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M Trexler

Showing results (1-10 of 31) with videos related to

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Biochimica Et Biophysica Acta|June 28, 1984
Residues Cys-1 and Cys-79 are not essential for refolding of reduced-denatured kringle 4 fragment of human plasminogenM Trexler, L Patthy
Proceedings of the National Academy of Sciences of the United States of America|May 1, 1983
Folding autonomy of the kringle 4 fragment of human plasminogenM Trexler, L Patthy
Proceedings of the National Academy of Sciences of the United States of America|March 29, 2001
A human protein containing multiple types of protease-inhibitory modulesM Trexler, L Bányai, L Patthy
European Journal of Biochemistry|September 6, 2000
The LCCL moduleM Trexler, L Bányai, L Patthy
The Journal of Biological Chemistry|March 30, 2001
Localization of disulfide bonds in the frizzled module of Ror1 receptor tyrosine kinaseE Roszmusz, A Patthy, M Trexler, et al.
Biotechnology Progress|June 8, 2002
Bioreactor production of human alpha(1)-antitrypsin using metabolically regulated plant cell culturesMelody M Trexler, Karen A McDonald, Alan P Jackman
Biotechnology Progress|April 2, 2005
A cyclical semicontinuous process for production of human alpha 1-antitrypsin using metabolically induced plant cell suspension culturesMelody M Trexler, Karen A McDonald, Alan P Jackman
FEBS Letters|June 4, 1984
Kringles: modules specialized for protein binding. Homology of the gelatin-binding region of fibronectin with the kringle structures of proteasesL Patthy, M Trexler, Z Váli, et al.
Annals of Surgery|November 1, 1984
Total parenteral nutrition in pancreatic diseaseJ P Grant, S James, V Grabowski, et al.
Protein Science : a Publication of the Protein Society|September 22, 2001
Origin of fibronectin type II (FN2) modules: structural analyses of distantly-related members of the kringle family idey the kringle domain of neurotrypsin as a potential link between FN2 domains and kringlesO A Ozhogina, M Trexler, L Bányai, et al.
Pageof 4

Showing results (1-10 of 31) with videos related to

Sort By:
Pageof 4
Biochimica Et Biophysica Acta|June 28, 1984
Residues Cys-1 and Cys-79 are not essential for refolding of reduced-denatured kringle 4 fragment of human plasminogenM Trexler, L Patthy
Proceedings of the National Academy of Sciences of the United States of America|May 1, 1983
Folding autonomy of the kringle 4 fragment of human plasminogenM Trexler, L Patthy
Proceedings of the National Academy of Sciences of the United States of America|March 29, 2001
A human protein containing multiple types of protease-inhibitory modulesM Trexler, L Bányai, L Patthy
European Journal of Biochemistry|September 6, 2000
The LCCL moduleM Trexler, L Bányai, L Patthy
The Journal of Biological Chemistry|March 30, 2001
Localization of disulfide bonds in the frizzled module of Ror1 receptor tyrosine kinaseE Roszmusz, A Patthy, M Trexler, et al.
Biotechnology Progress|June 8, 2002
Bioreactor production of human alpha(1)-antitrypsin using metabolically regulated plant cell culturesMelody M Trexler, Karen A McDonald, Alan P Jackman
Biotechnology Progress|April 2, 2005
A cyclical semicontinuous process for production of human alpha 1-antitrypsin using metabolically induced plant cell suspension culturesMelody M Trexler, Karen A McDonald, Alan P Jackman
FEBS Letters|June 4, 1984
Kringles: modules specialized for protein binding. Homology of the gelatin-binding region of fibronectin with the kringle structures of proteasesL Patthy, M Trexler, Z Váli, et al.
Annals of Surgery|November 1, 1984
Total parenteral nutrition in pancreatic diseaseJ P Grant, S James, V Grabowski, et al.
Protein Science : a Publication of the Protein Society|September 22, 2001
Origin of fibronectin type II (FN2) modules: structural analyses of distantly-related members of the kringle family idey the kringle domain of neurotrypsin as a potential link between FN2 domains and kringlesO A Ozhogina, M Trexler, L Bányai, et al.
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