1 |
Hypertrophic cardiomyopathy-causing Asp175asn and Glu180gly Tpm1 mutations shift tropomyosin strands further towards the open position during the ATPase cycle Borovikav YS, Rysev NA, Karpicheva OE, Redwood CS Biochemical and Biophysical Research Communications, 407(1), 197, 2011 |
2 |
The effect of the dilated cardiomyopathy-causing Glu40Lys TPM1 mutation on actin-myosin interactions during the ATPase cycle Borovikov YS, Avrova SV, Karpicheva OE, Robinson P, Redwood CS Biochemical and Biophysical Research Communications, 411(3), 496, 2011 |
3 |
A new property of twitchin to restrict the "rolling" of mussel tropomyosin and decrease its affinity for actin during the actomyosin ATPase cycle Avrova SV, Shelud'ko NS, Borovikov YS Biochemical and Biophysical Research Communications, 394(1), 126, 2010 |
4 |
Dilated cardiomyopathy mutations in alpha-tropomyosin inhibit its movement during the ATPase cycle Borovikov YS, Karpicheva OE, Chudalova GA, Robinson P, Redwood CS Biochemical and Biophysical Research Communications, 381(3), 403, 2009 |
5 |
Caldesmon inhibits the rotation of smooth actin subdomain-1 and alters its mobility during the ATP hydrolysis cycle Kulikova N, Avrova SV, Borovikov YS Biochemical and Biophysical Research Communications, 390(1), 125, 2009 |
6 |
Caldesmon inhibits the actin-myosin interaction by changing its spatial orientation and mobility during the ATPase activity cycle Kulikova N, Pronina OE, Dabrowska R, Borovikov YS Biochemical and Biophysical Research Communications, 357(2), 461, 2007 |
7 |
Caldesmon restricts the movement of both C and N-termini of tropomyosin on F-actin in ghost fibers during the actomyosin ATPase cycle Kulikova N, Pronina OE, Dabrowska R, Borovikov YS Biochemical and Biophysical Research Communications, 345(1), 280, 2006 |