scholarly journals Comprehensive characterization of the site-specific N-glycosylation of wild-type and recombinant human lactoferrin expressed in the milk of transgenic cloned cattle

Glycobiology ◽  
2010 ◽  
Vol 21 (2) ◽  
pp. 206-224 ◽  
Author(s):  
Tian Yu ◽  
Chengdong Guo ◽  
Jianwu Wang ◽  
Piliang Hao ◽  
Shunchao Sui ◽  
...  
1990 ◽  
Vol 10 (1) ◽  
pp. 235-242
Author(s):  
L Meyer-Leon ◽  
R B Inman ◽  
M M Cox

Holliday structures are formed in the course of FLP protein-promoted site-specific recombination. Here, we demonstrate that Holliday structures are formed in reactions involving wild-type substrates and that they are kinetically competent with respect to the overall reaction rate. Together with a previous demonstration of chemical competence (L. Meyer-Leon, L.-C. Huang, S. W. Umlauf, M. M. Cox, and R. B. Inman, Mol. Cell. Biol. 8:3784-3796, 1988), Holliday structures therefore meet all criteria necessary to establish that they are obligate reaction intermediates in FLP-mediated site-specific recombination. In addition, kinetic evidence suggests that two distinct forms of the Holliday intermediate are present in the reaction pathway, interconverted in an isomerization process that is rate limiting at 0 degree C.


PLoS ONE ◽  
2017 ◽  
Vol 12 (2) ◽  
pp. e0171477 ◽  
Author(s):  
Annabelle Le Parc ◽  
Sercan Karav ◽  
Camille Rouquié ◽  
Elizabeth A. Maga ◽  
Apichaya Bunyatratchata ◽  
...  

1997 ◽  
Vol 272 (13) ◽  
pp. 8802-8807 ◽  
Author(s):  
Jan H. Nuijens ◽  
Patrick H. C. van Berkel ◽  
Marlieke E. J. Geerts ◽  
Peter Paul Hartevelt ◽  
Herman A. de Boer ◽  
...  

2017 ◽  
Vol 38 (7) ◽  
pp. 849-862
Author(s):  
Susanna Lualdi ◽  
Genny Del Zotto ◽  
Olga Zegarra-Moran ◽  
Nicoletta Pedemonte ◽  
Fabio Corsolini ◽  
...  

1990 ◽  
Vol 10 (1) ◽  
pp. 235-242 ◽  
Author(s):  
L Meyer-Leon ◽  
R B Inman ◽  
M M Cox

Holliday structures are formed in the course of FLP protein-promoted site-specific recombination. Here, we demonstrate that Holliday structures are formed in reactions involving wild-type substrates and that they are kinetically competent with respect to the overall reaction rate. Together with a previous demonstration of chemical competence (L. Meyer-Leon, L.-C. Huang, S. W. Umlauf, M. M. Cox, and R. B. Inman, Mol. Cell. Biol. 8:3784-3796, 1988), Holliday structures therefore meet all criteria necessary to establish that they are obligate reaction intermediates in FLP-mediated site-specific recombination. In addition, kinetic evidence suggests that two distinct forms of the Holliday intermediate are present in the reaction pathway, interconverted in an isomerization process that is rate limiting at 0 degree C.


2005 ◽  
Vol 55 (2) ◽  
pp. 213-222 ◽  
Author(s):  
Diah Rachmawati ◽  
Takuya Mori ◽  
Takehiko Hosaka ◽  
Fumio Takaiwa ◽  
Eiichi Inoue ◽  
...  

2019 ◽  
Vol 21 (Supplement_6) ◽  
pp. vi42-vi42
Author(s):  
Elizabeth Fernandez ◽  
Wilson Mai ◽  
Nicholas Bayley ◽  
Linda Liau ◽  
Timothy Cloughesy ◽  
...  

Abstract Conventional therapies (e.g., temozolomide (TMZ), Irradiation (IR)) transiently halt tumor growth of glioblastoma (GBM) but fail to induce cell death through apoptosis. Consequently, the inability to kill GBM tumor cells ultimately leads to disease progression and a poor patient survival. The precise molecular mechanisms by which GBM are refractory to apoptosis remain enigmatic. We preformed BH3 profiling to functionally characterize the intrinsic apoptotic machinery and define the molecular ‘blocks’ that obstruct GBM apoptosis under both basal and treatment states. Using a molecularly diverse panel of freshly purified patient tumors, patient-derived neurospheres and patient-derived orthotopic xenografts, we identified that nearly all GBMs have two anti-apoptotic blocks, BCL-xL and MCL-1, which are essential for GBM survival in an untreated state. TMZ or IR (TMZ/IR) disabled the MCL-1 block in a subset of GBMs, leaving tumors exclusively dependent on BCL-xL for survival. Mechanistic studies revealed that TMZ/IR treatment induced p53-dependent expression of the pro-apoptotic protein, PUMA, which subsequently bound to and neutralized MCL-1. Consequently, pharmacological inhibition of BCL-xL in combination with TMZ/IR initiated intrinsic apoptosis and was synergistically lethal in p53 wild-type GBM. These studies identify the existence of two anti-apoptotic proteins that are critical for GBM survival, which can be therapeutically exploited in a molecularly defined subset of GBMs for tumor eradication.


2019 ◽  
Vol 83 (5) ◽  
pp. 851-859 ◽  
Author(s):  
Xiaonan Pang ◽  
Yuxi Tong ◽  
Wenzhi Xue ◽  
Yi-feng Yang ◽  
Xiwen Chen ◽  
...  

Molecules ◽  
2020 ◽  
Vol 25 (20) ◽  
pp. 4655
Author(s):  
Katarina Molnarova ◽  
Petr Kozlík

Protein glycosylation analysis is challenging due to the structural variety of complex conjugates. However, chromatographically separating glycans attached to tryptic peptides enables their site-specific characterization. For this purpose, we have shown the importance of selecting a suitable hydrophilic interaction liquid chromatography (HILIC) stationary phase in the separation of glycopeptides and their isomers. Three different HILIC stationary phases, i.e., HALO® penta-HILIC, Glycan ethylene bridged hybrid (BEH) Amide, and ZIC-HILIC, were compared in the separation of complex N-glycopeptides of hemopexin and Immunoglobulin G glycoproteins. The retention time increased with the polarity of the glycans attached to the same peptide backbone in all HILIC columns tested in this study, except for the ZIC-HILIC column when adding sialic acid to the glycan moiety, which caused electrostatic repulsion with the negatively charged sulfobetaine functional group, thereby decreasing retention. The HALO® penta-HILIC column provided the best separation results, and the ZIC-HILIC column the worst. Moreover, we showed the potential of these HILIC columns for the isomeric separation of fucosylated and sialylated glycoforms. Therefore, HILIC is a useful tool for the comprehensive characterization of glycoproteins and their isomers.


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