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1 epithelial membrane antigen and negative for S100 protein.
2  mechanism for the regulation of cPLA2 by an S100 protein.
3 sly been observed for any target bound to an S100 protein.
4 8, and a relatively low percentage expressed S100 protein.
5 e I and type II transglutaminases can modify S100 proteins.
6 tions affect the properties and functions of S100 proteins.
7 served for noncanonical EF-hands, except for S100 proteins.
8 nism for calcium-promoted oligomerisation of S100 proteins.
9  were mandatory for high-affinity binding to S100 proteins.
10 volved in the stimulation of p53 activity by S100 proteins.
11                                   Mean serum S100 protein 24 hours after CPR was significantly lower
12                    During infection, certain S100 proteins act as damage-associated molecular pattern
13 5-HTR1B and p11 by screening brain-expressed S100 proteins against serotonin and noradrenergic recept
14 eins associated with inflammatory responses (S100 proteins, alarmins, protease inhibitors); and glyco
15 d survival of 1.1% over patients with either S100 protein alone.
16 ch as advanced glycation end products (AGE), S100 proteins, amyloid beta, and HMGB1 has been linked t
17 y fluorescent immunohistochemical stains for S100 protein and CD34, tumor cells labeling with both ma
18                         Upon binding Ca(2+), S100 proteins and CaM interact with protein targets and
19  molecular pattern molecules (DAMPs) such as S100 proteins and high-mobility group box 1 (HMGB1).
20     Novel evidence using biomarkers, such as S100 proteins and novel single nucleotide polymorphism d
21 modification is a property shared by several S100 proteins and that both type I and type II transglut
22 timicrobial activity of CP relative to other S100 proteins, and clarify the impact of metal depletion
23 ding advanced glycation end products (AGEs), S100 proteins, and HMGB1.
24                                              S100 proteins are a family of 10-14 kDa EF-hand-containi
25                                              S100 proteins are a subfamily of EF-hand calcium-binding
26                                              S100 proteins are calcium-regulated proteins that regula
27                                              S100 proteins are calcium-responsive signaling proteins
28 uberculosis infection, neutrophils producing S100 proteins are dominant within the inflammatory lung
29                                              S100 proteins are known to act as innate amplifier of in
30 wever, the exact biological functions of the S100 proteins are largely unknown as there are several f
31 on of helix 3 in the apo state of these four S100 proteins are likely due to variations in the amino
32 thogenesis of epidermal disease, as selected S100 proteins are markedly overexpressed in psoriasis, w
33                                              S100 proteins are of interest as mediators of calcium-as
34                                      Several S100 proteins are up-regulated in pancreatic ductal aden
35 hus underscoring the role of Ca2+ binding to S100 proteins as a molecular switch.
36                                 Importantly, S100 proteins bound p63 and p73 with different affinitie
37     In addition, we show that the Zn-binding S100 protein calprotectin has antimicrobial effects agai
38                             The host-defense S100 proteins calprotectin (CP) (S100A8/S100A9 oligomer)
39 oviding insights regarding how more than one S100 protein can interact with the same peptide target.
40 rst time that interactions between different S100 proteins can affect cancer-related activity, and th
41 evious work, these data reveal that multiple S100 proteins can repress the elaboration of an oncogeni
42                                          The S100 proteins comprise a family of 21 low molecular weig
43                           Elevated levels of S100 proteins could be detected in patients with acute G
44 es of this Akt-induced murine RT revealed an S100 protein-defined subcluster of highly aggressive lym
45 cle specific sequences (E-box and M-CAT), an S100 protein element, and a (GCT) trinucleotide repeat.
46                                              S100 proteins exist in cells as anti-parallel hetero- an
47                        Thus, a member of the S100 protein family acts as an astroglia-derived morphog
48             p11 (S100A10) is a member of the S100 protein family and forms a heterotetrameric complex
49                                          The S100 protein family functions as protein-protein interac
50              In heart and skeletal muscle an S100 protein family member, S100A1, binds to the ryanodi
51                                      Several S100 protein family members bind PPP5C increasing PPP5C
52                                As with other S100 protein family members, mts1 is a symmetric homodim
53 iversity and specificity to S100A1 and other S100 protein family members.
54 ue to considerable sequence homology between S100 protein family members.
55 -reactive protein (CRP) and 6 members of the S100 protein family of calcium-binding proteins.
56 AnI and AnII bind to selected members of the S100 protein family shows that these interactions are sp
57                     S100P is a member of the S100 protein family that is expressed in several maligna
58                   S100A13 is a member of the S100 protein family that is involved in the copper-depen
59  is similar to that of another member of the S100 protein family, calcyclin (S100A6), and less like t
60            S100B(beta beta), a member of the S100 protein family, is a Ca(2+)-binding protein with no
61                      S100A1, a member of the S100 protein family, is an EF-hand containing Ca(2+)-bin
62 K/AKT and MAPK/ERK.S100A14,one member of the S100 protein family, is significantly associated with ou
63                           As a member of the S100 protein family, Mts1 is predicted to contain four a
64 lix bundle as found for other members of the S100 protein family.
65 could potentially be used to subclassify the S100 protein family.
66     S100A1 is a member of the Ca(2+)-binding S100 protein family.
67 cificity with the other members of the human S100 protein family.
