Vibrational spectroscopy and DFT calculations of the di-amino acid peptide l-aspartyl-l-glutamic acid in the zwitterionic state

2009 ◽  
Vol 11 (30) ◽  
pp. 6389 ◽  
Author(s):  
Nighat Kausar ◽  
Trevor J. Dines ◽  
Babur Z. Chowdhry ◽  
Bruce D. Alexander
2009 ◽  
Vol 40 (11) ◽  
pp. 1478-1497 ◽  
Author(s):  
Andrew P. Mendham ◽  
Trevor J. Dines ◽  
Martin J. Snowden ◽  
Babur Z. Chowdhry ◽  
Robert Withnall

2009 ◽  
Vol 40 (6) ◽  
pp. 661-669 ◽  
Author(s):  
Nighat Kausar ◽  
Bruce D. Alexander ◽  
Trevor J. Dines ◽  
Robert Withnall ◽  
Babur Z. Chowdhry

2009 ◽  
Vol 41 (3) ◽  
pp. 288-302 ◽  
Author(s):  
Andrew P. Mendham ◽  
Rex A. Palmer ◽  
Brian S. Potter ◽  
Trevor J. Dines ◽  
Martin J. Snowden ◽  
...  

2009 ◽  
Vol 41 (2) ◽  
pp. 148-159 ◽  
Author(s):  
Andrew P. Mendham ◽  
Brian S. Potter ◽  
Rex A. Palmer ◽  
Trevor J. Dines ◽  
John C. Mitchell ◽  
...  

2009 ◽  
Vol 40 (6) ◽  
pp. 670-678 ◽  
Author(s):  
Nighat Kausar ◽  
Bruce D. Alexander ◽  
Trevor J. Dines ◽  
Robert Withnall ◽  
Babur Z. Chowdhry

Author(s):  
Chi-Ming Wei ◽  
Margaret Hukee ◽  
Christopher G.A. McGregor ◽  
John C. Burnett

C-type natriuretic peptide (CNP) is a newly identified peptide that is structurally related to atrial (ANP) and brain natriuretic peptide (BNP). CNP exists as a 22-amino acid peptide and like ANP and BNP has a 17-amino acid ring formed by a disulfide bond. Unlike these two previously identified cardiac peptides, CNP lacks the COOH-terminal amino acid extension from the ring structure. ANP, BNP and CNP decrease cardiac preload, but unlike ANP and BNP, CNP is not natriuretic. While ANP and BNP have been localized to the heart, recent investigations have failed to detect CNP mRNA in the myocardium although small concentrations of CNP are detectable in the porcine myocardium. While originally localized to the brain, recent investigations have localized CNP to endothelial cells consistent with a paracrine role for CNP in the control of vascular tone. While CNP has been detected in cardiac tissue by radioimmunoassay, no studies have demonstrated CNP localization in normal human heart by immunoelectron microscopy.


1990 ◽  
Vol 265 (9) ◽  
pp. 5324-5328
Author(s):  
K K Arora ◽  
P Shenbagamurthi ◽  
M Fanciulli ◽  
P L Pedersen

2011 ◽  
Vol 42 (2) ◽  
pp. 230-238 ◽  
Author(s):  
Babur Z. Chowdhry ◽  
Trevor J. Dines ◽  
Stephen A. Leharne ◽  
John P. Ryall ◽  
Iqbal T. Shadi ◽  
...  

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
M. Geiger ◽  
T. Janes ◽  
H. Keshavarz ◽  
S. Summers ◽  
C. Pinger ◽  
...  

Abstract People with type 1 diabetes (T1D) require exogenous administration of insulin, which stimulates the translocation of the GLUT4 glucose transporter to cell membranes. However, most bloodstream cells contain GLUT1 and are not directly affected by insulin. Here, we report that C-peptide, the 31-amino acid peptide secreted in equal amounts with insulin in vivo, is part of a 3-component complex that affects red blood cell (RBC) membranes. Multiple techniques were used to demonstrate saturable and specific C-peptide binding to RBCs when delivered as part of a complex with albumin. Importantly, when the complex also included Zn2+, a significant increase in cell membrane GLUT1 was measured, thus providing a cellular effect similar to insulin, but on a transporter on which insulin has no effect.


1989 ◽  
Vol 165 (1) ◽  
pp. 131-137 ◽  
Author(s):  
M. Vicens ◽  
J.J. Fiol ◽  
A. Terron ◽  
V. Moreno

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