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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.
11 5-HTR1B and p11 by screening brain-expressed S100 proteins against serotonin and noradrenergic recept
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
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
21 uberculosis infection, neutrophils producing S100 proteins are dominant within the inflammatory lung
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
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
36 cle specific sequences (E-box and M-CAT), an S100 protein element, and a (GCT) trinucleotide repeat.
44 AnI and AnII bind to selected members of the S100 protein family shows that these interactions are sp
47 is similar to that of another member of the S100 protein family, calcyclin (S100A6), and less like t
50 K/AKT and MAPK/ERK.S100A14,one member of the S100 protein family, is significantly associated with ou
58 we report the first crystal structure of an S100 protein from this organism, the calcium-bound state
67 cts (RAGE) binds multiple ligands, including S100 proteins, high mobility group box chromosomal prote
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
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
78 eral recent advances in our understanding of S100 protein-mediated metal sequestration at the site of
80 d the stimulatory effects of proinflammatory S100 proteins might play a relevant role in the pathogen
87 n the basis of our data, we hypothesize that S100 proteins regulate the oligomerization state of all
89 tion complex on human chromosome 1q21 and 13 S100 proteins (S100A2, S100A3, S100A4, S100A6, S100A7, S
96 on the target preference of each individual S100 protein, the concentration of the proteins and calc
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
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