Handbook of Biologically Active PeptidesAbba Kastin, Abba J. Kastin 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. |
From inside the book
Results 1-5 of 72
Page 79
... action of MccB17 has been the subject of considerable research and is therefore probably the best understood of all microcins [12, 22, 23, 27]. The peptide targets DNA gyrase, a topoisomerase that is essential for ATP-dependent negative ...
... action of MccB17 has been the subject of considerable research and is therefore probably the best understood of all microcins [12, 22, 23, 27]. The peptide targets DNA gyrase, a topoisomerase that is essential for ATP-dependent negative ...
Page 80
... action. Biochimie. 2002;84:511–519. Destoumieux-Garzon D, Thomas X, Santamaria M, Goulard C, Barthélémy M, Boscher B, Bessin Y, Molle G, Pons AM, Letellier L, Péduzzi J, Rebuffat S. Microcin E492 antibacterial activity: Evidence for a ...
... action. Biochimie. 2002;84:511–519. Destoumieux-Garzon D, Thomas X, Santamaria M, Goulard C, Barthélémy M, Boscher B, Bessin Y, Molle G, Pons AM, Letellier L, Péduzzi J, Rebuffat S. Microcin E492 antibacterial activity: Evidence for a ...
Page 104
... action. FEMS Microbiol Rev 2001;25:285–308. Morgan SM, O'Connor PM, Cotter PD, Ross RP, Hill C. Sequential actions or the two-component peptides of the lantibiotic lacticin 3147 explain its antimicrobial activity at nanomolar ...
... action. FEMS Microbiol Rev 2001;25:285–308. Morgan SM, O'Connor PM, Cotter PD, Ross RP, Hill C. Sequential actions or the two-component peptides of the lantibiotic lacticin 3147 explain its antimicrobial activity at nanomolar ...
Page 110
... action. Many studies have observed that bacteriocins can cause efflux of potassium ions from susceptible bacteria. Such leakage will lead to the depolarization of the bacterial cytoplasmic membrane and excess ATP consumption, which in ...
... action. Many studies have observed that bacteriocins can cause efflux of potassium ions from susceptible bacteria. Such leakage will lead to the depolarization of the bacterial cytoplasmic membrane and excess ATP consumption, which in ...
Page 115
... action. Group B colicins utilize the Ton-dependent system, consisting of TonB and ExbB-ExbD (Table 2). “Ton” mutants are resistant to the phage T1—hence the name “Ton.” As can be seen from the tables, the lethal action of most colicins ...
... action. Group B colicins utilize the Ton-dependent system, consisting of TonB and ExbB-ExbD (Table 2). “Ton” mutants are resistant to the phage T1—hence the name “Ton.” As can be seen from the tables, the lethal action of most colicins ...
Contents
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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Common terms and phrases
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
Popular passages
Page 403 - WITCH. Fillet of a fenny snake, In the cauldron boil and bake; Eye of newt and toe of frog, Wool of bat and tongue of dog, Adder's fork and blind-worm's...
Page 565 - Nagasawa, T., Hirota, S., Tachibana, K., Takakura, N., Nishikawa, S., Kitamura, Y, Yoshida, N., Kikutani, H., and Kishimoto, T. (1996). Defects of B-cell lymphopoiesis and bone-marrow myelopoiesis in mice lacking the CXC chemokine PBSF/SDF-1.
Page 600 - Houghten, RA (1985) General method for the rapid solid-phase synthesis of large numbers of peptides: specificity of antigen-antibody interaction at the level of individual amino acids.
Page 505 - D. (1998) Vaccination of melanoma patients with peptide- or tumor lysate-pulsed dendritic cells. Nat. Med. 4, 328-332 (see comments).
Page 594 - AJ (1986) The epitopes of influenza nucleoprotein recognized by cytotoxic T lymphocytes can be defined with short synthetic peptides.
Page 498 - Slamon DJ, Leyland-jones B, Shak S et al. Use of chemotherapy plus a monoclonal antibody against HER2 for metastatic breast cancer that overexpresses HER2.
Page 564 - Feng, Y., Broder, CC, Kennedy, PE, and Berger, EA (1996) HIV-1 entry cofactor: functional cDNA cloning of a seven-transmembrane, G protein-coupled receptor.
Page 564 - The lymphocyte chemoattractant SDF-1- is a ligand for LESTR/fusin and blocks HIV-1 entry. Nature 1996;382: 829-833.
Page 601 - DW (1997). A combinatorial approach defines specificities of members of the caspase family and granzyme B. Functional relationships established for key mediators of apoptosis.
Page 504 - Simultaneous humoral and cellular immune response against cancer-testis antigen NY-ESO-1: definition of human histocompatibility leukocyte antigen (HLA)-A2binding peptide epitopes. J. Exp. Med..