Zobrazeno 1 - 10
of 123
pro vyhledávání: '"Lloyd W. Ruddock"'
Publikováno v:
Scientific Reports, Vol 14, Iss 1, Pp 1-11 (2024)
Abstract Fibulin-2 is a multidomain, disulfide-rich, homodimeric protein which belongs to a broader extracellular matrix family. It plays an important role in the development of elastic fiber structures. Malfunction of fibulin due to mutation or poor
Externí odkaz:
https://doaj.org/article/07b6c39d37bc4aaba300f8dc23304b3f
Autor:
Aatir A. Tungekar, Lloyd W. Ruddock
Publikováno v:
Scientific Reports, Vol 13, Iss 1, Pp 1-10 (2023)
Abstract With increased accessibility and tissue penetration, smaller antibody formats such as antibody fragments (Fab) and single chain variable fragments (scFv) show potential as effective and low-cost choices to full-length antibodies. These forma
Externí odkaz:
https://doaj.org/article/d963382c805f4fb783fd7803dab4c2b2
Publikováno v:
Scientific Reports, Vol 13, Iss 1, Pp 1-12 (2023)
Abstract Global health challenges such as the coronavirus pandemic warrant the urgent need for a system that allows efficient production of diagnostic and therapeutic interventions. Antibody treatments against SARS-CoV-2 were developed with an unprec
Externí odkaz:
https://doaj.org/article/90b7d1ca49914b27b9d29dd9dd4f78b5
Publikováno v:
MicrobiologyOpen, Vol 12, Iss 2, Pp n/a-n/a (2023)
Abstract High‐value heterologous proteins produced in Escherichia coli that contain disulfide bonds are almost invariably targeted to the periplasm via the Sec pathway as it, among other advantages, enables disulfide bond formation and simplifies d
Externí odkaz:
https://doaj.org/article/a1e396970f3548a29fe9d0d343ba4aa0
Autor:
Mirva J. Saaranen, Heli I. Alanen, Kirsi E. H. Salo, Emmanuel Nji, Pekka Kärkkäinen, Constanze Schmotz, Lloyd W. Ruddock
Publikováno v:
Antioxidants, Vol 11, Iss 10, p 1920 (2022)
Proteins in the thioredoxin superfamily share a similar fold, contain a -CXXC- active site, and catalyze oxidoreductase reactions by dithiol-disulfide exchange mechanisms. Protein disulfide isomerase (PDI) has two -CGHC- active sites. For in vitro st
Externí odkaz:
https://doaj.org/article/1e58d329cb18476c956b5ec56f05aec3
Publikováno v:
Scientific Reports, Vol 8, Iss 1, Pp 1-12 (2018)
Abstract Coronary artery disease is the most common cause of death globally and is linked to a number of risk factors including serum low density lipoprotein, high density lipoprotein, triglycerides and lipoprotein(a). Recently two proteins, angiopoi
Externí odkaz:
https://doaj.org/article/4b52b49cf90646698db345f847aeac53
Autor:
Anna Gąciarz, Narendar Kumar Khatri, M. Lourdes Velez-Suberbie, Mirva J. Saaranen, Yuko Uchida, Eli Keshavarz-Moore, Lloyd W. Ruddock
Publikováno v:
Microbial Cell Factories, Vol 16, Iss 1, Pp 1-12 (2017)
Abstract Background The production of recombinant proteins containing disulfide bonds in Escherichia coli is challenging. In most cases the protein of interest needs to be either targeted to the oxidizing periplasm or expressed in the cytoplasm in th
Externí odkaz:
https://doaj.org/article/975a1d4b5d574b23b1ebbdb2d51f4762
Publikováno v:
Drug Metabolism and Disposition. 51:764-770
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::07959edd21123d4b6469092cc2472d76
https://doi.org/10.1124/dmd.122.001244
https://doi.org/10.1124/dmd.122.001244
Publikováno v:
FEBS Letters.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e72b7a569bff28c92b0b9357e60ce869
https://doi.org/10.1002/1873-3468.14669
https://doi.org/10.1002/1873-3468.14669
Autor:
Aatir A, Tungekar, Lloyd W, Ruddock
Publikováno v:
International journal of molecular sciences. 23(23)
Cost-effective production of therapeutic proteins in microbial hosts is an indispensable tool towards accessible healthcare. Many of these heterologously expressed proteins, including all antibody formats, require disulfide bond formation to attain t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::609b67007b55c55cce78ae6208d36238
https://pubmed.ncbi.nlm.nih.gov/36499069
https://pubmed.ncbi.nlm.nih.gov/36499069