m-dPEG®₈-MAL

m-dPEG®₂₄-MAL (#10319)

Greg T. Hermanson, Bioconjugate Techniques, 2nd Edition, Elsevier Inc., Burlington, MA 01803, April, 2008 (ISBN-13: 978-0-12-370501-3; ISBN-10: 0-12-370501-0). Specifically see pp. 726-729 in his Chapter 18 on discrete PEG compounds for pegylation applications.

Greg T. Hermanson, Bioconjugate Techniques, 3rd Edition, Elsevier, Waltham, MA 02451, 2013, ISBN 978-0-12-382239-0; See chapter 18, Discrete PEG Reagents, pp.787-821, for a full overview of the dPEG® products.

Modulation of Cell Surface Protein Free Thiols: A Potential Novel Mechanism of Action of the Sesquiterpene Lactone Parthenolide. Jolanta Skalska, Paul S. Brookes, Sergiy M. Nadtochiy, Shannon P. Hilchey, Craig T. Jordan, Monica L. Guzman, Sanjay B. Maggirwar, Margaret M. Briehl, Steven H. Bernstein. PLoS ONE. 4 (12), e8115. December 2, 2009. DOI: 10.1371 /journal.pone.0008115.

Cell-Specific Delivery of Diverse Cargos by BacteriophageMS2 Virus-like Particles. Carlee E. Ashley Eric C. Carnes, Genevieve K. Phillips, Paul N. Durfee, Mekensey D. Buley, Christopher A. Lino, David P. Padilla, Brandy Phillips, Mark B. Carter, Cheryl L. Willman, C. Jeffrey Brinker, Jerri do Carmo Caldeira, Bryce Chackerian, Walker Wharton, and David S. Peabody.ACS Nano, 2011, 5 (7), pp 5729–5745, May 26, 2011. DOI: 10.1021/nn201397z.

Going through the barrier: coupled disulfide exchange reactions promote efficient catalysis in Quiescin sulfhydryl oxidase. Benjamin A. Israel, Vamsi K. Kodali, and Colin Thorpe. The Journal of Biological Chemistry. 2013, December 30, 2013. DOI: 10.1074/jbc.M113.536219.

2-Cys peroxiredoxins participate in the oxidation of chloroplast enzymes in the dark. Valle Ojeda, Juan Manuel, Pérez-Ruiz, and Francisco Javier Cejudo. Molecular Plant. 2018, pp 1-32. October 4, 2018. DOI: 10.1016/j.molp.2018.09.005.

Complement Activation and Cell Uptake Responses Toward Polymer-Functionalized Protein Nanocapsules. Nicholas M. Molino, Kateryna Bilotkach, Deborah A. Fraser, Dongmei Ren, and Szu-Wen Wang. Biomacromolecules, 2012, 13 (4), pp 974–981. March 14, 2012. DOI: 10.1021/bm300083e.

Redox-regulated dynamic interplay between Cox19 and the copper-binding protein Cox11 in the intermembrane space of mitochondria facilitates biogenesis of cytochrome c oxidase. Manuela Bode, Michael W. Woellhaf, Maria Bohnert, Martin van der Laan, Frederik Sommer, Martin Jung, Richard Zimmermann, Michael Schroda, Johannes M. Herrmann. Molecular Biology of the Cell. April 29, 2015. DOI: 10.1091/mbc.E14-11-1526

NTRC-dependent redox balance of 2-Cys peroxiredoxins is needed for optimal function of the photosynthetic apparatus. Juan Manuel Pérez-Ruiz, Belén Naranjo, Valle Ojeda, Manuel Guinea, and Francisco Javier Cejudo. Proceedings of the National Academy of Sciences of the United States of America. 2017, 114 (45) pp 12069-12074. 9/26/2017. DOI: 10.1073/pnas.1706003114.

m-dPEG®₁₂-MAL (#10289)

Greg T. Hermanson, Bioconjugate Techniques, 2nd Edition, Elsevier Inc., Burlington, MA 01803, April, 2008 (ISBN-13: 978-0-12-370501-3; ISBN-10: 0-12-370501-0). See all of the extensive references to the reactions of maleimides with a variety of compounds and applications, Hermanson, p.1174 (index for maleimides) and references therein.

Greg T. Hermanson, Bioconjugate Techniques, 3rd Edition, Elsevier, Waltham, MA 02451, 2013, ISBN 978-0-12-382239-0; See Chapter 18, Discrete PEG Reagents, pp. 787-821, for a full overview of the dPEG® products.

Homodimerisation of the Lymph Vessel Endothelial Receptor LYVE-1 through a Redox-Labile Disulfide is Critical for Hyaluronan Binding in Lymphatic Endothelium. Suneale Banerji, William Lawrance, Clive Metcalfe, David C. Briggs, Akira Yamauchi, Omer Dushek, P. Anton van der Merwe, Anthony J. Day, and David G. Jackson. The Journal of Biological Chemistry. 2016, October 12, 2016. DOI: 10.1074/jbc.M116.736926.

Interleukin-2 signalling is modulated by a labile disulfide bond in the CD132 chain of its receptor. Clive Metcalfe, Peter Cresswell and A. Neil Barclay. Open Biology. 2012, 2 (1). January 11, 2012. DOI: 10.1098/rsob.110036.

DksA2, a zinc-independent structural analog of the transcription factor DksA. Ran Furman, Tapan Biswas, Eric M. Danhart, Mark P. Foster, Oleg V. Tsodikov, Irina Artsimovitch. FEBS Letters. 2013, 587 (6) pp 614–619. January 31, 2013. DOI: 10.1016/j.febslet.2013.01.073.

Rapid ratiometric biomarker detection with topically applied SERS nanoparticles. Yu “Winston” Wang, Altaz Khan, Madhura Som, Danni Wang, Ye Chen, Steven Y. Leigh, Daphne Meza, Patrick Z. McVeigh, Brian C. Wilson and Jonathan T.C. Liu. Technology. 2014, 2 (2) pp 1-15. May 19, 2014. DOI: 10.1142/S2339547814500125.

Redox-regulated dynamic interplay between Cox19 and the copper-binding protein Cox11 in the intermembrane space of mitochondria facilitates biogenesis of cytochrome c oxidase. Manuela Bode, Michael W. Woellhaf, Maria Bohnert, Martin van der Laan, Frederik Sommer, Martin Jung, Richard Zimmermann, Michael Schroda, Johannes M. Herrmann. Molecular Biology of the Cell. April 29, 2015. DOI: 10.1091/mbc.E14-11-1526

A glutaredoxin in the mitochondrial intermembrane space has stage-specific functions in the thermo-tolerance and proliferation of African trypanosomes. Samantha Ebersoll, Blessing Musunda, Torsten Schmenger, Natalie Dirdjaja, Marian Bonilla, Bruno Manta, Kathrin Ulrich, Marcelo A. Comini, and R. Luise Krauth-Siegel. Redox Biology. 2018, 15, pp 532-547. January 31, 2018. DOI: 10.1016/j.redox.2018.01.011.

MAL-dPEG®₄-(m-dPEG®₂₄)₃ (#10456)

Greg T. Hermanson, Bioconjugate Techniques, 2nd Edition, Elsevier Inc., Burlington, MA 01803, April, 2008 (ISBN-13: 978-0-12-370501-3; ISBN-10: 0-12-370501-0). Chapter 1, p. 30.

Greg T. Hermanson, Bioconjugate Techniques, 3rd Edition, Elsevier, Waltham, MA 02451, 2013, ISBN 978-0-12-382239-0; See Chapter 18, Discrete PEG Reagents, pp. 787-821, for a full overview of the dPEG® products.