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of 27
pro vyhledávání: '"K N, PARAMESWARAN"'
Autor:
K. N. Parameswaran Nampoothiri, Laurent Abel, Sheela Nampoothiri, Surjit Singh, Jean-Laurent Casanova, Stéphanie Boisson-Dupuis
Publikováno v:
The Indian Journal of Pediatrics. 80:505-508
Multifocal Tuberculous (TB) osteomyelitis is an extremely rare entity in immunocompetent individuals. The authors report a 19-mo-old girl with multifocal TB osteomyelitis which resolved completely following institution of four drug antituberculous tr
Autor:
Pauline T. Velasco, Laszlo Lorand, K. N. Parameswaran, Ellen C. Chen, Xiang-Fei Cheng, James H. Wilson
Publikováno v:
Journal of Biological Chemistry. 272:10311-10317
Nepsilon-(gamma-glutamyl)lysine cross-links, connecting various peptide chain segments, are frequently the major products in transglutaminase-catalyzed reactions. We have now investigated the effectiveness of these enzymes for hydrolyzing the gamma:e
Autor:
Mary Ann Greco, Joseph C. Kvedar, K. N. Parameswaran, William S. Lane, Laszlo Lorand, Howard P. Baden
Publikováno v:
Journal of Investigative Dermatology. 104:204-210
In this report, the pancornulins are identified as members of the spr (small, proline-rich) multigene family by amino acid sequence and mass spectrometry analyses. One of the pancornulins (14.9 kDa) is identical to the protein predicted by spr-1 clon
Publikováno v:
Bioconjugate Chemistry. 3:37-41
Biotinylated peptides Biot-Gln-Gln-Ile-Val and Biot-epsilon-Aca-Gln-Gln-Ile-Val were shown to act as acceptor substrates for amines in reactions catalyzed by both tissue transglutaminase and coagulation factor XIIIa. Moreover, the peptides could be e
Autor:
K. N. Parameswaran
Publikováno v:
Organic Preparations and Procedures International. 22:119-121
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 95(2)
The E domain of fibrinogen represents the central region of the protein that, after the removal of fibrinopeptides from the N-termini of its α chains by thrombin, orders the noncovalent assembly of fibrin units into a half-staggered array. This stru
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The transglutaminase (protein-glutamine: amine gamma-glutamyltransferase, EC 2.3.2.13)-catalyzed cross-linking of proteins in biological systems can often be inhibited by inclusion of small primary amines or glutamine-containing peptides, which act a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aeab26bdbb45c6330208da050fc91101
https://europepmc.org/articles/PMC50509/
https://europepmc.org/articles/PMC50509/
Publikováno v:
Biochemical and biophysical research communications. 186(1)
The transglutaminase-catalyzed incorporation of the fluorescent amine, dansylcadaverine, into casein derivatives, such as N,N-dimethylcasein, is accompanied by a large increase in intensity of emission (Lorand et al., Anal. Biochem. 44, 221-231, 1971
Peptides patterned on the N-terminal sequence of fibronectin were synthesized and tested for amine acceptor qualities in reactions with dansylcadaverine catalyzed either by coagulation factor XIIIa or intracellular transglutaminase (protein-glutamine
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::976a4e5e7af9ea44b5bff474b1c5b4bd
https://europepmc.org/articles/PMC54978/
https://europepmc.org/articles/PMC54978/