ライフサイエンスコーパス: S100 protein

1 mechanism for the regulation of cPLA2 by an S100 protein.

2 sly been observed for any target bound to an S100 protein.

3 8, and a relatively low percentage expressed S100 protein.

4 epithelial membrane antigen and negative for S100 protein.

5 nism for calcium-promoted oligomerisation of S100 proteins.

6 were mandatory for high-affinity binding to S100 proteins.

7 volved in the stimulation of p53 activity by S100 proteins.

8 e I and type II transglutaminases can modify S100 proteins.

9 Mean serum S100 protein 24 hours after CPR was significantly lower

10 During infection, certain S100 proteins act as damage-associated molecular pattern

11 5-HTR1B and p11 by screening brain-expressed S100 proteins against serotonin and noradrenergic recept

12 d survival of 1.1% over patients with either S100 protein alone.

13 ch as advanced glycation end products (AGE), S100 proteins, amyloid beta, and HMGB1 has been linked t

14 y fluorescent immunohistochemical stains for S100 protein and CD34, tumor cells labeling with both ma

15 molecular pattern molecules (DAMPs) such as S100 proteins and high-mobility group box 1 (HMGB1).

16 modification is a property shared by several S100 proteins and that both type I and type II transglut

17 timicrobial activity of CP relative to other S100 proteins, and clarify the impact of metal depletion

18 S100 proteins are a family of 10-14 kDa EF-hand-containi

19 S100 proteins are calcium-regulated proteins that regula

20 S100 proteins are calcium-responsive signaling proteins

21 uberculosis infection, neutrophils producing S100 proteins are dominant within the inflammatory lung

22 S100 proteins are known to act as innate amplifier of in

23 wever, the exact biological functions of the S100 proteins are largely unknown as there are several f

24 on of helix 3 in the apo state of these four S100 proteins are likely due to variations in the amino

25 thogenesis of epidermal disease, as selected S100 proteins are markedly overexpressed in psoriasis, w

26 S100 proteins are of interest as mediators of calcium-as

27 Several S100 proteins are up-regulated in pancreatic ductal aden

28 hus underscoring the role of Ca2+ binding to S100 proteins as a molecular switch.

29 Importantly, S100 proteins bound p63 and p73 with different affinitie

30 In addition, we show that the Zn-binding S100 protein calprotectin has antimicrobial effects agai

31 oviding insights regarding how more than one S100 protein can interact with the same peptide target.

32 rst time that interactions between different S100 proteins can affect cancer-related activity, and th

33 evious work, these data reveal that multiple S100 proteins can repress the elaboration of an oncogeni

34 The S100 proteins comprise a family of 21 low molecular weig

35 Elevated levels of S100 proteins could be detected in patients with acute G

36 cle specific sequences (E-box and M-CAT), an S100 protein element, and a (GCT) trinucleotide repeat.

37 S100 proteins exist in cells as anti-parallel hetero- an

38 p11 (S100A10) is a member of the S100 protein family and forms a heterotetrameric complex

39 In heart and skeletal muscle an S100 protein family member, S100A1, binds to the ryanodi

40 As with other S100 protein family members, mts1 is a symmetric homodim

41 iversity and specificity to S100A1 and other S100 protein family members.

42 ue to considerable sequence homology between S100 protein family members.

43 -reactive protein (CRP) and 6 members of the S100 protein family of calcium-binding proteins.

44 AnI and AnII bind to selected members of the S100 protein family shows that these interactions are sp

45 S100P is a member of the S100 protein family that is expressed in several maligna

46 S100A13 is a member of the S100 protein family that is involved in the copper-depen

47 is similar to that of another member of the S100 protein family, calcyclin (S100A6), and less like t

48 S100B(beta beta), a member of the S100 protein family, is a Ca(2+)-binding protein with no

49 S100A1, a member of the S100 protein family, is an EF-hand containing Ca(2+)-bin

50 K/AKT and MAPK/ERK.S100A14,one member of the S100 protein family, is significantly associated with ou

51 As a member of the S100 protein family, Mts1 is predicted to contain four a

52 S100A1 is a member of the Ca(2+)-binding S100 protein family.

53 cificity with the other members of the human S100 protein family.

