ライフサイエンスコーパス: ADAM

1 receptor) to chymotrypsin/trypsin or soluble ADAM.

2 hat is important for the activation of these ADAMs.

3 e melt source region lies east towards Mount Adams.

4 ptional activation of the sheddase molecule, ADAM 10 (A disintegrin and metalloprotease domain-contai

5 hese studies further suggest that inhibiting ADAM 10 activity could be of therapeutic benefit in AKI.

6 pases, and the ectodomains of the sheddases, ADAMs 10 and 17.

7 ls results in a significant up-regulation of Adams 10, 17, 12, and 19.

8 le of a disintegrin and a metalloproteinase (ADAM) 10 and ADAM17 for leukocyte migration in vitro and

9 ated in a disintegrin and metalloproteinase (ADAM) 10 maturation, during macrophage proinflammatory a

10 ion of a disintegrin and metalloproteinases (ADAMs) 10 and 17, which convert transmembrane fractalkin

11 A disintegrin and metalloproteinase (ADAM)10 and ADAM17 are physiologic relevant sheddases of

12 te that a disintegrin and metalloproteinase (ADAM)10 is the primary physiological sheddase of ICOSL i

13 domain of a disintegrin and metalloprotease (ADAM)10, a transmembrane metalloprotease mediating ectod

14 mainly a disintegrin and metalloproteinase (ADAM)10, ADAM17, ADAM19, and MMP3.

15 sion of a disintegrin and metalloproteinase (ADAM)10, which is the primary sheddase of CD23, as well

16 teases "a disintegrin and metalloproteases" (ADAM)-10 and ADAM-17, as demonstrated through the use of

17 metalloproteinase domain-containing protein (ADAM)-10, ADAM-17, and ADAM-10 activities were measured

18 n-containing protein (ADAM)-10, ADAM-17, and ADAM-10 activities were measured with SensoLyte 520 ADAM

19 iosis patients and find growth-factor-driven ADAM-10 activity and MET shedding are jointly dysregulat

20 In contrast, Mek inhibition reduces ADAM-10 and -17 activities but fails to inhibit compensa

21 We find that ADAM-10 and -17 dynamically integrate numerous signaling

22 l, an increase in expression and activity of ADAM-10 and ADAM-17 in old peripheral blood mononuclear

23 cells within RA ST expressed high levels of ADAM-10 compared with cells within osteoarthritis ST and

24 ADAM-10 expression was determined using immunohistology,

25 ADAM-10 expression was significantly elevated at the pro

26 In order to examine the role of ADAM-10 in angiogenesis, we performed in vitro Matrigel

27 These data show that ADAM-10 is overexpressed in RA and suggest that ADAM-10

28 ADAM-10 may be a potential therapeutic target in inflamm

29 M-10 is overexpressed in RA and suggest that ADAM-10 may play a role in RA angiogenesis.

30 s were performed with specific antibodies to ADAM-10 or ADAM-17.

31 To determine whether ADAM-10 plays a role in angiogenesis in the context of R

32 In addition, ADAM-10 siRNA-treated HMVECs from the RA synovial fibrob

33 ADAM-10 siRNA-treated HMVECs had decreased endothelial c

34 l cells (HMVECs) transfected with control or ADAM-10 small interfering RNA (siRNA).

35 in and Metalloproteinases (ADAMs), including ADAM-10, ADAM-17 and ADAM-33, which suggest that selecti

36 m the cell surface by the metalloproteinase, ADAM-10, in combination with heparan sulfate.

37 ical presentation with a PUL and assayed for ADAM-12 by ELISA.

38 Serum ADAM-12 concentrations were increased in women with hist

39 Serum ADAM-12 did not differentiate histologically-confirmed E

40 ulatory element (NRE) at the 5'-UTR of human ADAM-12 gene, which acts as a transcriptional repressor.

41 Increased urinary level of ADAM-12 in breast and bladder cancers correlates with di

42 oundation for therapeutic down-regulation of ADAM-12 in cancer, arthritis and cardiac hypertrophy.

43 spective study evaluating the performance of ADAM-12 in differentiating EP from the full spectrum of

44 ressor to maintain a low-level expression of ADAM-12 in most normal cells.

45 We now report here that overexpression of ADAM-12 in triple-negative MDA-MB-231 breast cancer cell

46 Basal expression of ADAM-12 is very low in adult tissues but rises markedly

47 NS/SIGNIFICANCE: When measured in isolation, ADAM-12 levels had limited value as a diagnostic biomark

48 gest that interaction of these proteins with ADAM-12 NRE is critical for transcriptional repression o

49 tional suppression, loss of which results in ADAM-12 overexpression in breast cancer cells.

