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 e performance on plant and non-plant protein submitochondrial datasets.

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

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

7 the mitochondria without forming detectable submitochondrial foci.

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

9 In the present study, submitochondrial fractionation and digitonin permeabiliz

10 Submitochondrial fractionation and pharmacological studi

11 Submitochondrial fractionation showed that both Mrp21p a

12 Submitochondrial fractionation studies found native ACAD

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

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

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

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

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

18 Protein submitochondrial localization enables the understanding

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

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

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

22 mployed MINFLUX nanoscopy to investigate the submitochondrial localization of the core MICOS subunit

23 d a new method, SubMito-XGBoost, for protein submitochondrial localization prediction.

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

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

26 From this particular submitochondrial location, PINK1 interacts with componen

27 tors are fed into XGBoost to predict protein submitochondrial locations.

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

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

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

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

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

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

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

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

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

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

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

39 However, in submitochondrial particles devoid of antioxidant defense

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

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

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

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

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

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

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

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

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

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

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

51 Treatment of submitochondrial particles with protein kinase A and ATP

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

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

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

55 Using submitochondrial particles, we confirmed that in the con

56 es of experiments with both mitochondria and submitochondrial particles.

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

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

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

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

61 nthetic activities of ATP synthase in bovine submitochondrial particles.

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

63 challenging, if not impossible, to visualize submitochondrial structures or protein distributions usi

64 Submitochondrial studies showed that cytochrome c in the

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