Zobrazeno 1 - 10
of 74
pro vyhledávání: '"Ann Ginsburg"'
Publikováno v:
Journal of Biological Chemistry. 280:35424-35432
The functional form of ClpP, the proteolytic component of ATP-dependent Clp proteases, is a hollow-cored particle composed of two heptameric rings joined face-to-face forming an aqueous chamber containing the proteolytic active sites. We have found t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e15113488cbe30656dc93023adcf5b76
https://doi.org/10.1074/jbc.m507240200
https://doi.org/10.1074/jbc.m507240200
Publikováno v:
Journal of Biological Chemistry. 280:12221-12230
Substrate recognition by Clp chaperones is dependent on interactions with motifs composed of specific peptide sequences. We studied the binding of short motif-bearing peptides to ClpA, the chaperone component of the ATP-dependent ClpAP protease of Es
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5e70fc2b6728053c55036d6876a1e10c
https://doi.org/10.1074/jbc.m411733200
https://doi.org/10.1074/jbc.m411733200
Publikováno v:
Thermochimica Acta. 420:37-43
The activity of enzyme I (EI), the first protein in the bacterial PEP:sugar phosphotransferase system, is regulated by a monomer–dimer equilibrium where a Mg2+-dependent autophosphorylation by PEP requires the homodimer. Using inactive EI(H189A), i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a3f16b043b10a0f1f4c6bc35bc144a36
https://doi.org/10.1016/j.tca.2003.10.028
https://doi.org/10.1016/j.tca.2003.10.028
Autor:
Ann Ginsburg, Thomas E. Olszewski, John A. Hammer, Kirsten Remmert, M.Blair Bowers, Mariana N. Dimitrova
Publikováno v:
Journal of Biological Chemistry. 279:3068-3077
CARMIL, also known as Acan 125, is a multidomain protein that was originally identified on the basis of its interaction with the Src homology 3 (SH3) domain of type I myosins from Acanthamoeba. In a subsequent study of CARMIL from Dictyostelium, pull
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d0ffbe021fde956b89d802cfc896d56e
https://doi.org/10.1074/jbc.m308829200
https://doi.org/10.1074/jbc.m308829200
Autor:
Mathias Krumbiegel, Robert Blumenthal, David P. Remeta, Conceição A.S.A. Minetti, and Ann Ginsburg, Anu Puri
Publikováno v:
Biochemistry. 41:2044-2054
The conformational and thermal stability of full-length hemagglutinin (HA) of influenza virus (strain X31) has been investigated using a combination of differential scanning calorimetry (DSC), analytical ultracentrifugation, fluorescence, and circula
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::57b9c375308b230773d4c1a53d6ad493
https://doi.org/10.1021/bi015614a
https://doi.org/10.1021/bi015614a
Autor:
Sergei B. Ruvinov, Mariana N. Dimitrova, Alan Peterkofsky, Roman H. Szczepanowski, Ann Ginsburg
Publikováno v:
Biochemistry. 41:906-913
The bacterial PEP:sugar phosphotransferase system couples the phosphorylation and translocation of specific sugars across the membrane. The activity of the first protein in this pathway, enzyme I (EI), is regulated by a monomer-dimer equilibrium wher
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fbbbc70aeab253166d00a32fff241657
https://doi.org/10.1021/bi011801x
https://doi.org/10.1021/bi011801x
Publikováno v:
Biochemistry. 40:4923-4931
The conformational stabilities of the vnd (ventral nervous system defective)/NK-2 homeodomain [HD(wt); residues 1-80 that encompass the 60-residue homeodomain] and those harboring mutations in helix III of the DNA recognition site [HD(H52R) and HD(H5
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7356d3034e1e1172b3cff784be0be6a9
https://doi.org/10.1021/bi0022341
https://doi.org/10.1021/bi0022341
Publikováno v:
Archives of Biochemistry and Biophysics. 371:115-123
Guanidine x HCl (GdnHCl)-induced unfolding of tetrameric N(5)-(L-1-carboxyethyl)-L-ornithine synthase (CEOS; 141,300 M(r)) from Lactococcus lactis at pH 7.2 and 25 degrees C occurred in several phases. The enzyme was inactivated at approximately 1 M
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::16cb59bee0aac2b419da3647079aba92
https://doi.org/10.1006/abbi.1999.1429
https://doi.org/10.1006/abbi.1999.1429
Autor:
Rodney L. Levine, Jae-Ryong Kim, Ann Ginsburg, Ki-Sun Kwon, Sue Goo Rhee, Seung-Rock Lee, Hae Won Yoon
Publikováno v:
Journal of Biological Chemistry. 274:4722-4734
A thioredoxin reductase (TrxR), named here TrxR2, that did not react with antibodies to the previously identified TrxR (now named TrxR1) was purified from rat liver. Like TrxR1, TrxR2 was a dimeric enzyme containing selenocysteine (Secys) as the COOH
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::96bc931d931fb0d07cb650fec3319b59
https://doi.org/10.1074/jbc.274.8.4722
https://doi.org/10.1074/jbc.274.8.4722
Publikováno v:
Protein Science. 8:1899-1903
Self-association of ClpB (a mixture of 95- and 80-kDa subunits) has been studied with gel filtration chromatography, analytical ultracentrifugation, and electron microscopy. Monomeric ClpB predominates at low protein concentration (0.07 mg/mL), while
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6b1393e3430045d93ae3eccc28c74b29
https://doi.org/10.1110/ps.8.9.1899
https://doi.org/10.1110/ps.8.9.1899