68 broader implications for the function of the S100 protein family.
69 or dysregulation of two members of the large S100 protein family.
70  we report the first crystal structure of an S100 protein from this organism, the calcium-bound state
71                         High fecal levels of S100 proteins, from 30 days to 1 year of age, were assoc
72 al ends of the protein, regions that specify S100 protein function.
73  is a general mechanism designed to regulate S100 protein function.
74                                     Fourteen S100 protein genes are located within the epidermal diff
75  the REG gene family and the calcium-binding S100 protein genes S100A9 and S100P.
76       Since binding of effector molecules to S100 proteins has been shown to involve the C-terminus a
77                                              S100 proteins have been implicated in various inflammato
78                                              S100 proteins have no intrinsic enzyme activity but bind
79              In addition, these inflammatory S100 proteins have potent antimicrobial properties and a
80 ed Glycation End products (AGEs), HMGB1, and S100 proteins, have all been shown to activate both TLRs
81 cts (RAGE) binds multiple ligands, including S100 proteins, high mobility group box chromosomal prote
82                               A low level of S100 proteins in infants' fecal samples associated with
83 n RSK1, which is inhibited by Ca(2+)-binding S100 proteins in malignant melanomas.
84 te Th17 development, emphasizing the role of S100 proteins in Th17-triggered inflammation.
85 ss or necrosis lead the release of HMGB1 and S100 proteins in the extracellular compartment where the
86    We therefore investigated the presence of S100 proteins in the stool, serum, and bowel tissue of p
87 ered when studying the functional effects of S100 proteins in their biological context.
88 significantly increased abundance of several S100 proteins, including Fibronectin and Tenascin-C (Tnc
89 p11 (S100A10), a member of a large family of S100 proteins, interacts with serotonin receptor 1B (5-H
90                         Although the typical S100 protein intersubunit four-helix bundle is conserved
91            The cellular functions of several S100 proteins involve specific interactions with phospho
92                                DEGs encoding S100 proteins, keratins, small proline-rich repeat prote
93 . B-defensins like DEFB4A, DEFB4B, DEFB103A, S100 proteins like S100A7, S100A12), chemotactic factors
94     We investigated the relationship between S100 proteins, LRNC, and biologic therapy in psoriasis.
95                                          The S100 proteins make up a family of dimeric calcium bindin
96 nd thereafter, to explore mechanisms whereby S100 proteins may regulate release of inflammatory media
97 eral recent advances in our understanding of S100 protein-mediated metal sequestration at the site of
98                          Regarding our data, S100 proteins might be novel markers for the diagnosis a
99 d the stimulatory effects of proinflammatory S100 proteins might play a relevant role in the pathogen
100                                              S100 proteins modulate p53 activity by interacting with
101                                    Like most S100 proteins, Mts1 exists as a dimer in solution and co
102 These include the transition metal-chelating S100 proteins, natural resistance-associated macrophage
103              Immunocytochemical staining for S100 protein, neurofilament protein, tyrosine hydroxylas
104                                Additionally, S100 protein, neuron-specific enolase, beta-amyloid prot
105 e of patients with GvHD and the influence of S100 proteins on the induction of Th17 cells.
106                               The fused-type S100 protein profilaggrin and its proteolytic products i
107                                              S100 proteins promote cancer cell migration and metastas
108  for small molecule screening based on known S100 protein-protein interactions.
109 n the basis of our data, we hypothesize that S100 proteins regulate the oligomerization state of all
110                        As with other dimeric S100 proteins, S100A1 is a symmetric homodimer with heli
111 tion complex on human chromosome 1q21 and 13 S100 proteins (S100A2, S100A3, S100A4, S100A6, S100A7, S
112           In addition to binding Ca(2+), the S100 protein S100B binds Zn(2+) with relatively high aff
113 hand Ca(2+)-binding proteins (CBPs), such as S100 proteins (S100s) and calmodulin (CaM), are signalin
114                     Function-blocking Abs to S100 proteins significantly altered allergic inflammator
115                                As with other S100 protein structures, the quaternary structure of Zn(
116 ible than the corresponding regions of other S100 proteins studied to date.
117             However, there are several other S100 proteins that are produced in response to infection
118                  In this review, we focus on S100 proteins that exhibit antimicrobial properties thro
119  on the target preference of each individual S100 protein, the concentration of the proteins and calc
120 irst structures of a zinc-only complex of an S100 protein to be determined.
121 f the ability of Ca(2+)-calmodulin or Ca(2+)-S100 proteins to antagonize the inhibitory function of c
122 nding of representative members of the human S100 proteins to short N-terminal peptides of annexin I
123 ng RAGE-dependent signals from extracellular S100 proteins to the cytoplasmic signaling complexes.
124   Furthermore, stimulation of monocytes with S100 proteins was found to promote Th17 development, emp
125                                From 25 human S100 proteins, we focused our attention on S100A4 becaus
126 owing recent reports of amyloid formation by S100 proteins, we investigated the aggregation propertie
127 modifications have been observed for several S100 proteins, we propose that modification of Cys81 may
128                                              S100 proteins were expressed by lamina propria macrophag
129 l, these results put forward novel roles for S100 proteins, whose metal-modulated aggregation propens
130  However, colocalization of both Melan-A and S100 protein with CD34 was demonstrated.

 
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