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Sökning: WFRF:(Ridderstrom M)

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  • Nagi, Saad, et al. (författare)
  • An ultrafast system for signaling mechanical pain in human skin
  • 2019
  • Ingår i: Science Advances. - : American Association for the Advancement of Science (AAAS). - 2375-2548. ; 5:7
  • Tidskriftsartikel (refereegranskat)abstract
    • The canonical view is that touch is signaled by fast-conducting, thickly myelinated afferents, whereas pain is signaled by slow-conducting, thinly myelinated ("fast" pain) or unmyelinated ("slow" pain) afferents. While other mammals have thickly myelinated afferents signaling pain (ultrafast nociceptors), these have not been demonstrated in humans. Here, we performed single-unit axonal recordings (microneurography) from cutaneous mechanoreceptive afferents in healthy participants. We identified A-fiber high-threshold mechanoreceptors (A-HTMR5) that were insensitive to gentle touch, encoded noxious skin indentations, and displayed conduction velocities similar to A-fiber low-threshold mechanoreceptors. Intraneural electrical stimulation of single ultrafast A-HTMRs evoked painful percepts. Testing in patients with selective deafferentation revealed impaired pain judgments to graded mechanical stimuli only when thickly myelinated fibers were absent. This function was preserved in patients with a loss-of-function mutation in mechanotransduction channel PIEZO2.These findings demonstrate that human mechanical pain does not require PIEZO2 and can be signaled by fast-conducting, thickly myelinated afferents.
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  • Mannervik, B, et al. (författare)
  • An evolutionary approach to the design of glutathione-linked enzymes
  • 1998
  • Ingår i: CHEMICO-BIOLOGICAL INTERACTIONS. - : ELSEVIER SCI IRELAND LTD. - 0009-2797. ; 112, s. 15-21
  • Tidskriftsartikel (övrigt vetenskapligt/konstnärligt)abstract
    • Studies of protein structure provide information about principles of protein design that have come into play in natural evolution. This information can be exploited in the redesign of enzymes for novel functions. The glutathione-binding domain of glutathi
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  • Cameron, AD, et al. (författare)
  • Crystal structure of human glyoxalase .1. Evidence for gene duplication and 3D domain swapping
  • 1997
  • Ingår i: EMBO JOURNAL. - : OXFORD UNIV PRESS. - 0261-4189. ; 16:12, s. 3386-3395
  • Tidskriftsartikel (övrigt vetenskapligt/konstnärligt)abstract
    • The zinc metalloenzyme glyoxalase I catalyses the glutathione-dependent inactivation of toxic methylglyoxal. The structure of the dimeric human enzyme in complex with S-benzyl-glutathione has been determined by multiple isomorphous replacement (MIR) and r
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  • Cameron, AD, et al. (författare)
  • Crystal structure of human glyoxalase II and its complex with a glutathione thiolester substrate analogue
  • 1999
  • Ingår i: STRUCTURE WITH FOLDING & DESIGN. - : CURRENT BIOLOGY LTD. - 0969-2126. ; 7:9, s. 1067-1078
  • Tidskriftsartikel (övrigt vetenskapligt/konstnärligt)abstract
    • Background: Glyoxalase II, the second of two enzymes in the glyoxalase system, is a thiolesterase that catalyses the hydrolysis of S-D-lactoylgtutathione to form glutathione and D-lactic acid. Results: The structure of human glyoxalase II was solved initi
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  • Resultat 1-10 av 15

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