ライフサイエンスコーパス: submitochondrial

1 Numerous proteins from various submitochondrial compartments were observed to be carbon

2 mported proteins are directed to one of four submitochondrial compartments--the outer mitochondrial m

3 import into and sorting to their destination submitochondrial compartments.

4 ly of the large GTPase Mfn2 and changing its submitochondrial distribution and membrane mobility-prop

5 ndria isolated from somatic tissues, and the submitochondrial distribution pattern of the Gpx4 protei

6 the mitochondria without forming detectable submitochondrial foci.

7 r mitochondrial membrane (OMM) contact point submitochondrial fraction and, as super-resolution micro

8 In the present study, submitochondrial fractionation and digitonin permeabiliz

9 Submitochondrial fractionation and pharmacological studi

10 Submitochondrial fractionation showed that both Mrp21p a

11 Submitochondrial fractionation studies found native ACAD

12 epatic distribution of mtNOS, immunoblotting submitochondrial fractions, and immunohistochemistry of

13 By producing highly purified submitochondrial fractions, we report here that Mclk1(+/

14 At the submitochondrial level, mitofilin, a core MINOS subunit,

15 ed by controversy around its subcellular and submitochondrial localization and the authenticity of it

16 theless, the targeting mode of Pink1 and its submitochondrial localization are still not conclusively

17 he use of electron microscopy to resolve the submitochondrial localization of calcium uptake regulato

18 ed in mitochondria, and we have examined the submitochondrial localization of MRP-1 and investigated

19 tex and SH-SY5Y neuroblastoma cells, but the submitochondrial localization of mu-calpain was not dete

20 ochondrial import sequence, its cellular and submitochondrial localization remains unclear in part be

21 This study investigated the submitochondrial location of cyclophilin D by following

22 When bovine heart submitochondrial particles (SMP) were illuminated with U

23 of Mrp1 in heart homogenate, sarcolemma, and submitochondrial particles (SMP) were increased 1.6-, 2-

24 c1 complex) has been studied in bovine heart submitochondrial particles (SMP) when cytochrome b was r

25 dox reaction of the bis-heme cytochrome b in submitochondrial particles (SMP), and all three inhibiti

26 tase (complex I) detected in tightly coupled submitochondrial particles (SMP).

27 nsfer pathway of complex III in bovine heart submitochondrial particles (SMP).

28 I, bc1 complex) were studied in bovine heart submitochondrial particles (SMP).

29 d that the rate of O-2 generation in cardiac submitochondrial particles (SMPs) was directly related t

30 The rate of (O2(./-)) generation by submitochondrial particles (SMPs) was inversely related

31 indicate that complex I is inactivated when submitochondrial particles are treated with Ca2+.

32 t human factor B, which when added to bovine submitochondrial particles depleted of their factor B re

33 However, in submitochondrial particles devoid of antioxidant defense

34 with anti-OSCP IgG from a fraction of bovine submitochondrial particles enriched in oligomycin-sensit

35 NO. production obtained with homogenates and submitochondrial particles indicated that most of the en

36 hondrial NADH dehydrogenase (complex I) with submitochondrial particles isolated from Epstein-Barr vi

37 none markedly increased H2O2 production from submitochondrial particles oxidizing the complex I subst

38 In the study presented here, submitochondrial particles prepared from rat heart were

39 mitochondria, mitochondrial homogenates, and submitochondrial particles produced NO. (followed by the

40 Similarly, liver submitochondrial particles revealed a 44% decrease in th

41 Furthermore, we had previously shown that in submitochondrial particles the affinity of complex I for

42 Sprague-Dawley rat hearts and corresponding submitochondrial particles was studied.

43 nalyses of rat liver mitochondria as well as submitochondrial particles were negative for any peptide

44 ure, never frozen rat liver mitochondria and submitochondrial particles were obtained.

45 Treatment of submitochondrial particles with protein kinase A and ATP

46 pyruvate suppressed superoxide production by submitochondrial particles, and attenuated oxidative str

47 In bovine heart mitochondria and in submitochondrial particles, membrane-associated proteins

48 When Ndi1 was incorporated into bovine heart submitochondrial particles, the Q-bound form, but not th

49 Using submitochondrial particles, we confirmed that in the con

50 es of experiments with both mitochondria and submitochondrial particles.

51 ce of O2*- released from this preparation of submitochondrial particles.

52 t not the Q-free Ndi1, was incorporated into submitochondrial particles.

53 ygen consumption of cells, mitochondria, and submitochondrial particles.

54 g helices 2 and 3 of QPs3, in mitoplasts and submitochondrial particles.

55 pectrometry to produce a quantitative map of submitochondrial protein distribution in S. cerevisiae.

56 Submitochondrial studies showed that cytochrome c in the

57 is c-subunit channel (mPTP) in brain-derived submitochondrial vesicles (SMVs) enriched for F1FO ATP s