Zobrazeno 1 - 10
of 25
pro vyhledávání: '"Jonathan D. Lowenson"'
Autor:
Rebeccah A. Warmack, Eric Z. Pang, Esther Peluso, Jonathan D. Lowenson, Joseph Y. Ong, Jorge Z. Torres, Steven G. Clarke
Publikováno v:
Biochemistry
The spontaneous L-isoaspartate protein modification has been observed to negatively affect protein function. However, this modification can be reversed in many proteins in reactions initiated by the protein-L-isoaspartyl (D-aspartyl) O-methyltransfer
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5cb4d40718752685f8d461498a77a9a2
https://doi.org/10.1021/acs.biochem.2c00130
https://doi.org/10.1021/acs.biochem.2c00130
Publikováno v:
PLoS ONE, Vol 7, Iss 10, p e46719 (2012)
L-isoaspartyl (D-aspartyl) O-methyltransferase deficient mice (Pcmt1(-/-)) accumulate isomerized aspartyl residues in intracellular proteins until their death due to seizures at approximately 45 days. Previous studies have shown that these mice have
Externí odkaz:
https://doaj.org/article/4e7b3c28318d4105a4284ff5380ca8b0
Publikováno v:
Journal of Proteome Research. 12:4566-4576
Protein l-isoaspartyl methyltransferase (PIMT) repairs the isoaspartyl residues (isoAsp) that originate from asparagine deamidation and aspartic acid (Asp) isomerization to Asp residues. Deletion of the gene encoding PIMT in mice (Pcmt1) leads to iso
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9e065df53c2499d89ff565a09a24690f
https://doi.org/10.1021/pr400688r
https://doi.org/10.1021/pr400688r
Autor:
Tingsu Chen, Steven Clarke, Eckhard Jankowsky, Nihar R. Nayak, Randy D. Dinkins, A. Bruce Downie, Balasubrahmanyam Addepalli, Andrea Putnam, Sharyn E. Perry, Jonathan D. Lowenson, Patrick A. Limbach
Publikováno v:
The Plant Cell. 25:2573-2586
Orthodox seeds are capable of withstanding severe dehydration. However, in the dehydrated state, Asn and Asp residues in proteins can convert to succinimide residues that can further react to predominantly form isomerized isoAsp residues upon rehydra
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::01765bf6a356bdc78213255ad7bfcc2a
https://doi.org/10.1105/tpc.113.113456
https://doi.org/10.1105/tpc.113.113456
Autor:
Denis G. Shklyaruck, Jonathan D. Lowenson, Vadim V. Shmanai, Steven Clarke, Mikhail S. Shchepinov
Publikováno v:
Amino acids, vol 48, iss 9
Racemization in proteins and peptides at sites of L-asparaginyl and L-aspartyl residues contributes to their spontaneous degradation, especially in the biological aging process. Amino acid racemization involves deprotonation of the alpha carbon and r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ad33f5d4cd0db029a9fc56db176a3610
https://escholarship.org/uc/item/0kv1c441
https://escholarship.org/uc/item/0kv1c441
Autor:
Tingsu Chen, Jonathan D. Lowenson, Steven Clarke, Zhaohui Sunny Zhou, Sharyn E. Perry, A. Bruce Downie, Susmita Maitra Majee, Nancy R. Forsthoefel, Daniel M. Vernon, Taylor D. Lloyd, Nihar R. Nayak, Randy D. Dinkins, Kim R. Schäfermeyer, Alyssa C. Eliopoulos, Tomas Rejtar
Publikováno v:
Journal of Biological Chemistry. 285:37281-37292
The role of protein isoaspartyl methyltransferase (PIMT) in repairing a wide assortment of damaged proteins in a host of organisms has been inferred from the affinity of the enzyme for isoaspartyl residues in a plethora of amino acid contexts. The id
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::042526cbfdbdadfcf1448221ab336b3c
https://doi.org/10.1074/jbc.m110.157008
https://doi.org/10.1074/jbc.m110.157008
Autor:
Tianzhu Zang, Joshua J. Klaene, Shujia Dai, Zhaohui Sunny Zhou, Joshua F. Alfaro, Steven Clarke, He G. Sun, Barry L. Karger, Jonathan D. Lowenson, Laura A. Gillies, Byung Ju Kim
Publikováno v:
Analytical Chemistry. 80:3882-3889
Isoaspartate formation is a ubiquitous post-translation modification arising from spontaneous asparagine deamidation or aspartate isomerization. The formation of isoaspartate inserts a methylene group into the protein backbone, generating a "kink", a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::455c3149a67777fa0a4cfac5e0c746df
https://doi.org/10.1021/ac800251q
https://doi.org/10.1021/ac800251q
Autor:
Wayne G. Carter, Steven Clarke, Matthew Thakur, Kevin Bailey, Vasanthy Vigneswara, Jonathan D. Lowenson, David E. Ray, Claire D. Powell
Publikováno v:
Journal of Biological Chemistry. 281:32619-32629
We report the use of a proteomic strategy to identify hitherto unknown substrates for mammalian protein l-isoaspartate O-methyltransferase. This methyltransferase initiates the repair of isoaspartyl residues in aged or stress-damaged proteins in vivo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2219fba34d0540838809eeef01b4316f
https://doi.org/10.1074/jbc.m605421200
https://doi.org/10.1074/jbc.m605421200
Publikováno v:
Journal of Biological Chemistry. 276:20695-20702
l-Isoaspartyl (d-aspartyl) O-methyltransferase (PCMT1) can initiate the conversion of damaged aspartyl and asparaginyl residues to normal l-aspartyl residues. Mice lacking this enzyme (Pcmt1−/− mice) have elevated levels of damaged residues and d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4b2747e7628985ff621a5d27d53f8134
https://doi.org/10.1074/jbc.m100987200
https://doi.org/10.1074/jbc.m100987200
Publikováno v:
Journal of Biological Chemistry. 274:20671-20678
Within proteins and peptides, both L-asparaginyl and L-aspartyl residues spontaneously degrade, generating isomerized and racemized aspartyl residues. The enzyme protein L-isoaspartate (D-aspartate) O-methyltransferase (E.C. 2.1.1.77) initiates the c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7b7252bd37f31ce10ae9b2f82e0dfd7d
https://doi.org/10.1074/jbc.274.29.20671
https://doi.org/10.1074/jbc.274.29.20671