195 related articles for article (PubMed ID: 2839474)
1. Identification of two phosphorylated threonines in the tail region of Dictyostelium myosin II.
Vaillancourt JP; Lyons C; Côté GP
J Biol Chem; 1988 Jul; 263(21):10082-7. PubMed ID: 2839474
[TBL] [Abstract][Full Text] [Related]
2. Selective removal of the carboxyl-terminal tail end of the Dictyostelium myosin II heavy chain by chymotrypsin.
Côté GP; McCrea SM
J Biol Chem; 1987 Sep; 262(27):13033-8. PubMed ID: 2958448
[TBL] [Abstract][Full Text] [Related]
3. Phosphorylation of threonine residues on cloned fragments of the Dictyostelium myosin heavy chain.
Wagle G; Noegel A; Scheel J; Gerisch G
FEBS Lett; 1988 Jan; 227(1):71-5. PubMed ID: 2828113
[TBL] [Abstract][Full Text] [Related]
4. Identification of three phosphorylation sites on each heavy chain of Acanthamoeba myosin II.
Côté GP; Collins JH; Korn ED
J Biol Chem; 1981 Dec; 256(24):12811-6. PubMed ID: 6118366
[TBL] [Abstract][Full Text] [Related]
5. Amino acid sequence of a segment of the Acanthamoeba myosin II heavy chain containing all three regulatory phosphorylation sites.
Côté GP; Robinson EA; Appella E; Korn ED
J Biol Chem; 1984 Oct; 259(20):12781-7. PubMed ID: 6149217
[TBL] [Abstract][Full Text] [Related]
6. Chemoattractant-elicited increases in Dictyostelium myosin phosphorylation are due to changes in myosin localization and increases in kinase activity.
Berlot CH; Devreotes PN; Spudich JA
J Biol Chem; 1987 Mar; 262(8):3918-26. PubMed ID: 3029131
[TBL] [Abstract][Full Text] [Related]
7. The 204-kDa smooth muscle myosin heavy chain is phosphorylated in intact cells by casein kinase II on a serine near the carboxyl terminus.
Kelley CA; Adelstein RS
J Biol Chem; 1990 Oct; 265(29):17876-82. PubMed ID: 2170399
[TBL] [Abstract][Full Text] [Related]
8. Two phosphorylations specific to the tail region of the 204-kDa heavy chain isoform of porcine aorta smooth muscle myosin.
Fukui Y; Morita F
J Biochem; 1996 Apr; 119(4):783-90. PubMed ID: 8743582
[TBL] [Abstract][Full Text] [Related]
9. Dictyostelium myosin: characterization of chymotryptic fragments and localization of the heavy-chain phosphorylation site.
Peltz G; Kuczmarski ER; Spudich JA
J Cell Biol; 1981 Apr; 89(1):104-8. PubMed ID: 7228895
[TBL] [Abstract][Full Text] [Related]
10. Structural analysis of myosin heavy chain kinase A from Dictyostelium. Evidence for a highly divergent protein kinase domain, an amino-terminal coiled-coil domain, and a domain homologous to the beta-subunit of heterotrimeric G proteins.
Futey LM; Medley QG; Côté GP; Egelhoff TT
J Biol Chem; 1995 Jan; 270(2):523-9. PubMed ID: 7822274
[TBL] [Abstract][Full Text] [Related]
11. Myosin heavy chain kinase from developed Dictyostelium cells. Purification and characterization.
Ravid S; Spudich JA
J Biol Chem; 1989 Sep; 264(25):15144-50. PubMed ID: 2549052
[TBL] [Abstract][Full Text] [Related]
12. Replacement of threonine residues by serine and alanine in a phosphorylatable heavy chain fragment of Dictyostelium myosin II.
Lück-Vielmetter D; Schleicher M; Grabatin B; Wippler J; Gerisch G
FEBS Lett; 1990 Aug; 269(1):239-43. PubMed ID: 2387408
[TBL] [Abstract][Full Text] [Related]
13. Filament formation and actin-activated ATPase activity are abolished by proteolytic removal of a small peptide from the tip of the tail of the heavy chain of Acanthamoeba myosin II.
Kuznicki J; Côté GP; Bowers B; Korn ED
J Biol Chem; 1985 Feb; 260(3):1967-72. PubMed ID: 3155741
[TBL] [Abstract][Full Text] [Related]
14. Regulation of the actin-activated ATPase activity of Acanthamoeba myosin II by copolymerization with phosphorylated and dephosphorylated peptides derived from the carboxyl-terminal end of the heavy chain.
Ganguly C; Atkinson MA; Attri AK; Sathyamoorthy V; Bowers B; Korn ED
J Biol Chem; 1990 Jun; 265(17):9993-8. PubMed ID: 2141027
[TBL] [Abstract][Full Text] [Related]
15. Purification and characterization of a myosin heavy chain kinase from Dictyostelium discoideum.
Côte GP; Bukiejko U
J Biol Chem; 1987 Jan; 262(3):1065-72. PubMed ID: 3027076
[TBL] [Abstract][Full Text] [Related]
16. Preparation of a phospholipid-insensitive, autophosphorylation-activated catalytic fragment of Acanthamoeba myosin I heavy chain kinase.
Brzeska H; Martin B; Kulesza-Lipka D; Baines I; Korn ED
J Biol Chem; 1992 Mar; 267(7):4949-56. PubMed ID: 1311323
[TBL] [Abstract][Full Text] [Related]
17. Limited tryptic digestion of Acanthamoeba myosin IA abolishes regulation of actin-activated ATPase activity by heavy chain phosphorylation.
Lynch TJ; Brzeska H; Korn ED
J Biol Chem; 1987 Oct; 262(28):13842-9. PubMed ID: 2958454
[TBL] [Abstract][Full Text] [Related]
18. Expression of Dictyostelium myosin tail segments in Escherichia coli: domains required for assembly and phosphorylation.
O'Halloran TJ; Ravid S; Spudich JA
J Cell Biol; 1990 Jan; 110(1):63-70. PubMed ID: 2404023
[TBL] [Abstract][Full Text] [Related]
19. Partial purification of two myosin heavy chain kinases from Dictyostelium discoideum.
Kuczmarski ER
J Muscle Res Cell Motil; 1986 Dec; 7(6):501-9. PubMed ID: 3027120
[TBL] [Abstract][Full Text] [Related]
20. Functional consequences of the proteolytic removal of regulatory serines from the nonhelical tailpiece of Acanthamoeba myosin II.
Sathyamoorthy V; Atkinson MA; Bowers B; Korn ED
Biochemistry; 1990 Apr; 29(15):3793-7. PubMed ID: 2160267
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
