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Masa Cemazar

Showing results (11-20 of 20) with videos related to

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Current Topics in Medicinal Chemistry|July 26, 2012
Discovery and applications of disulfide-rich cyclic peptidesMasa Cemazar, Soohyun Kwon, Tunjung Mahatmanto, et al.
Trends in Biochemical Sciences|July 4, 2006
Protein disulfide isomerase: the structure of oxidative foldingChristian W Gruber, Masa Cemazar, Begoña Heras, et al.
Biopolymers|November 6, 2008
Biochemical and biophysical characterization of a novel plant protein disulfide isomeraseChristian W Gruber, Masa Cemazar, Adam Mechler, et al.
Structure (London, England : 1993)|June 13, 2008
The structure of a two-disulfide intermediate assists in elucidating the oxidative folding pathway of a cyclic cystine knot proteinMasa Cemazar, Ajinkya Joshi, Norelle L Daly, et al.
Protein Engineering|October 16, 2003
Vicinal disulfide turnsOliviero Carugo, Masa Cemazar, Sotir Zahariev, et al.
The Journal of Biological Chemistry|March 21, 2006
Knots in rings. The circular knotted protein Momordica cochinchinensis trypsin inhibitor-II folds via a stable two-disulfide intermediateMasa Cemazar, Norelle L Daly, Sara Häggblad, et al.
Proceedings of the National Academy of Sciences of the United States of America|May 2, 2003
Oxidative folding intermediates with nonnative disulfide bridges between adjacent cysteine residuesMasa Cemazar, Sotir Zahariev, Jakob J Lopez, et al.
Biochemistry|April 7, 2011
The role of conserved Glu residue on cyclotide stability and activity: a structural and functional study of kalata B12, a naturally occurring Glu to Asp mutantConan K L Wang, Richard J Clark, Peta J Harvey, et al.
The Journal of Biological Chemistry|May 25, 2007
A novel plant protein-disulfide isomerase involved in the oxidative folding of cystine knot defense proteinsChristian W Gruber, Masa Cemazar, Richard J Clark, et al.
The Journal of Biological Chemistry|December 14, 2007
Staphylococcus aureus DsbA does not have a destabilizing disulfide. A new paradigm for bacterial oxidative foldingBegoña Heras, Mareike Kurz, Russell Jarrott, et al.
Pageof 2

Showing results (11-20 of 20) with videos related to

Sort By:
Pageof 2
You have reached the last page of results.This site can display upto 20 results.
Current Topics in Medicinal Chemistry|July 26, 2012
Discovery and applications of disulfide-rich cyclic peptidesMasa Cemazar, Soohyun Kwon, Tunjung Mahatmanto, et al.
Trends in Biochemical Sciences|July 4, 2006
Protein disulfide isomerase: the structure of oxidative foldingChristian W Gruber, Masa Cemazar, Begoña Heras, et al.
Biopolymers|November 6, 2008
Biochemical and biophysical characterization of a novel plant protein disulfide isomeraseChristian W Gruber, Masa Cemazar, Adam Mechler, et al.
Structure (London, England : 1993)|June 13, 2008
The structure of a two-disulfide intermediate assists in elucidating the oxidative folding pathway of a cyclic cystine knot proteinMasa Cemazar, Ajinkya Joshi, Norelle L Daly, et al.
Protein Engineering|October 16, 2003
Vicinal disulfide turnsOliviero Carugo, Masa Cemazar, Sotir Zahariev, et al.
The Journal of Biological Chemistry|March 21, 2006
Knots in rings. The circular knotted protein Momordica cochinchinensis trypsin inhibitor-II folds via a stable two-disulfide intermediateMasa Cemazar, Norelle L Daly, Sara Häggblad, et al.
Proceedings of the National Academy of Sciences of the United States of America|May 2, 2003
Oxidative folding intermediates with nonnative disulfide bridges between adjacent cysteine residuesMasa Cemazar, Sotir Zahariev, Jakob J Lopez, et al.
Biochemistry|April 7, 2011
The role of conserved Glu residue on cyclotide stability and activity: a structural and functional study of kalata B12, a naturally occurring Glu to Asp mutantConan K L Wang, Richard J Clark, Peta J Harvey, et al.
The Journal of Biological Chemistry|May 25, 2007
A novel plant protein-disulfide isomerase involved in the oxidative folding of cystine knot defense proteinsChristian W Gruber, Masa Cemazar, Richard J Clark, et al.
The Journal of Biological Chemistry|December 14, 2007
Staphylococcus aureus DsbA does not have a destabilizing disulfide. A new paradigm for bacterial oxidative foldingBegoña Heras, Mareike Kurz, Russell Jarrott, et al.
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