Zobrazeno 1 - 10
of 23
pro vyhledávání: '"Alexander J. Murphy"'
Autor:
Anne K. Engmann, John J. Hatch, Prakruti Nanda, Priya Veeraraghavan, Abdulkadir Ozkan, Alexandros Poulopoulos, Alexander J. Murphy, Jeffrey D. Macklis
Publikováno v:
Nat Protoc
During neuronal development, growth cones (GCs) of projection neurons navigate complex extracellular environments to reach distant targets, thereby generating extraordinarily complex circuitry. These dynamic structures located at the tips of axonal p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::78302fb2631e78f61b219cc0e9bb31d2
https://pubmed.ncbi.nlm.nih.gov/35022617
https://pubmed.ncbi.nlm.nih.gov/35022617
Autor:
Alexander J. Murphy, Richard J. Coll
Publikováno v:
Biochemistry. 30:1456-1461
The CaATPase of sarcoplasmic reticulum was reacted with ({gamma}-{sup 32}P)ATP to form the covalent phosphoenzyme intermediate. Noncompetitive inhibition by reactive red-120 and chelation of calcium allowed the authors to monitor single-turnover kine
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a5f049764e0ceec13419efef69a41012
https://doi.org/10.1021/bi00220a002
https://doi.org/10.1021/bi00220a002
Reaction of a carbodiimide adduct of ATP at the active site of sarcoplasmic reticulum calcium ATPase
Autor:
Alexander J. Murphy
Publikováno v:
Biochemistry. 29:11236-11242
An adduct of a carbodiimide and ATP was synthesized from 1-ethyl-3-[3-(dimethylamino)propyl]carbodiimide (EDC) and the nucleotide. Despite its limited stability (t 1/2 for hydrolysis of about 5 min at 25 o C), it was shown to react with and inactivat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::11c59a7c2dbb4daa527d973803ff7b8f
https://doi.org/10.1021/bi00503a012
https://doi.org/10.1021/bi00503a012
Publikováno v:
FEBS letters. 335(1)
The sarcoplasmic reticulum Ca 2+ -ATPase loses hydrolytic activity and the ability to be phosphorylated by P i following incubation with EDC [1-ethyl-3-(3-dimethylaminopropyl)carbodiimide]. 4 nmol of tempamine per mg SR protein can be coupled to eith
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8230cbda2feb52e7f430a87ff6ed9b2f
https://pubmed.ncbi.nlm.nih.gov/7902300
https://pubmed.ncbi.nlm.nih.gov/7902300
Autor:
Alexander J. Murphy, Stefan Highsmith
Publikováno v:
Biochemistry. 31(2)
The ionic strength dependence of the binding of rabbit skeletal muscle myosin subfragment 1, S1, to F-actin in the presence of saturating concentrations of MgATP or MgADP was analyzed in order to determine the association constants at zero ionic stre
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1da80329d1724b9571059e7445d41970
https://pubmed.ncbi.nlm.nih.gov/1731895
https://pubmed.ncbi.nlm.nih.gov/1731895
Autor:
Alexander J. Murphy
Publikováno v:
Biochemistry. 15:4492-4496
Modification of calcium-translocating sarcoplasmic reticulum membranes (SR) with 5,5'-dithiobis(2-nitrobenzoate) (Nbs2) reveals four classes (kinetic sets) of sulfhydryl groups. Of the 25 mol/1.5 X 10(5) G OF SR protein (i.e., containing 1 mol of ATP
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d0cfb52f8f6a3e56c8ea6dc0c6f7ca24
https://doi.org/10.1021/bi00665a025
https://doi.org/10.1021/bi00665a025
Autor:
Alexander J. Murphy
Publikováno v:
Biochemical and Biophysical Research Communications. 70:1048-1054
Reaction of rabbit sarcoplasmic reticulum vesicles with the arginyl residue reagent 2,3-butanedione results in the inactivation of the Ca+2-dependent ATPase activity. At pH 6.9, 25°, with 10 mM butanedione the pseudo-first order rate constant is 0.0
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::76ff7fb19eae5938bc380b8d877b0f3b
https://doi.org/10.1016/0006-291x(76)91008-1
https://doi.org/10.1016/0006-291x(76)91008-1
Autor:
Alexander J. Murphy
Publikováno v:
Archives of Biochemistry and Biophysics. 180:114-120
Incubation of sarcoplasmic reticulum membranes (SR) with pyridoxal-5′-phosphate (PLP) followed by NaBH4 reduction results in a progressive loss of calcium-dependent ATPase activity. The rate constants and extents of inactivation are not linear func
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0c42c6ab3531cdf635c21ed2131ecef5
https://doi.org/10.1016/0003-9861(77)90014-5
https://doi.org/10.1016/0003-9861(77)90014-5
Autor:
Alexander J. Murphy
Publikováno v:
Biochemical and Biophysical Research Communications. 70:160-166
Treatment of rabbit sarcoplasmic reticulum vesicles with the cross-linking agent, cupric phenanthroline, causes production of high-molecular weight bands on SDS-gel electrophoresis. A plot of log mol wt vs mobility indicates that the main band produc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e35eca5c1bb43e144f6bd2527a00e80f
https://doi.org/10.1016/0006-291x(76)91122-0
https://doi.org/10.1016/0006-291x(76)91122-0
Autor:
Alexander J. Murphy, Richard J. Coll
Publikováno v:
FEBS Letters. 187:131-134
Sarcoplasmic reticulum CaATPase hydrolysis of high concentrations of ATP was studied in the presence of ADP. The results obtained were best described as noncompetitive inhibition; added product lowered the Vmax but did not affect the slopes of Eadie-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b417a5abe56e1e86d9cf268f49748630
https://doi.org/10.1016/0014-5793(85)81228-x
https://doi.org/10.1016/0014-5793(85)81228-x