Transfer of disulfide bond formation modules via yeast artificial chromosomes promotes the expression of heterologous proteins in Kluyveromyces marxianus

Authors: Pingping Wu, Wenjuan Mo, Tian Tian, Kunfeng Song, Yilin Lyu, Haiyan Ren, Jungang Zhou, Yao Yu, Hong Lu

Source: mLife, Vol 3, Iss 1, Pp 129-142 (2024)

Subject Terms: disulfide bond formation, expression of heterologous proteins, Kluyveromyces marxianus, telomere, yeast artificial chromosome, Microbiology, QR1-502

File Description: electronic resource

Relation: https://doaj.org/toc/2770-100X

Access URL: https://doaj.org/article/aae96c0d41aa432aaf08c546dd77cd9f

Scalable production of recombinant three-finger proteins: from inclusion bodies to high quality molecular probes

Authors: Jiang Xu, Xiao Lei, Ao Li, Jun Li, Shuxing Li, Lin Chen

Source: Microbial Cell Factories, Vol 23, Iss 1, Pp 1-14 (2024)

Subject Terms: Three finger protein, E. coli recombinant expression, Inclusion body refolding, Disulfide bond formation, Oxidation refolding, Microbiology, QR1-502

File Description: electronic resource

Relation: https://doaj.org/toc/1475-2859

Access URL: https://doaj.org/article/60389c4a8f0643e8bda72292a47db618

Evidence that protein thiols are not primary targets of intracellular reactive oxygen species in growing Escherichia coli

Authors: Stefanie S. Eben, James A. Imlay

Source: Frontiers in Microbiology, Vol 14 (2023)

Subject Terms: oxidative stress, glutaredoxin, thioredoxin, E. coli, disulfide bond formation, Microbiology, QR1-502

File Description: electronic resource

Relation: https://www.frontiersin.org/articles/10.3389/fmicb.2023.1305973/full; https://doaj.org/toc/1664-302X

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A quantitative interpretation of oxidative protein folding activity in Escherichia coli

Authors: Lukas A. Rettenbacher, Tobias von der Haar

Source: Microbial Cell Factories, Vol 21, Iss 1, Pp 1-12 (2022)

Subject Terms: Escherichia coli, Disulfide bond formation, Oxidative folding, Disulfide proteome, Kinetic modelling, Systems biology, Microbiology, QR1-502

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Relation: https://doaj.org/toc/1475-2859

Access URL: https://doaj.org/article/cb5a42f6086844d58eac50577ef0b87b

Arthropod Venom Components and Their Potential Usage

Authors: Konno, Katsuhiro, Rádis-Baptista, Gandhi

Subject Terms: R5-920, RA1190-1270, spider toxin, hybrid immunogen, channel-like pore-forming activity, venom peptides, chemotherapy, piperidine heterocyclic amines, computational docking, insect immune system, venom, toxoplasmosis, wasps, ion channel structure, mechanical allodynia, Dinoponera quadriceps, natural antibiotics, bees, acid-gated currents, nematicide, novel therapeutics, toxins, protons, Hymenoptera venom, ants, chronic pain, heart contractility, transcriptome, drug targets, skin, peptides, LTQ Orbitrap Hybrid Mass Spectrometer, cantharidin, Centruroides limpidus Karch, pilosulin-like peptide, mechanism, scorpion, stent, homology modelling, amphipathic ?-helix structure, Berberomeloe majalis, mass spectrometric analysis, phospholipases D, Nav1.7, biotools, metalloproteases, myrmecology, Tenebrio molitor, antifeedant, ixodicide, virtual screening, Loxosceles, acid-sensing ion channels, small hive beetle, knottins, Nav channel activity, envenomation, pharmacology, Staphylococcus aureus, spider venom, scorpion venom, insecticidal peptide, Formicidae, AMP, de novo sequencing, tertiapin, leishmaniasis, brown spider, proteome, keratitis, Acinetobacter baumannii, neuropathic pain, bee venom, bioinformatics, ICK peptide, human African trypanosomiasis, automated patch-clamp, Hymenoptera, antimicrobial peptide, LyeTxI-b, linear cationic ?-helical peptide, melittin, Chagas disease, mass spectrometry analysis, neutralizing antibodies, apoptosis, protein–peptide interactions, malaria, pH regulation, voltage-gated sodium channel, venom toxicity, insect neurotoxin, solitary wasp, oxaliplatin, arthropod, mastoparan, cold allodynia, pain target, cutaneous disease, pain, NaV, proteomics, industrial biotechnology, ant, directed disulfide bond formation, antivenoms, blister beetle, venom allergens, ICK-like toxins, Loxosceles spp., alternative treatment, recombinant toxins, FMRF-amide, Medicine and Nursing

