화학공학소재연구정보센터
검색결과 : 10건
No. Article
1 The molecular mechanism of muscle dysfunction associated with the R133W mutation in Tpm2.2
Borovikov YS, Karpicheva OE, Avrova SV, Simonyan AO, Sirenko VV, Redwood CS
Biochemical and Biophysical Research Communications, 523(1), 258, 2020
2 The molecular mechanisms of a high Ca2+-sensitivity and muscle weakness associated with the Ala155Thr substitution in Tpm3.12
Avrova SV, Karpicheva OE, Simonyan AO, Sirenko VV, Redwood CS, Borovikov YS
Biochemical and Biophysical Research Communications, 515(2), 372, 2019
3 The reason for the low Ca2+-sensitivity of thin filaments associated with the Glu41 Lys mutation in the TPM2 gene is "freezing" of tropomyosin near the outer domain of actin and inhibition of actin monomer switching off during the ATPase cycle
Avrova SV, Karpicheva OE, Rysev NA, Simonyan AO, Sirenko VV, Redwood CS, Borovikov YS
Biochemical and Biophysical Research Communications, 502(2), 209, 2018
4 The reason for a high Ca2+-sensitivity associated with Arg91Gly substitution in TPM2 gene is the abnormal behavior and high. flexibility of tropomyosin during the ATPase cycle
Borovikov YS, Simonyan AO, Karpicheva OE, Avrova SV, Rysev NA, Sirenko VV, Piers A, Redwood CS
Biochemical and Biophysical Research Communications, 494(3-4), 681, 2017
5 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
6 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
7 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
8 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
9 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
10 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