Matches in SemOpenAlex for { <https://semopenalex.org/work/W4241620280> ?p ?o ?g. }
Showing items 1 to 56 of
56
with 100 items per page.
- W4241620280 endingPage "156" @default.
- W4241620280 startingPage "147" @default.
- W4241620280 abstract "Hemorphins are endogenous peptides belonging to the family of “nonclassical” or “atypical” opioid peptides. They are generated by enzymatic hydrolysis of the β-, κ-, δ-, or ϵ-chain of the blood protein hemoglobin. Originally, the hemorphins were isolated from enzymatically treated bovine blood. In recent years hemorphin structures have been identified as naturally occurring peptides in brain, plasma, and cerebrospinal fluid. This article will review recent studies of the hemorphins regarding their structures, mechanisms for their release, and their biological actions. A particular emphasis will be directed to their role in exercising human and their clinical relevance. © 1997 John Wiley & Sons, Inc. Biopoly 43: 147–156, 1997" @default.
- W4241620280 created "2022-05-12" @default.
- W4241620280 creator A5037716681 @default.
- W4241620280 creator A5056842744 @default.
- W4241620280 creator A5067362563 @default.
- W4241620280 date "1997-01-01" @default.
- W4241620280 modified "2023-09-26" @default.
- W4241620280 title "The hemorphins: A new class of opioid peptides derived from the blood protein hemoglobin" @default.
- W4241620280 doi "https://doi.org/10.1002/(sici)1097-0282(1997)43:2<147::aid-bip8>3.3.co;2-b" @default.
- W4241620280 hasPublicationYear "1997" @default.
- W4241620280 type Work @default.
- W4241620280 citedByCount "0" @default.
- W4241620280 crossrefType "journal-article" @default.
- W4241620280 hasAuthorship W4241620280A5037716681 @default.
- W4241620280 hasAuthorship W4241620280A5056842744 @default.
- W4241620280 hasAuthorship W4241620280A5067362563 @default.
- W4241620280 hasConcept C170493617 @default.
- W4241620280 hasConcept C185592680 @default.
- W4241620280 hasConcept C2778917026 @default.
- W4241620280 hasConcept C2779281246 @default.
- W4241620280 hasConcept C2781063702 @default.
- W4241620280 hasConcept C3020437955 @default.
- W4241620280 hasConcept C42407357 @default.
- W4241620280 hasConcept C55493867 @default.
- W4241620280 hasConcept C71924100 @default.
- W4241620280 hasConcept C88016717 @default.
- W4241620280 hasConceptScore W4241620280C170493617 @default.
- W4241620280 hasConceptScore W4241620280C185592680 @default.
- W4241620280 hasConceptScore W4241620280C2778917026 @default.
- W4241620280 hasConceptScore W4241620280C2779281246 @default.
- W4241620280 hasConceptScore W4241620280C2781063702 @default.
- W4241620280 hasConceptScore W4241620280C3020437955 @default.
- W4241620280 hasConceptScore W4241620280C42407357 @default.
- W4241620280 hasConceptScore W4241620280C55493867 @default.
- W4241620280 hasConceptScore W4241620280C71924100 @default.
- W4241620280 hasConceptScore W4241620280C88016717 @default.
- W4241620280 hasIssue "2" @default.
- W4241620280 hasLocation W42416202801 @default.
- W4241620280 hasOpenAccess W4241620280 @default.
- W4241620280 hasPrimaryLocation W42416202801 @default.
- W4241620280 hasRelatedWork W104662695 @default.
- W4241620280 hasRelatedWork W1988425404 @default.
- W4241620280 hasRelatedWork W1991546010 @default.
- W4241620280 hasRelatedWork W1993573421 @default.
- W4241620280 hasRelatedWork W2092779526 @default.
- W4241620280 hasRelatedWork W2132633660 @default.
- W4241620280 hasRelatedWork W2153468986 @default.
- W4241620280 hasRelatedWork W2371445650 @default.
- W4241620280 hasRelatedWork W2392536574 @default.
- W4241620280 hasRelatedWork W2411060740 @default.
- W4241620280 hasVolume "43" @default.
- W4241620280 isParatext "false" @default.
- W4241620280 isRetracted "false" @default.
- W4241620280 workType "article" @default.