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Access URL: https://directory.doabooks.org/handle/20.500.12854/41343
https://mdpi.com/books/pdfview/book/2126

Breaking antimicrobial resistance by disrupting extracytoplasmic protein folding

Authors: R Christopher D Furniss, Nikol Kaderabkova, Declan Barker, Patricia Bernal, Evgenia Maslova, Amanda AA Antwi, Helen E McNeil, Hannah L Pugh, Laurent Dortet, Jessica MA Blair, Gerald Larrouy-Maumus, Ronan R McCarthy, Diego Gonzalez, Despoina AI Mavridou

Source: eLife, Vol 11 (2022)

Subject Terms: antimicrobial resistance, disulfide bond formation, cell envelope, K. pneumoniae, P. aeruginosa, G. mellonella, Medicine, Science, Biology (General), QH301-705.5

File Description: electronic resource

Relation: https://elifesciences.org/articles/57974; https://doaj.org/toc/2050-084X

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Comparative proteome analysis in an Escherichia coli CyDisCo strain identifies stress responses related to protein production, oxidative stress and accumulation of misfolded protein

Authors: Isabel Guerrero Montero, Katarzyna Magdalena Dolata, Rabea Schlüter, Gilles Malherbe, Susanne Sievers, Daniela Zühlke, Thomas Sura, Emma Dave, Katharina Riedel, Colin Robinson

Source: Microbial Cell Factories, Vol 18, Iss 1, Pp 1-15 (2019)

Subject Terms: Escherichia coli CyDisCo, Twin-arginine transport, Recombinant protein, Disulfide bond formation, Misfolding, Proteome, Microbiology, QR1-502

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Relation: http://link.springer.com/article/10.1186/s12934-019-1071-7; https://doaj.org/toc/1475-2859

Access URL: https://doaj.org/article/399c3e37f4cd4ef5837d604c5b84ca95

The Molecular Basis for Erns Dimerization in Classical Swine Fever Virus

Authors: Manjula Mischler, Gregor Meyers

Source: Viruses, Vol 13, Iss 11, p 2204 (2021)

Subject Terms: pestivirus, flavivirus, envelope protein, dimerization of glycoprotein, amphipathic helix, disulfide bond formation, Microbiology, QR1-502

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Relation: https://www.mdpi.com/1999-4915/13/11/2204; https://doaj.org/toc/1999-4915

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Erv1 of Arabidopsis thaliana can directly oxidize mitochondrial intermembrane space proteins in the absence of redox-active Mia40

Authors: Valentina Peleh, Flavien Zannini, Sandra Backes, Nicolas Rouhier, Johannes M. Herrmann

Source: BMC Biology, Vol 15, Iss 1, Pp 1-14 (2017)

Subject Terms: Disulfide bond formation, Eukaryotic evolution, Intermembrane space, Mitochondria, Oxidative protein folding, Protein translocation, Biology (General), QH301-705.5

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Relation: http://link.springer.com/article/10.1186/s12915-017-0445-8; https://doaj.org/toc/1741-7007

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PDIA1/P4HB is required for efficient proinsulin maturation and ß cell health in response to diet induced obesity

Authors: Insook Jang, Anita Pottekat, Juthakorn Poothong, Jing Yong, Jacqueline Lagunas-Acosta, Adriana Charbono, Zhouji Chen, Donalyn L Scheuner, Ming Liu, Pamela Itkin-Ansari, Peter Arvan, Randal J Kaufman

Source: eLife, Vol 8 (2019)

Subject Terms: PDIA1, proinsulin maturation, beta cell function, glucose homeostasis, disulfide bond formation, type 2 diabetes, Medicine, Science, Biology (General), QH301-705.5

File Description: electronic resource

Relation: https://elifesciences.org/articles/44528; https://doaj.org/toc/2050-084X

Access URL: https://doaj.org/article/606748e9851d4069a19e7e64c04c8f22

Adiporedoxin, an upstream regulator of ER oxidative folding and protein secretion in adipocytes

Authors: Mark P. Jedrychowski, Libin Liu, Collette J. Laflamme, Kalypso Karastergiou, Tova Meshulam, Shi-Ying Ding, Yuanyuan Wu, Mi-Jeong Lee, Steven P. Gygi, Susan K. Fried, Paul F. Pilch

Source: Molecular Metabolism, Vol 4, Iss 11, Pp 758-770 (2015)

Subject Terms: Adipocyte, Adipokine, Protein secretion, Endoplasmic reticulum, Oxidoreductase, Disulfide bond formation, Internal medicine, RC31-1245

