acth analogues
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2013 ◽  
Vol 80 (3) ◽  
pp. 236-237 ◽  
Author(s):  
Fernando Perez-Ruiz ◽  
Ana María Herrero-Beites

Biochemistry ◽  
2009 ◽  
Vol 48 (41) ◽  
pp. 9775-9784 ◽  
Author(s):  
Yingkui Yang ◽  
Victor J. Hruby ◽  
Min Chen ◽  
Chiquito Crasto ◽  
Minying Cai ◽  
...  

Bone ◽  
1987 ◽  
Vol 8 (4) ◽  
pp. 267
Author(s):  
S.C. Corlett ◽  
A.D. Care ◽  
M. Couch ◽  
A.R. Sykes

1977 ◽  
Vol 84 (3) ◽  
pp. 470-484 ◽  
Author(s):  
Johannes W. van Nispen ◽  
Godefridus I. Tesser ◽  
Pierre L. Barthe ◽  
René Maier ◽  
Lotte Schenkel-Hulliger

ABSTRACT The steroidogenic and lipolytic activities of corticotrophin-(1-24)-tetracosapeptide and [Lys17,18]corticotrophin-(1-18)-octadecapeptide amide were compared with those of corresponding analogues substituted in position 8 with norarginine and homoarginine, and in position 9 with phenylalanine and pentamethylphenylalanine. The norarginine containing analogues demonstrated a rewarding activity, although they were generally somewhat less active than the homoarginine containing compounds. This confirms the previous conclusions concerning the indispensability of arginine as a guanidinium derivate. The analogues in which phenylalanine was a substitute for tryptophan, constituted partial agonists with a low activity in steroidogenesis and lipolysis but a rather high melanophore stimulating activity. Insertion of the permethylated derivative of phenylalanine in this position, which ensures the presence of an aminoacyl residue with the full electron donor properties of tryptophan, destroyed the low steroidogenic and lipolytic activity, but increased the MSH-activity about 2-fold.


Life Sciences ◽  
1976 ◽  
Vol 18 (10) ◽  
pp. 1099-1104 ◽  
Author(s):  
Hermine van der Helm-Hylkema ◽  
D. de Wied
Keyword(s):  

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