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pro vyhledávání: '"Tochowicz, A"'
Autor:
Tochowicz, Kacper
Publikováno v:
Śląskie Studia Polonistyczne; 2023, Vol. 21 Issue 1, p1-10, 10p
Publikováno v:
IEEE Software. 36:101-104
Automation has been replacing manual activities in workplace for decades. Robots had been most active in blue-collar industrial manufacturing. Now that they are entering white-collar jobs, in the form of software taking over administrative work, it i
Akademický článek
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Autor:
Daniela Cardinale, Maria Paola Costi, Puneet Saxena, Outi M. H. Salo-Ahen, Cecilia Pozzi, Hannu Myllykallio, Stefano Mangani, Rebecca C. Wade, Robert M. Stroud, Anna Tochowicz, Yap Boum, Glauco Ponterini, Stefania Ferrari
Publikováno v:
Salo-Ahen, Outi H.; Tochowicz, Anna; Pozzi, Cecilia; Cardinale, Daniela; Ferrari, Stefania; Boum, Yap; et al.(2015). Hotspots in an Obligate Homodimeric Anticancer Target. Structural and Functional Effects of Interfacial Mutations in Human Thymidylate Synthase. Journal of medicinal chemistry, 58(8), 3572-3581. UC Office of the President: Multicampus Research Programs and Initiatives (MRPI); a funding opportunity through UC Research Initiatives (UCRI). Retrieved from: http://www.escholarship.org/uc/item/5dv4g2t4
Human thymidylate synthase (hTS), a target for antiproliferative drugs, is an obligate homodimer. Single-point mutations to alanine at the monomer–monomer interface may enable the identification of specific residues that delineate sites for drugs a
Autor:
Janet Finer-Moore, Giambattista Guaitoli, Maria Paola Costi, Anna Tochowicz, Matteo Trande, Robert M. Stroud, Puneet Saxena, Matteo Santucci
Publikováno v:
Tochowicz, A; Santucci, M; Saxena, P; Guaitoli, G; Trande, M; Finer-Moore, J; et al.(2015). Alanine mutants of the interface residues of human thymidylate synthase decode key features of the binding mode of allosteric anticancer peptides. J Med Chem, 58(2). UC Office of the President: Multicampus Research Programs and Initiatives (MRPI); a funding opportunity through UC Research Initiatives (UCRI). Retrieved from: http://www.escholarship.org/uc/item/8k4226b6
J Med Chem
J Med Chem
Allosteric peptide inhibitors of thymidylate synthase (hTS) bind to the dimer interface and stabilize the inactive form of the protein. Four interface residues were mutated to alanine, and interaction studies were employed to decode the key role of t
Autor:
Janet Finer-Moore, Oliv Eidam, Sarah L. Griner, Joseph D. O'Connell, Anna Tochowicz, Sean Mark Dalziel, Robert M. Stroud
Publikováno v:
Journal of Medicinal Chemistry. 56:5446-5455
N-[4-[2-Propyn-1-yl[(6S)-4,6,7,8-tetrahydro-2-(hydroxymethyl)-4-oxo-3H-cyclopenta[g]quinazolin-6-yl]amino]benzoyl]-l-γ-glutamyl-d-glutamic acid 1 (BGC 945, now known as ONX 0801), is a small molecule thymidylate synthase (TS) inhibitor discovered at
Autor:
Yinyan Tang, Anna Tochowicz, William R. Roush, Brian D. Jones, James H. McKerrow, Ken Hirata, Jair L. Siqueira-Neto, Michael D. Cameron, Laura-Isobel McCall, Sharon L. Reed
Publikováno v:
Jones, BD; Tochowicz, A; Tang, Y; Cameron, MD; McCall, L-I; Hirata, K; et al.(2016). Synthesis and Evaluation of Oxyguanidine Analogues of the Cysteine Protease Inhibitor WRR-483 against Cruzain. ACS MEDICINAL CHEMISTRY LETTERS, 7(1), 77-82. doi: 10.1021/acsmedchemlett.5600336. UC San Diego: Retrieved from: http://www.escholarship.org/uc/item/2rb1s2cz
ACS MEDICINAL CHEMISTRY LETTERS, vol 7, iss 1
ACS MEDICINAL CHEMISTRY LETTERS, vol 7, iss 1
A series of oxyguanidine analogues of the cysteine protease inhibitor WRR-483 were synthesized and evaluated against cruzain, the major cysteine protease of the protozoan parasite Trypanosoma cruzi. Kinetic analyses of these analogues indicated that
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::808a9ad014e9376509408ec8c6623b47
http://www.escholarship.org/uc/item/2rb1s2cz
http://www.escholarship.org/uc/item/2rb1s2cz
Autor:
Anna Tochowicz, Klaus Richter, Hideaki Nagase, Wolfram Bode, Robert Visse, Klaus Maskos, Richard Evans, Peter Goettig, Noriko Ito, Yoshifumi Itoh, Daniel Franke, Ralf Palmisano, Yasuyuki Shitomi, Dmitri I. Svergun
Publikováno v:
The journal of biological chemistry 286, 7587-7600 (2011). doi:10.1074/jbc.M110.178434
The Journal of Biological Chemistry
The Journal of Biological Chemistry
Homodimerization is an essential step for membrane type 1 matrix metalloproteinase (MT1-MMP) to activate proMMP-2 and to degrade collagen on the cell surface. To uncover the molecular basis of the hemopexin (Hpx) domain-driven dimerization of MT1-MMP
Autor:
M Świerad, Marian Simka, Marcin Hartel, Paweł Latacz, Tomasz Ludyga, L Sedlak, M Tochowicz, Marek Kazibudzki, J Piegza
Publikováno v:
Phlebology: The Journal of Venous Disease. 25:286-295
Objectives The aim of this report is to assess the safety of endovascular treatment for chronic cerebrospinal venous insufficiency (CCSVI). Although balloon angioplasty and stenting seem to be safe procedures, there are currently no data on the treat