomolecules, Vol 10, Iss 7, p 1069 (2020)
The Droserasins, aspartic proteases from the carnivorous plant Drosera capensis, contain a 100-residue plant-specific insert (PSI) that is post-translationally cleaved and independently acts as an antimicrobial peptide. PSIs are of interest not only
Externí odkaz:
https://doaj.org/article/d419775b49f347c798e29e796c725175
Autor:
Walter J. Chazin, Alex G. Waterson, Rocco D. Gogliotti, Natalia Kozlyuk, Plamen P. Christov, Benjamin A. Gilston, Lauren E. Salay, Mohiuddin Ovee, Kwangho Kim
Publikováno v:
Proteins
The Receptor for Advanced Glycation End products (RAGE) is a pattern recognition receptor that signals for inflammation via the NF-κB pathway. RAGE has been pursued as a potential target to suppress symptoms of diabetes and is of interest in a numbe
Autor:
Lauren E. Salay, Plamen P. Christov, Rocco D. Gogliotti, Natalia Kozlyuk, Alex Gregory Waterson, Kwangho Kim, Walter J. Chazin, Benjamin A. Gilston, Mohiuddin Ovee
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0b1c11c84a9b732be46d615fa4e445ad
https://doi.org/10.1002/prot.26162/v2/response1
https://doi.org/10.1002/prot.26162/v2/response1
Publikováno v:
Biochemistry. 58:4505-4518
The βγ-crystallin superfamily contains both β- and γ-crystallins of the vertebrate eye lens and the microbial calcium-binding proteins, all of which are characterized by a common double-Greek key domain structure. The vertebrate βγ-crystallins
Publikováno v:
Biophysical Journal. 121:453a
Publikováno v:
Biochemistry, vol 55, iss 50
The tunicate (Ciona intestinalis) βγ-crystallin represents an intermediate case between the calcium-binding proteins ancestral to the vertebrate βγ-crystallin fold and the vertebrate structural crystallins. Unlike the structural βγ-crystallins
Publikováno v:
Biochemistry
The βγ-crystallin superfamily contains both the β- and γ-crystallins of the vertebrate eye lens and the microbial calcium-binding proteins, all of which are characterized by a common double-Greek key domain structure. The vertebrate βγ-crystall
Autor:
Andrew J. Monteith, Natalia Kozlyuk, Eric P. Skaar, Velia Garcia, Walter J. Chazin, Steven M. Damo
Publikováno v:
Methods in Molecular Biology ISBN: 9781493990290
S100 proteins are distinct dimeric EF-hand Ca(2+)-binding proteins that can bind Zn(2+), Mn(2+), and other transition metals with high affinity at two sites in the dimer interface. Certain S100 proteins, including S100A7, S100A12, S100A8, and S100A9,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::71afffefaca5591a7e208dd3d501788e
https://doi.org/10.1007/978-1-4939-9030-6_18
https://doi.org/10.1007/978-1-4939-9030-6_18
Autor:
Brooke P Carpenter, Ivan Hung, Gemma R. Takahashi, Joana Paulino, Xi Chen, Rachel W. Martin, Marquise G. Crosby, Carter T. Butts, John E. Kelly, Marc A. Sprague-Piercy, Natalia Kozlyuk, Jan C. Bierma, Rongfu Zhang
Publikováno v:
Biomolecules, Vol 10, Iss 1069, p 1069 (2020)
Biomolecules
Volume 10
Issue 7
Biomolecules
Volume 10
Issue 7
The Droserasins, aspartic proteases from the carnivorous plant Drosera capensis, contain a 100-residue plant-specific insert (PSI) that is post-translationally cleaved and independently acts as an antimicrobial peptide. PSIs are of interest not only