54 broader implications for the function of the S100 protein family.

55 or dysregulation of two members of the large S100 protein family.

56 lix bundle as found for other members of the S100 protein family.

57 could potentially be used to subclassify the S100 protein family.

58 we report the first crystal structure of an S100 protein from this organism, the calcium-bound state

59 al ends of the protein, regions that specify S100 protein function.

60 is a general mechanism designed to regulate S100 protein function.

61 Fourteen S100 protein genes are located within the epidermal diff

62 the REG gene family and the calcium-binding S100 protein genes S100A9 and S100P.

63 Since binding of effector molecules to S100 proteins has been shown to involve the C-terminus a

64 S100 proteins have been implicated in various inflammato

65 S100 proteins have no intrinsic enzyme activity but bind

66 In addition, these inflammatory S100 proteins have potent antimicrobial properties and a

67 cts (RAGE) binds multiple ligands, including S100 proteins, high mobility group box chromosomal prote

68 n RSK1, which is inhibited by Ca(2+)-binding S100 proteins in malignant melanomas.

69 te Th17 development, emphasizing the role of S100 proteins in Th17-triggered inflammation.

70 ss or necrosis lead the release of HMGB1 and S100 proteins in the extracellular compartment where the

71 We therefore investigated the presence of S100 proteins in the stool, serum, and bowel tissue of p

72 ered when studying the functional effects of S100 proteins in their biological context.

73 significantly increased abundance of several S100 proteins, including Fibronectin and Tenascin-C (Tnc

74 p11 (S100A10), a member of a large family of S100 proteins, interacts with serotonin receptor 1B (5-H

75 Although the typical S100 protein intersubunit four-helix bundle is conserved

76 The cellular functions of several S100 proteins involve specific interactions with phospho

77 The S100 proteins make up a family of dimeric calcium bindin

78 eral recent advances in our understanding of S100 protein-mediated metal sequestration at the site of

79 Regarding our data, S100 proteins might be novel markers for the diagnosis a

80 d the stimulatory effects of proinflammatory S100 proteins might play a relevant role in the pathogen

81 S100 proteins modulate p53 activity by interacting with

82 Like most S100 proteins, Mts1 exists as a dimer in solution and co

83 Immunocytochemical staining for S100 protein, neurofilament protein, tyrosine hydroxylas

84 e of patients with GvHD and the influence of S100 proteins on the induction of Th17 cells.

85 The fused-type S100 protein profilaggrin and its proteolytic products i

86 S100 proteins promote cancer cell migration and metastas

87 n the basis of our data, we hypothesize that S100 proteins regulate the oligomerization state of all

88 As with other dimeric S100 proteins, S100A1 is a symmetric homodimer with heli

89 tion complex on human chromosome 1q21 and 13 S100 proteins (S100A2, S100A3, S100A4, S100A6, S100A7, S

90 In addition to binding Ca(2+), the S100 protein S100B binds Zn(2+) with relatively high aff

91 Function-blocking Abs to S100 proteins significantly altered allergic inflammator

92 As with other S100 protein structures, the quaternary structure of Zn(

93 ible than the corresponding regions of other S100 proteins studied to date.

94 However, there are several other S100 proteins that are produced in response to infection

95 In this review, we focus on S100 proteins that exhibit antimicrobial properties thro

96 on the target preference of each individual S100 protein, the concentration of the proteins and calc

97 irst structures of a zinc-only complex of an S100 protein to be determined.

98 f the ability of Ca(2+)-calmodulin or Ca(2+)-S100 proteins to antagonize the inhibitory function of c

99 nding of representative members of the human S100 proteins to short N-terminal peptides of annexin I

100 ng RAGE-dependent signals from extracellular S100 proteins to the cytoplasmic signaling complexes.

101 Furthermore, stimulation of monocytes with S100 proteins was found to promote Th17 development, emp

102 owing recent reports of amyloid formation by S100 proteins, we investigated the aggregation propertie

103 modifications have been observed for several S100 proteins, we propose that modification of Cys81 may

104 l, these results put forward novel roles for S100 proteins, whose metal-modulated aggregation propens

105 However, colocalization of both Melan-A and S100 protein with CD34 was demonstrated.