Handbook of Biologically Active PeptidesAbba Kastin, Abba J. Kastin Elsevier, 2011-04-28 - 1640 psl. Peptides play a crucial role in many physiological processes including actions as neurotransmitters, hormones, and antibiotics. Research has shown their importance in such fields as neuroscience, immunology, pharmacology, and cell biology. The Handbook of Biologically Active Peptides presents, for the first time, this tremendous body of knowledge in the field of biologically active peptides in one single reference. The section editors and contributors represent some of the most sophisticated and distinguished scientists working in basic sciences and clinical medicine. The Handbook of Biologically Active Peptides is a definitive, all-encompassing reference that will be indispensable for individuals ranging from peptide researchers, to biochemists, cell and molecular biologists, neuroscientists, pharmacologists, and to endocrinologists. Chapters are designed to be a source for workers in the field and will enable researchers working in a specific area to examine other related areas with which they would not ordinarily be familiar. *Chapters are designed to be a source for workers in the field and will enable researchers working in a specific area to examine other related areas that they would not ordinarily be familiar.*Fascinating relationships described in the book include the presence of some peptides originally found in frog skin that persist in the human human and brain where they can affect food intake and obesity. |
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... demonstrated that the activation-tagging T-DNA was inserted 1482 base pairs (bp) downstream of the stop codon of the gene At5g16020 with the enhancer elements toward the gene At5g16020 [20]. There are three annotated genes close to the ...
... demonstrated that the activation-tagging T-DNA was inserted 1482 base pairs (bp) downstream of the stop codon of the gene At5g16020 with the enhancer elements toward the gene At5g16020 [20]. There are three annotated genes close to the ...
111 psl.
... demonstrated convincingly that the pediocin-like bacteriocins consist of two domains that are separated by a flexible hinge [12, 16, 40]. Studies of hybrid pediocin-like bacteriocins have shown that the positively charged (and most ...
... demonstrated convincingly that the pediocin-like bacteriocins consist of two domains that are separated by a flexible hinge [12, 16, 40]. Studies of hybrid pediocin-like bacteriocins have shown that the positively charged (and most ...
127 psl.
... demonstrate antifungal activity [24]. Grenier et al. [9] have demonstrated that some fungi express β-1,3-glucanases similar to thaumatin-like proteins. Some angiosperms produce glucanases or glucanaselike proteins with antifungal ...
... demonstrate antifungal activity [24]. Grenier et al. [9] have demonstrated that some fungi express β-1,3-glucanases similar to thaumatin-like proteins. Some angiosperms produce glucanases or glucanaselike proteins with antifungal ...
146 psl.
... demonstrate a molecular mass of 30kDa and 19 kDa, respectively, well within the range of molecular masses shown by ... demonstrated by the quadruplet of RIPs from F. velutipes fruiting bodies. The production of calcaelin by the ...
... demonstrate a molecular mass of 30kDa and 19 kDa, respectively, well within the range of molecular masses shown by ... demonstrated by the quadruplet of RIPs from F. velutipes fruiting bodies. The production of calcaelin by the ...
166 psl.
... demonstrated using the ETH promoter to drive expression of EGFP in transgenic flies. A nucleotide sequence encoding the following fusion protein was constructed: the ETH gene upstream promoter region (∼300 bp), the ORF encoding part of ...
... demonstrated using the ETH promoter to drive expression of EGFP in transgenic flies. A nucleotide sequence encoding the following fusion protein was constructed: the ETH gene upstream promoter region (∼300 bp), the ORF encoding part of ...
Turinys
1 | |
55 | |
125 | |
157 | |
261 | |
Venom Peptides Section | 339 |
CancerAnticancer Peptides Section | 421 |
Vaccine Peptides Section | 491 |
Gastrointestinal Peptides Section | 999 |
Cardiovascular Peptides Section | 1163 |
Renal Peptides Section | 1227 |
Respiratory Peptides Section | 1283 |
Opioid Peptides Section | 1313 |
Neurotrophic Peptides Section | 1379 |
BloodBrain Barrier Peptides Section | 1415 |
Other Peptide Topics | 1481 |
Immunological and Inflammatory Peptides Section | 547 |
Brain Peptides Section | 621 |
Endocrine Peptides Section | 829 |
Ingestive Peptides Section | 889 |
Index | 1565 |
Color Plates | 1597 |
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Pagrindiniai terminai ir frazės
Acad action activity addition amino acids amphibian analogs analysis antagonists antibodies antigen antimicrobial binding Biochem Biol Biologically Active brain breast C-terminal cancer cause cDNA cells channels characterized Chem cloned common complex conserved contain demonstrated derived determined disease disulfide domain effects encoding epitopes expression factor frog function gene growth hormone human identified immune important increase indicate induced inhibition insect interaction involved isolated known levels ligands lines major mechanism mediated membrane mice molecular molecules mRNA multiple muscle Nature neurons neuropeptide novel observed organs patients peptide plants position potential precursor present processing produced protein recently receptor region regulation release residues response role secretion selective sequence showed shown signal similar skin specific stimulate structure studies suggesting surface synthetic Table tion tissues toxins treatment tumor University vaccine various venom
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