Zobrazeno 1 - 10
of 125
pro vyhledávání: '"Lloyd W Ruddock"'
Publikováno v:
PLoS ONE, Vol 13, Iss 8, p e0202391 (2018)
NHLRC2 (NHL repeat-containing protein 2) is an essential protein. Mutations of NHLRC2, including Asp148Tyr, have been recently associated with a novel FINCA disease (fibrosis, neurodegeneration, cerebral angiomatosis), which is fatal in early childho
Externí odkaz:
https://doaj.org/article/a78080ecba3243e28e4aa71b036ebb11
Autor:
Anna Gąciarz, Lloyd W Ruddock
Publikováno v:
PLoS ONE, Vol 12, Iss 12, p e0189964 (2017)
CyDisCo is a system facilitating disulfide bond formation in recombinant proteins in the cytoplasm of Escherichia coli. Previously we screened for soluble expression of single chain antibody fragments (scFv) in the cytoplasm of E. coli in the presenc
Externí odkaz:
https://doaj.org/article/b20c4dca2bcf4e808e5ac0438e460c4b
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:
Alistair G Irvine, A Katrine Wallis, Narinder Sanghera, Michelle L Rowe, Lloyd W Ruddock, Mark J Howard, Richard A Williamson, Claudia A Blindauer, Robert B Freedman
Publikováno v:
PLoS ONE, Vol 9, Iss 1, p e82511 (2014)
In contrast to molecular chaperones that couple protein folding to ATP hydrolysis, protein disulfide-isomerase (PDI) catalyzes protein folding coupled to formation of disulfide bonds (oxidative folding). However, we do not know how PDI distinguishes
Externí odkaz:
https://doaj.org/article/0e34e8c1ec1741bcb3533b17bd207e47
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:
Aatir A. Tungekar, Lloyd W. Ruddock
Publikováno v:
International Journal of Molecular Sciences, Vol 23, Iss 23, p 14740 (2022)
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://doaj.org/article/4a9392ed841c47d0ab5555b6b0db3df8
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:
Drug Metabolism and Disposition. 51:764-770