Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Patricia M. Walden"'
Autor:
Selvakumar Edwardraja, Artem Melman, Paolo Bollella, Jason Whitfield, Patricia M. Walden, Claudia E. Vickers, Evgeny Katz, Zhong Guo, Kirill Alexandrov
Publikováno v:
ACS Sensors. 6:3596-3603
Enzymatic polypeptide proteolysis is a widespread and powerful biological control mechanism. Over the last few years, substantial progress has been made in creating artificial proteolytic systems where an input of choice modulates the protease activi
Autor:
Wayne A. Johnston, Kirill Alexandrov, Sergey Mureev, Dejan Gagoski, Robert G. Parton, Shayli Varasteh Moradi, Patricia M. Walden, Kerrie-Ann McMahon
Publikováno v:
Journal of Proteome Research. 19:1522-1532
The rapid spread of arthropod-borne Zika virus poses a serious public health threat that calls for effective ways of controlling and treating viral infection. This in turn necessitates better understanding of the mechanisms of virus assembly and its
Autor:
Zhong Guo, Kirill Alexandrov, Evgeny Katz, Jacobus P.J. Ungerer, Patricia M. Walden, Cagla Ergun Ayva, Oleh Smutok, Wayne A. Johnston, Artem Melman, Brett McWhinney
Publikováno v:
Angewandte Chemie (International ed. in English). 61(6)
Protein biosensors play an increasingly important role as reporters for research and clinical applications. Here we present an approach for the construction of fully integrated but modular electrochemical biosensors based on the principal component o
Autor:
Wayne A. Johnston, Selvakumar Edwardraja, Zhenling Cui, Jason Whitfield, Fernanda Ely, Elvira Wijker, Ignacio Retamal Lantadilla, Jacobus P.J. Ungerer, Patricia M. Walden, Claudia E. Vickers, Zhong Guo, Kirill Alexandrov
Publikováno v:
Journal of the American Chemical Society. 141:8128-8135
Allosteric protein switches are key controllers of information and energy processing in living organisms and are desirable engineered control tools in synthetic systems. Here we present a generally applicable strategy for construction of allosteric s
Autor:
Lakshmanane Premkumar, Begoña Heras, Andrew E. Whitten, Jennifer L. Martin, Gordon J. King, Patricia M. Walden, Maria A. Halili
Publikováno v:
Acta Crystallographica. Section D, Structural Biology
The disulfide isomerase α-DsbA2 from Wolbachia pipientisis is unexpectedly homotrimeric and lacks the ‘shape-shifting’ conformational flexibility that defines another trimeric disulfide isomerase, ScsC from Proteus mirabilis.
Disulfide-bond
Disulfide-bond
Autor:
Patricia M Walden, Maria A Halili, Julia K Archbold, Fredrik Lindahl, David P Fairlie, Kenji Inaba, Jennifer L Martin
Publikováno v:
PLoS ONE, Vol 8, Iss 11, p e81440 (2013)
The α-proteobacterium Wolbachia pipientis infects more than 65% of insect species worldwide and manipulates the host reproductive machinery to enable its own survival. It can live in mutualistic relationships with hosts that cause human disease, inc
Externí odkaz:
https://doaj.org/article/8ab836e21a37448581a777dff3304497
Autor:
Ignacio Retamal Lantadilla, Claudia E. Vickers, Patricia M. Walden, Jason Whitfield, Zhong Guo, Kirill Alexandrov, Wayne A. Johnston, Selvakumar Edwardraja
Publikováno v:
ACS synthetic biology. 9(6)
The ability of proteins to interconvert unrelated biochemical inputs and outputs underlays most energy and information processing in biology. A common conversion mechanism involves a conformational change of a protein receptor in response to a ligand
Autor:
Jennifer L. Martin, David P. Fairlie, Wilko Duprez, Begoña Heras, Maria A. Halili, Lakshmanane Premkumar, Fabian Kurth, Patricia M. Walden
Publikováno v:
Acta Crystallographica Section D: Biological Crystallography
The gene product of M. tuberculosis Rv2969c is shown to be a disulfide oxidase enzyme that has a canonical DsbA-like fold with novel structural and functional characteristics.
The bacterial disulfide machinery is an attractive molecular target f
The bacterial disulfide machinery is an attractive molecular target f
Autor:
Jennifer L. Martin, Begoña Heras, Stephen R. Shouldice, Makrina Totsika, Patricia M. Walden, Mark A. Schembri
Publikováno v:
Antioxidants & Redox Signaling. 14:1729-1760
Since its discovery in 1991, the bacterial periplasmic oxidative folding catalyst DsbA has been the focus of intense research. Early studies addressed why it is so oxidizing and how it is maintained in its less stable oxidized state. The crystal stru
Autor:
Maria A. Halili, David P. Fairlie, Jennifer L. Martin, Kenji Inaba, Patricia M. Walden, Julia K. Archbold, Fredrik Lindahl
Publikováno v:
PLoS ONE, Vol 8, Iss 11, p e81440 (2013)
PLoS ONE
PLoS ONE
The α-proteobacterium Wolbachia pipientis infects more than 65% of insect species worldwide and manipulates the host reproductive machinery to enable its own survival. It can live in mutualistic relationships with hosts that cause human disease, inc