|
|
|
||||
| Home Help Feedback Subscriptions Archive Search Table of Contents | |||||
This article has been cited by other articles:
![]() |
N. Bruneau, D. Lombardo, and M. Bendayan The Affinity Binding Sites of Pancreatic Bile Salt-Dependent Lipase in Pancreatic and Intestinal Tissues J. Histochem. Cytochem., February 1, 2000; 48(2): 267 - 276. [Abstract] [Full Text] |
||||
![]() |
A. Arias, C. Velez-Granell, G Mayer, and M Bendayan Colocalization of chaperone Cpn60, proinsulin and convertase PC1 within immature secretory granules of insulin-secreting cells suggests a role for Cpn60 in insulin processing J. Cell Sci., January 6, 2000; 113(11): 2075 - 2083. [Abstract] [PDF] |
||||
![]() |
J. D. Cechetto, B. J. Soltys, and R. S. Gupta Localization of Mitochondrial 60-kD Heat Shock Chaperonin Protein (Hsp60) in Pituitary Growth Hormone Secretory Granules and Pancreatic Zymogen Granules J. Histochem. Cytochem., January 1, 2000; 48(1): 45 - 56. [Abstract] [Full Text] |
||||
![]() |
I. U. Khan, R. Wallin, R. S. Gupta, and G. M. Kammer Protein kinase A-catalyzed phosphorylation of heat shock protein 60 chaperone regulates its attachment to histone 2B in the T lymphocyte plasma membrane PNAS, September 1, 1998; 95(18): 10425 - 10430. [Abstract] [Full Text] [PDF] |
||||
![]() |
N Bruneau, D Lombardo, and M Bendayan Participation of GRP94-related protein in secretion of pancreatic bile salt-dependent lipase and in its internalization by the intestinal epithelium J. Cell Sci., January 9, 1998; 111(17): 2665 - 2679. [Abstract] [PDF] |
||||
![]() |
G. Mayer and M. Bendayan Biotinyl-Tyramide: A Novel Approach for Electron Microscopic Immunocytochemistry J. Histochem. Cytochem., November 1, 1997; 45(11): 1449 - 1454. [Abstract] [Full Text] [PDF] |
||||
![]() |
N. Bruneau and D. Lombardo Chaperone Function of a Grp 94-related Protein for Folding and Transport of the Pancreatic Bile Salt-dependent Lipase J. Biol. Chem., June 2, 1995; 270(22): 13524 - 13533. [Abstract] [Full Text] [PDF] |
||||
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||