Výsledky vyhledávání - "Ruddock, L. W."

Akademický článek

Autor: Morgan, B. J. T., Ridout, M. S., Ruddock, L. W.

Publikováno v: Biometrics, 2003 Sep 01. 59(3), 562-569.

Externí odkaz: https://www.jstor.org/stable/3695432

Introduction of a more glutaredoxin-like active site to PDI results in competition between protein substrate and glutathione binding

Autor: Saaranen, M. J. (Mirva J.), Alanen, H. I. (Heli I.), Salo, K. E. (Kirsi E. H.), Nji, E. (Emmanuel), Kärkkäinen, P. (Pekka), Schmotz, C. (Constanze), Ruddock, L. W. (Lloyd W.)

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://explore.openaire.eu/search/publication?articleId=od______2423::d3a3a66d5ecc35f5b1a2356247dc9266
http://urn.fi/urn:nbn:fi-fe2023061956380

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Efficient production of Fc fusion proteins in the cytoplasm of Escherichia coli:dissecting and mitigating redox heterogeneity

Autor: Tungekar, A. A. (Aatir A.), Ruddock, L. W. (Lloyd W.)

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=od______2423::525d9ec13147281943a1b99183997b57
http://urn.fi/urn:nbn:fi-fe2023060652613

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So you want to express your protein in Escherichia coli?

Autor: Tungekar, A. A. (Aatir A.), Castillo-Corujo, A. (Angel), Ruddock, L. W. (Lloyd W.)

Recombinant proteins have been extensively employed as therapeutics for the treatment of various critical and life-threatening diseases and as industrial enzymes in high-value industrial processes. Advances in genetic engineering and synthetic biolog

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od______2423::3a1d11940fcbd7d7e74bf1c6fe8aa42a
http://urn.fi/urn:nbn:fi-fe2022022420734

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High-resolution crystal structure of human pERp1, a saposin-like protein involved in IgA, IgM and integrin maturation in the endoplasmic reticulum

Autor: Sowa, S. T. (Sven T.), Moilanen, A. (Antti), Biterova, E. (Ekaterina), Saaranen, M. J. (Mirva J.), Lehtiö, L. (Lari), Ruddock, L. W. (Lloyd W.)

The folding of disulfide bond containing proteins in the endoplasmic reticulum (ER) is a complex process that requires protein folding factors, some of which are protein-specific. The ER resident saposin-like protein pERp1 (MZB1, CNPY5) is crucial fo

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od______2423::de7344efc202e7496e61f074de563207
http://urn.fi/urn:nbn:fi-fe2021041610685

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Non-native proteins inhibit the ER oxidoreductin 1 (Ero1)–protein disulfide-isomerase relay when protein folding capacity is exceeded

Autor: Moilanen, A. (Antti), Ruddock, L. W. (Lloyd W.)

Protein maturation in the endoplasmic reticulum (ER) depends on a fine balance between oxidative protein folding and quality control mechanisms, which together ensure high-capacity export of properly folded proteins from the ER. Oxidative protein fol

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od______2423::980d6ad9dccca93f11208f7fefed7573
http://urn.fi/urn:nbn:fi-fe2020090868880

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Exome sequencing reveals a phenotype modifying variant in ZNF528 in primary osteoporosis with a COL1A2 deletion

Autor: Skarp, S. (Sini), Xia, J. (Ji‐Han), Zhang, Q. (Qin), Löija, M. (Marika), Costantini, A. (Alice), Ruddock, L. W. (Lloyd W.), Mäkitie, O. (Outi), Wei, G. (Gong‐Hong), Männikkö, M. (Minna)

We studied a family with severe primary osteoporosis carrying a heterozygous p.Arg8Phefs*14 deletion in COL1A2, leading to haploinsufficiency. Three affected individuals carried the mutation and presented nearly identical spinal fractures but lacked

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od______2423::7255ee09a70993d59eb6b236caeb22dd
http://urn.fi/urn:nbn:fi-fe202101222357

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Cysteine 343 in the substrate binding domain is the primary S-Nitrosylated site in protein disulfide isomerase

Autor: Ogura, J. (Jiro), Ruddock, L. W. (Lloyd W.), Mano, N. (Nariyasu)

Abnormal protein accumulations are typical pathological features for neurodegenerative diseases. Protein disulfide isomerase (PDI) is a critical enzyme in oxidative protein folding. S-nitrosylated PDI has been detected in the postmortem brain in neur

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od______2423::026b36f0b6d584e56e4295e3ee382c8b
http://urn.fi/urn:nbn:fi-fe202103056643

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The crystal structure of human microsomal triglyceride transfer protein

Autor: Biterova, E. I. (Ekaterina I.), Isupov, M. N. (Michail N.), Keegan, R. M. (Ronan M.), Lebedev, A. A. (Andrey A.), Sohail, A. A. (Anil A.), Liaqat, I. (Inam), Alanen, H. I. (Heli I.), Ruddock, L. W. (Lloyd W.)

Microsomal triglyceride transfer protein (MTP) plays an essential role in lipid metabolism, especially in the biogenesis of very low-density lipoproteins and chylomicrons via the transfer of neutral lipids and the assembly of apoB-containing lipoprot

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od______2423::23f436b71838fa71eea35f45015d7b90
https://www.pnas.org/lookup/suppl/doi:10.1073/pnas.1903029116/-/DCSupplemental

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Applications of catalyzed cytoplasmic disulfide bond formation

Autor: Saaranen, M. J. (Mirva J.), Ruddock, L. W. (Lloyd W.)

Disulfide bond formation is an essential post-translational modification required for many proteins to attain their native, functional structure. The formation of disulfide bonds, otherwise known as oxidative protein folding, occurs in the endoplasmi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od______2423::10e8ea4126acb4cf5c8d2035499a2748
http://urn.fi/urn:nbn:fi-fe202103046550

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