Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Jeffrey W. Stebbins"'
Autor:
David L. Linemeyer, Paul D. van Poelje, Mark D. Erion, Edward Earl Cable, Jinzhao Hou, Patricia D. Finn, Bruce R. Ito, Jeffrey W. Stebbins
Publikováno v:
Hepatology. 49:407-417
Non-alcoholic fatty liver disease (NAFLD) is one of the most common forms of chronic liver disease, with a prevalence ranging from 10% to 30%. The use of thyroid hormone receptor (TR) agonists for the treatment of NAFLD has not been considered viable
Publikováno v:
Neurochemical Research. 23:1005-1010
Purified human central nervous system myelin contains an endogenous cysteine protease which degrades the 100-kDa myelin-associated glycoprotein into a slightly smaller 90-kDa derivative called dMAG, and which has been implicated in demyelinating dise
Publikováno v:
Biochemistry. 31:2328-2332
Allosteric enzymes are part of a unique class of enzymes which regulate metabolic pathways. On the molecular level, allosteric regulation is the result of interactions between discrete binding sites on the enzyme. In order to accommodate these multip
Publikováno v:
Biochemistry. 36(8)
Myelin-associated glycoprotein (MAG) is a transmembrane structural protein that is thought to be involved in the formation and/or maintenance of the myelin sheath. MAG is proteolyzed at a discrete location near its transmembrane domain by a calcium a
Autor:
Evan R. Kantrowitz, Diane E. Robertson, Jeffrey W. Stebbins, Mary F. Roberts, Raymond C. Stevens, William N. Lipscomb
Publikováno v:
Protein science : a publication of the Protein Society. 1(11)
The replacement of Arg-54 by Ala in the active site of Escherichia coli aspartate transcarbamoylase causes a 17,000-fold loss of activity but does not significantly influence the binding of substrates or substrate analogs (Stebbins, J.W., Xu, W., & K
Publikováno v:
Biochemistry. 29(16)
Site-specific mutagenesis has been used to create two mutant versions of aspartate transcarbamoylase. Arg-167 and Gln-231, both previously identified as interacting with the portion of the bisubstrate analogue N-(phosphonoacetyl)-L-aspartate (PALA) t
Publikováno v:
Biochemistry. 28:1617-1626
The allosteric transition of Escherichia coli aspartate transcarbamylase involves significant alterations in structure at both the quaternary and tertiary levels. On the tertiary level, the 240s loop (residues 230-245 of the catalytic chain) repositi
Publikováno v:
Biochemistry. 28(6)
Site-directed mutagenesis was used to create four mutant versions of Escherichia coli aspartate transcarbamylase at three positions in the catalytic chain of the enzyme. The location of all the amino acid substitutions was near the carbamyl phosphate