File Description: electronic resource

Relation: http://www.sciencedirect.com/science/article/pii/S2212877815001726; https://doaj.org/toc/2212-8778

Access URL: https://doaj.org/article/a3dc06a4d9be427492c6dea1f64ccac4

Cell-Free Synthesis Meets Antibody Production: A Review

Authors: Marlitt Stech, Stefan Kubick

Source: Antibodies, Vol 4, Iss 1, Pp 12-33 (2015)

Subject Terms: cell-free, cell-free protein synthesis, antibody, antibody fragment, scFv, disulfide bond formation, microsomal vesicles, eukaryotic lysate, Immunologic diseases. Allergy, RC581-607

File Description: electronic resource

Relation: http://www.mdpi.com/2073-4468/4/1/12; https://doaj.org/toc/2073-4468

Access URL: https://doaj.org/article/493bf686bfbe4a548e7096b24327ddc3

Absence of Thiol-Disulfide Oxidoreductase DsbA Impairs cbb3-Type Cytochrome c Oxidase Biogenesis in Rhodobacter capsulatus

Authors: Ozlem Onder, Andreia F. Verissimo, Bahia Khalfaoui-Hassani, Annette Peters, Hans-Georg Koch, Fevzi Daldal

Source: Frontiers in Microbiology, Vol 8 (2017)

Subject Terms: disulfide bond formation, copper homeostasis, cbb3-type cytochrome c oxidase biogenesis, Rhodobacter capsulatus, respiration, photosynthesis, Microbiology, QR1-502

File Description: electronic resource

Relation: http://journal.frontiersin.org/article/10.3389/fmicb.2017.02576/full; https://doaj.org/toc/1664-302X

Access URL: https://doaj.org/article/ce0021b3511948dab81271c0bc8e6291

Chemical Synthesis, Proper Folding, Nav Channel Selectivity Profile and Analgesic Properties of the Spider Peptide Phlotoxin 1

Authors: Sébastien Nicolas, Claude Zoukimian, Frank Bosmans, Jérôme Montnach, Sylvie Diochot, Eva Cuypers, Stephan De Waard, Rémy Béroud, Dietrich Mebs, David Craik, Didier Boturyn, Michel Lazdunski, Jan Tytgat, Michel De Waard

Source: Toxins, Vol 11, Iss 6, p 367 (2019)

Subject Terms: spider toxin, directed disulfide bond formation, Nav channel activity, Nav1.7, pain target, automated patch-clamp, Medicine

File Description: electronic resource

Relation: https://www.mdpi.com/2072-6651/11/6/367; https://doaj.org/toc/2072-6651

Access URL: https://doaj.org/article/e86d22f9474449df85156f8c0d4cf8f5

Molecular Mechanisms of the Methionine Sulfoxide Reductase System from Neisseria meningitidis

Authors: Sandrine Boschi-Muller

Source: Antioxidants, Vol 7, Iss 10, p 131 (2018)

Subject Terms: methionine sulfoxide, MSR, PilB, Trx, periplasm, disulfide-bond formation (Dsb) D, Therapeutics. Pharmacology, RM1-950

File Description: electronic resource

Relation: http://www.mdpi.com/2076-3921/7/10/131; https://doaj.org/toc/2076-3921

Access URL: https://doaj.org/article/c2a3c7c305b34c90bced6a55c6382800

Protein Folding and Assembly

Authors: Rudi Glockshuber

Source: CHIMIA, Vol 55, Iss 4 (2001)

Subject Terms: Catalysis of disulfide bond formation, Prion proteins, Protein assembly, Protein folding, Type 1 pili, Chemistry, QD1-999

File Description: electronic resource

Relation: https://www.chimia.ch/chimia/article/view/3406; https://doaj.org/toc/0009-4293; https://doaj.org/toc/2673-2424

Access URL: https://doaj.org/article/6ca67b99a8fd43e4ae7e3b1504468b22

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SHuffle, a novel Escherichia coli protein expression strain capable of correctly folding disulfide bonded proteins in its cytoplasm

Authors: Lobstein Julie, Emrich Charlie A, Jeans Chris, Faulkner Melinda, Riggs Paul, Berkmen Mehmet

Source: Microbial Cell Factories, Vol 11, Iss 1, p 56 (2012)

Subject Terms: SHuffle, Protein expression strain, Disulfide bond formation, Disulfide bond isomerization, DsbC, trxB, gor, ahpC*, Microbiology, QR1-502

File Description: electronic resource

Relation: http://www.microbialcellfactories.com/content/11/1/56; https://doaj.org/toc/1475-2859

Access URL: https://doaj.org/article/1ba6a13507564c98854f2f47e660d209

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