Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Charles L. Borders"'
Autor:
Lindsay A. Horst, Michael J. Thomenius, Paul L. Edmiston, Betsy A. Kersteen, Michael J. Jourden, Guy B. Mulligan, Paul R. Geiss, Charles L. Borders, Nichole R. Myers, Ryan M. Almeida, Melissa M. Barty, Melissa J. Brym, Mark J. Snider
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1751:178-183
Six fully conserved arginine residues (R129, R131, R235, R291, R319, and R340) closely grouped in the nucleotide binding site of rabbit muscle creatine kinase (rmCK) were mutated; four to alanine and all six to lysine. Kinetic analyses in the directi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::440fc2470a883e09022b8980f12a30d8
https://doi.org/10.1016/j.bbapap.2005.06.002
https://doi.org/10.1016/j.bbapap.2005.06.002
Autor:
Mark J. Snider, Paul L. Edmiston, Elikem R.K. Gbeddy, Katherine M. MacGregor, Guy B. Mulligan, Charles L. Borders, Michael J. Thomenius
Publikováno v:
Protein Science. 12:532-537
To explore the possibility that asparagine 285 plays a key role in transition state stabilization in phosphagen kinase catalysis, the N285Q, N285D, and N285A site-directed mutants of recombinant rabbit muscle creatine kinase (rmCK) were prepared and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e732eb89f6f733de8b08447c604de47b
https://doi.org/10.1110/ps.0230403
https://doi.org/10.1110/ps.0230403
Publikováno v:
Biochemistry. 41:6995-7000
Recombinant rabbit muscle creatine kinase (CK) was titrated with MgADP in 50 mM Bicine and 5 mM Mg(OAc)2, pH 8.3, at 30.0 degrees C by following a decrease in the protein's intrinsic fluorescence. In the presence of 50 mM NaOAc, but in the absence of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4a41b6ffdb9a16b69a31d05cad648025
https://doi.org/10.1021/bi020105+
https://doi.org/10.1021/bi020105+
Publikováno v:
Biochemistry. 35:7895-7902
Creatine kinase (CK; EC 2.7.3.2) catalyzes the reversible conversion of creatine and MgATP to phosphocreatine and MgADP. In the absence of an X-ray crystal structure, we have used the sequence homology of creatine kinases and other guanidino kinases
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::45ec8198b3f25b9ac885ffaf162c183a
https://doi.org/10.1021/bi952798i
https://doi.org/10.1021/bi952798i
Publikováno v:
Acta crystallographica. Section D, Biological crystallography. 63(Pt 3)
The structure of a transition-state analog complex of a highly soluble mutant (R134K) of rabbit muscle creatine kinase (rmCK) has been determined to 1.65 A resolution in order to elucidate the structural changes that are required to support and regul
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7367d573640497572e9833c1e7773d96
https://pubmed.ncbi.nlm.nih.gov/17327675
https://pubmed.ncbi.nlm.nih.gov/17327675
Autor:
Mark J. Snider, Charles L. Borders, Julia M. Cox, Melissa J. Brym, Andrea D. Jorjorian, Caroline A. Davis, Paul L. Edmiston, Michael J. Jourden, Chikio Chan
Publikováno v:
Biochemistry. 42(7)
Cytosolic creatine kinase exists in native form as a dimer; however, the reasons for this quaternary structure are unclear, given that there is no evidence of active site communication and more primitive guanidino kinases are monomers. Three fully co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::378dd56ae5e6b9e22a70d04331a65197
https://pubmed.ncbi.nlm.nih.gov/12590573
https://pubmed.ncbi.nlm.nih.gov/12590573
Publikováno v:
Biochemistry. 41(22)
Recombinant rabbit muscle creatine kinase (CK) was titrated with MgADP in 50 mM Bicine and 5 mM Mg(OAc)2, pH 8.3, at 30.0 degrees C by following a decrease in the protein's intrinsic fluorescence. In the presence of 50 mM NaOAc, but in the absence of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::1b4e42b52545966f3c98bcff5a556228
https://pubmed.ncbi.nlm.nih.gov/12033932
https://pubmed.ncbi.nlm.nih.gov/12033932
Autor:
Paul L. Edmiston, Nichole R. Moore, Charles L. Borders, Elizabeth A. Kersteen, Kristy L. Schavolt
Publikováno v:
Biochimica et biophysica acta. 1546(2)
Sequence homology analysis reveals that arginine-95 is fully conserved in 29 creatine kinases sequenced to date, but fully conserved as a tyrosine residue in 16 arginine kinases. Site-directed mutants of rabbit muscle creatine kinase (rmCK) were prep
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::62d7ccf0e4476f0cfaaae4455fe5e914
https://pubmed.ncbi.nlm.nih.gov/11295435
https://pubmed.ncbi.nlm.nih.gov/11295435
Publikováno v:
Biochemistry. 37(32)
All known Mn-containing superoxide dismutases (MnSODs) have a highly conserved histidine (His-30 in Escherichia coli FeSOD) in the active-site channel, and nearly all have an active-site arginine (Arg-170) that has been proposed to play a combined st
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::76034b7252481e7a13b4c0f0dbc1f9e9
https://pubmed.ncbi.nlm.nih.gov/9698380
https://pubmed.ncbi.nlm.nih.gov/9698380
Autor:
Fred W. McLafferty, Troy D. Wood, Ziqiang Guan, Charles L. Borders, Lorenzo H. Chen, George L. Kenyon
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 95(7)
Phenylglyoxal is an arginine-specific reagent that inactivates creatine kinase (CK). Previous results suggest that modification of the dimeric enzyme at a single arginine residue per subunit causes complete inactivation accompanied by the loss of nuc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::00bd89b6aceb70512e5da4e41f088168
https://pubmed.ncbi.nlm.nih.gov/9520370
https://pubmed.ncbi.nlm.nih.gov/9520370