scholarly journals The Role of Basic Amino Acid Surface Clusters on the Collagenase Activity of Cathepsin K

Biochemistry ◽  
2013 ◽  
Vol 52 (44) ◽  
pp. 7742-7752 ◽  
Author(s):  
Ferez S. Nallaseth ◽  
Fabien Lecaille ◽  
Zhenqiang Li ◽  
Dieter Brömme
Keyword(s):  
Amino Acid ◽  
Cathepsin K ◽  
Basic Amino Acid ◽  
Collagenase Activity

scholarly journals Role of peptide substrate structure in the selective processing of peptide prohormones at basic amino acid pairs by endoproteases

FEBS Letters ◽  
1988 ◽  
Vol 234 (1) ◽  
pp. 149-152 ◽  
Author(s):  
Pablo Gluschankof ◽  
Sophie Gomez ◽  
Agnès Lepage ◽  
Christophe Créminon ◽  
Fred Nyberg ◽  
...  
Keyword(s):  
Amino Acid ◽  
Basic Amino Acid ◽  
Peptide Substrate ◽  
Substrate Structure ◽  
Selective Processing

scholarly journals TRH-Like Peptides

2011 ◽  
pp. 207-215 ◽  
Author(s):  
R. BÍLEK ◽  
M. BIČÍKOVÁ ◽  
L. ŠAFAŘÍK
Keyword(s):  
Amino Acid ◽  
Biological Function ◽  
Basic Amino Acid ◽  
Thyroid Status ◽  
Peripheral Tissues ◽  
Amino Acid Histidine ◽  
Neural Tissues ◽  
Proliferative Ability ◽  
Endocrine Tissues

TRH-like peptides are characterized by substitution of basic amino acid histidine (related to authentic TRH) with neutral or acidic amino acid, like glutamic acid, phenylalanine, glutamine, tyrosine, leucin, valin, aspartic acid and asparagine. The presence of extrahypothalamic TRH-like peptides was reported in peripheral tissues including gastrointestinal tract, placenta, neural tissues, male reproductive system and certain endocrine tissues. Work deals with the biological function of TRH-like peptides in different parts of organisms where various mechanisms may serve for realisation of biological function of TRH-like peptides as negative feedback to the pituitary exerted by the TRH-like peptides, the role of pEEPam such as fertilization-promoting peptide, the mechanism influencing the proliferative ability of prostatic tissues, the neuroprotective and antidepressant function of TRH-like peptides in brain and the regulation of thyroid status by TRH-like peptides.

Fiber Formation from Solutions of Collagen. IV. On the Role of the Basic Amino Acid Residues*

Biochemistry ◽  
1962 ◽  
Vol 1 (2) ◽  
pp. 215-223 ◽  
Author(s):  
Howard B. Bensusan ◽  
Virgil R. Mumaw ◽  
Ann W. Scanu
Keyword(s):  
Amino Acid ◽  
Basic Amino Acid ◽  
Collagen Iv ◽  
Fiber Formation ◽  
Amino Acid Residues

Degradation of Double-Stranded RNA by Human Pancreatic Ribonuclease:  Crucial Role of Noncatalytic Basic Amino Acid Residues†

Biochemistry ◽  
2003 ◽  
Vol 42 (34) ◽  
pp. 10182-10190 ◽  
Author(s):  
Salvatore Sorrentino ◽  
Mariarosaria Naddeo ◽  
Aniello Russo ◽  
Giuseppe D'Alessio
Keyword(s):  
Amino Acid ◽  
Crucial Role ◽  
Basic Amino Acid ◽  
Amino Acid Residues ◽  
Double Stranded Rna ◽  
Pancreatic Ribonuclease ◽  
Human Pancreatic Ribonuclease

scholarly journals Structural Model of MD-2 and Functional Role of Its Basic Amino Acid Clusters Involved in Cellular Lipopolysaccharide Recognition

2004 ◽  
Vol 279 (27) ◽  
pp. 28475-28482 ◽  
Author(s):  
Anton Gruber ◽  
Mateja Manček ◽  
Hermann Wagner ◽  
Carsten J. Kirschning ◽  
Roman Jerala
Keyword(s):  
Amino Acid ◽  
Functional Role ◽  
Structural Model ◽  
Basic Amino Acid

Proteases and posttranslational processing of prohormones: a review

1983 ◽  
Vol 61 (7) ◽  
pp. 501-515 ◽  
Author(s):  
Claude Lazure ◽  
Nabil G. Seidah ◽  
Didier Pélaprat ◽  
Michel Chrétien
Keyword(s):  
Amino Acid ◽  
Current Knowledge ◽  
Secretory Granules ◽  
Basic Amino Acid ◽  
Biologically Active ◽  
Maturation Process ◽  
Active Peptides ◽  
Biologically Active Peptides ◽  
Precursor Molecules

Pioneering work on insulin and on lipotropin, published in 1967, led to the formulation of the hypothesis that biologically active peptides such as peptide hormones are derived from larger precursor molecules by enzymatic cleavage at basic amino acid pairs. Since then, an ever-increasing number of hormones and active peptides including neuropeptides have been found to be contained within the sequence of a larger precursor protein and are released by limited proteolytic cleavage. The hypothesis concerning the posttranslational maturation of precursor molecules into smaller active entities is now firmly established in many tissues (e.g., pituitary gland, pancreas) and for all kinds of organisms (e.g. mammals, fish), though the nature of the enzyme(s) responsible for this maturation process still remains unknown. This article presents current knowledge of the intracellular processing of precursor molecules, especially the conversion of prohormone to hormone. The discussion deals principally with the evidences concerning the localization of the maturation process mainly in the secretory granules, the role of basic amino acid pairs at the cleavage site, and the possible involvement of serine and (or) thiol endopeptidases in that process.

scholarly journals Role of the basic amino acid cluster and Glu-23 in pyrimidine dimer glycosylase activity of T4 endonuclease V.

1992 ◽  
Vol 89 (20) ◽  
pp. 9420-9424 ◽  
Author(s):  
T. Doi ◽  
A. Recktenwald ◽  
Y. Karaki ◽  
M. Kikuchi ◽  
K. Morikawa ◽  
...  
Keyword(s):  
Amino Acid ◽  
Basic Amino Acid ◽  
Pyrimidine Dimer ◽  
Endonuclease V ◽  
Amino Acid Cluster
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