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Peptide

About: Peptide is a research topic. Over the lifetime, 48651 publications have been published within this topic receiving 1582942 citations.


Papers
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Journal ArticleDOI
04 Apr 2002-Nature
TL;DR: It is reported that natural oligomers of human Aβ are formed soon after generation of the peptide within specific intracellular vesicles and are subsequently secreted from the cell, indicating that synaptotoxic Aβ oligomers can be targeted therapeutically.
Abstract: Although extensive data support a central pathogenic role for amyloid β protein (Aβ) in Alzheimer's disease1, the amyloid hypothesis remains controversial, in part because a specific neurotoxic species of Aβ and the nature of its effects on synaptic function have not been defined in vivo. Here we report that natural oligomers of human Aβ are formed soon after generation of the peptide within specific intracellular vesicles and are subsequently secreted from the cell. Cerebral microinjection of cell medium containing these oligomers and abundant Aβ monomers but no amyloid fibrils markedly inhibited hippocampal long-term potentiation (LTP) in rats in vivo. Immunodepletion from the medium of all Aβ species completely abrogated this effect. Pretreatment of the medium with insulin-degrading enzyme, which degrades Aβ monomers but not oligomers, did not prevent the inhibition of LTP. Therefore, Aβ oligomers, in the absence of monomers and amyloid fibrils, disrupted synaptic plasticity in vivo at concentrations found in human brain and cerebrospinal fluid. Finally, treatment of cells with γ-secretase inhibitors prevented oligomer formation at doses that allowed appreciable monomer production, and such medium no longer disrupted LTP, indicating that synaptotoxic Aβ oligomers can be targeted therapeutically.

4,315 citations

Journal ArticleDOI
TL;DR: The main actions of GLP-1 are to stimulate insulin secretion and to inhibit glucagon secretion, thereby contributing to limit postprandial glucose excursions and acts as an enterogastrone and part of the "ileal brake" mechanism.
Abstract: Glucagon-like peptide 1 (GLP-1) is a 30-amino acid peptide hormone produced in the intestinal epithelial endocrine L-cells by differential processing of proglucagon, the gene which is expressed in ...

2,657 citations

Journal ArticleDOI
30 Apr 1992-Nature
TL;DR: Purification and cloning of the complementary DNA indicates that IL-lβ-converting enzyme is composed of two nonidentical subunits that are derived from a single proenzyme, possibly by autoproteolysis.
Abstract: Interleukin-1 beta (IL-1 beta)-converting enzyme cleaves the IL-1 beta precursor to mature IL-1 beta, an important mediator of inflammation. The identification of the enzyme as a unique cysteine protease and the design of potent peptide aldehyde inhibitors are described. Purification and cloning of the complementary DNA indicates that IL-1 beta-converting enzyme is composed of two nonidentical subunits that are derived from a single proenzyme, possibly by autoproteolysis. Selective inhibition of the enzyme in human blood monocytes blocks production of mature IL-1 beta, indicating that it is a potential therapeutic target.

2,593 citations

Journal ArticleDOI
TL;DR: The main determinants required for Tat translocation within this sequence are delineated by synthesizing several peptides covering the Tat domain from residues 37 to 60 and the domain extending from amino acid 37 to 47, which corresponds to the α-helix structure, is not required for cellular uptake and for nuclear translocation.

2,459 citations

Journal ArticleDOI
15 Apr 1982-Nature
TL;DR: It is found that the peptide isolated from brain extracts of a peptide amide that was thought to be PYY is a previously uncharacterized peptide, which is designated neuropeptide Y (NPY), which is structurally and biologically similar to vasoactive intestinal peptide (VIP) while PYY shows similarities to pancreatic polypeptides (PP).
Abstract: The C-terminal α-amide structure is a characteristic feature of many biologically active peptides1,2 Using a novel chemical method for the detection of peptide amides3, we have isolated two naturally occurring peptides, peptide HI (PHI) and peptide YY (PYY), from extracts of porcine intestine and have shown that these peptide amides represent previously unknown biologically active peptides4 PHI is structurally and biologically similar to vasoactive intestinal peptide (VIP)5 while PYY shows similarities to pancreatic polypeptide (PP)6 Preliminary studies indicated that PHI and PYY may both be present in brain as well as in intestine4 We report here the isolation from brain extracts of a peptide amide that was thought to be PYY However, we found that the peptide, while having distinct structural and biological similarities to both PYY and PP, is a previously uncharacterized peptide, which we designate neuropeptide Y (NPY)

2,264 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
20232,737
20224,499
20211,117
20201,430
20191,315
20181,329