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B Easterbrook

Showing results (41-50 of 58) with videos related to

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The Journal of Biological Chemistry|May 3, 2012
Serum albumin prevents protein aggregation and amyloid formation and retains chaperone-like activity in the presence of physiological ligandsThomas E Finn, Andrea C Nunez, Margaret Sunde, et al.
Biochemistry|June 3, 1997
Histidine-rich glycoprotein binds to human IgG and C1q and inhibits the formation of insoluble immune complexesN N Gorgani, C R Parish, S B Easterbrook Smith, et al.
The Biochemical Journal|June 1, 1979
The atypical velocity response by pyruvate carboxylase to increasing concentrations of acetyl-coenzyme AS B Easterbrook-Smith, A J Campbell, D B Keech, et al.
The Journal of Biological Chemistry|March 6, 1999
Clusterin has chaperone-like activity similar to that of small heat shock proteinsD T Humphreys, J A Carver, S B Easterbrook-Smith, et al.
European Journal of Biochemistry|June 6, 2002
Suppression of apolipoprotein C-II amyloid formation by the extracellular chaperone, clusterinDanny M Hatters, Mark R Wilson, Simon B Easterbrook-Smith, et al.
Nephron|January 1, 1978
Susceptibility of human embryonic kidneys in organ culture to herpesvirus hominisJ F Crocker, J A Embil, K B Easterbrook, et al.
Biochemistry|December 22, 2000
Clusterin is an ATP-independent chaperone with very broad substrate specificity that stabilizes stressed proteins in a folding-competent stateS Poon, S B Easterbrook-Smith, M S Rybchyn, et al.
FEBS Letters|March 21, 2002
Clusterin is an extracellular chaperone that specifically interacts with slowly aggregating proteins on their off-folding pathwayStephen Poon, Teresa M Treweek, Mark R Wilson, et al.
Biochemistry|August 10, 2005
The acute phase protein haptoglobin is a mammalian extracellular chaperone with an action similar to clusterinJustin J Yerbury, Mark S Rybchyn, Simon B Easterbrook-Smith, et al.
Archives of Biochemistry and Biophysics|April 1, 1994
The effects of histidine residue modification on the immune precipitating ability of rabbit IgGR O O'Brien, P J Roeth, S A Thomson, et al.
Pageof 6

Showing results (41-50 of 58) with videos related to

Sort By:
Pageof 6
The Journal of Biological Chemistry|May 3, 2012
Serum albumin prevents protein aggregation and amyloid formation and retains chaperone-like activity in the presence of physiological ligandsThomas E Finn, Andrea C Nunez, Margaret Sunde, et al.
Biochemistry|June 3, 1997
Histidine-rich glycoprotein binds to human IgG and C1q and inhibits the formation of insoluble immune complexesN N Gorgani, C R Parish, S B Easterbrook Smith, et al.
The Biochemical Journal|June 1, 1979
The atypical velocity response by pyruvate carboxylase to increasing concentrations of acetyl-coenzyme AS B Easterbrook-Smith, A J Campbell, D B Keech, et al.
The Journal of Biological Chemistry|March 6, 1999
Clusterin has chaperone-like activity similar to that of small heat shock proteinsD T Humphreys, J A Carver, S B Easterbrook-Smith, et al.
European Journal of Biochemistry|June 6, 2002
Suppression of apolipoprotein C-II amyloid formation by the extracellular chaperone, clusterinDanny M Hatters, Mark R Wilson, Simon B Easterbrook-Smith, et al.
Nephron|January 1, 1978
Susceptibility of human embryonic kidneys in organ culture to herpesvirus hominisJ F Crocker, J A Embil, K B Easterbrook, et al.
Biochemistry|December 22, 2000
Clusterin is an ATP-independent chaperone with very broad substrate specificity that stabilizes stressed proteins in a folding-competent stateS Poon, S B Easterbrook-Smith, M S Rybchyn, et al.
FEBS Letters|March 21, 2002
Clusterin is an extracellular chaperone that specifically interacts with slowly aggregating proteins on their off-folding pathwayStephen Poon, Teresa M Treweek, Mark R Wilson, et al.
Biochemistry|August 10, 2005
The acute phase protein haptoglobin is a mammalian extracellular chaperone with an action similar to clusterinJustin J Yerbury, Mark S Rybchyn, Simon B Easterbrook-Smith, et al.
Archives of Biochemistry and Biophysics|April 1, 1994
The effects of histidine residue modification on the immune precipitating ability of rabbit IgGR O O'Brien, P J Roeth, S A Thomson, et al.
Pageof 6