50 Studies on ADAM-12 regulation have identified a highly conserved ne

51 forming negative regulatory element (NRE) in ADAM-12 that functions as a transcriptional suppressor t

52 The diagnostic potential of ADAM-12 was only significant when 'ambiguous' PUL outcom

53 disintegrin and metalloprotease protein-12 (ADAM-12) can be used differentiate EP from viable intrau

54 etalloprotease domain-containing protein 12 (ADAM-12) is upregulated in many human cancers and promot

55 Upregulation of ADAM-12, a novel member of the multifunctional ADAM fami

56 s critical for transcriptional repression of ADAM-12.

57 dentified a disintegrin and metalloprotease (ADAM)15 as a novel TRIF-interacting partner.

58 ADAM 17 (TNF-alpha converting enzyme, TACE) is a potenti

59 A fluorescence-based Adam 17 activity assay that cleaves pro-tumor necrosis f

60 h a short peptide substrate, the activity of Adam 17 showed different pH profiles.

61 ule, however, did not affect the activity of Adam 17 to its peptide substrate.

62 he reaction rate of pro-TNFalpha cleavage by Adam 17 was also reduced by a small molecule binding to

63 bited by an ADAM metallopeptidase domain 17 (Adam 17) active site inhibitor.

64 cy of the disintegrin and metalloproteinase (ADAM) 17 (SM22-Adam17(-/-)) were investigated in models

65 combinant a disintegrin and metalloprotease (ADAM) 17 cleaved the ectodomain of FcgammaRIIIA/CD16A an

66 A Disintegrin And Metalloproteinase (ADAM) 17 is one of the major sheddases involved in a var

67 inases, a disintegrin and metalloproteinase (ADAM)17 and ADAM10, are identified as enzymes that contr

68 AT augmentation therapy decreased neutrophil ADAM-17 activity and apoptosis in vivo and increased bac

69 talloproteinases (ADAMs), including ADAM-10, ADAM-17 and ADAM-33, which suggest that selective inhibi

70 se in expression and activity of ADAM-10 and ADAM-17 in old peripheral blood mononuclear cells compar

71 tion effort to identify potent and selective ADAM-17 inhibitors, starting with previously identified

72 In addition, ADAM-17 plays a key role in EGFR signaling and thus may

73 mpound 21, which showed an IC50 of 1.9 nM on ADAM-17 with greatly increased selectivity.

74 teinase domain-containing protein (ADAM)-10, ADAM-17, and ADAM-10 activities were measured with Senso

75 integrin and metalloproteases" (ADAM)-10 and ADAM-17, as demonstrated through the use of pharmacologi

76 nd is released in a soluble form (sALCAM) by ADAM-17-mediated shedding.

77 ich rely upon the cell surface protease TACE/ADAM-17.

78 asiveness, which is reduced by inhibitors of ADAM-17.

79 ormed with specific antibodies to ADAM-10 or ADAM-17.

80 ases (ADAMs), including ADAM-10, ADAM-17 and ADAM-33, which suggest that selective inhibitors might b

81 Moreover, our findings suggest that ADAMs 8, 9, and 10 could be targets for treatment of plu

82 duced expression of metalloproteases (MMP-9, ADAM-8), CC chemokines (CCL-20), CXC chemokines (IL-8, C

83 disintegrin and a metalloproteinase domain (ADAM) 9 is known to be expressed by monocytes and macrop

84 disease, in particular, decreased MMP-2 and ADAM-9 activities.

85 Taken together, stromal expression of ADAM-9 during melanoma development modulates the express

86 To analyze the role of stromal-derived ADAM-9 for the growth and survival of melanoma cells, we

87 However, the role of ADAM-9 in melanoma progression remains elusive.

88 In human melanoma, ADAM-9 is expressed in focalized areas of the tumor-stro

89 n of murine melanoma cells into the flank of ADAM-9(-/-) animals resulted in the development of signi

90 culture of melanoma cells in the presence of ADAM-9(-/-) fibroblasts led to increased melanoma cell p

91 creased amounts in culture supernatants from ADAM-9(-/-) fibroblasts.

92 itro coculture systems of melanoma cells and ADAM-9(-/-) fibroblasts.

93 X-induced generation of the soluble IL-6R by ADAM (a disintegrin and metallo) proteases enables IL-6

94 PMA-induced shedding was abrogated by an ADAM (A disintegrin and metalloprotease) 10 and 17 selec

95 Here we show that receptor cleavage by ADAM (A Disintegrin And Metalloprotease) metalloprotease

96 ADAMDEC1 (Decysin-1) is a putative ADAM (a disintegrin and metalloprotease)-like metallopro

97 Cleavage of membrane-anchored proteins by ADAM (a disintegrin and metalloproteinase) endopeptidase

98 to elucidate the role of key members of the ADAM (a disintegrin and metalloproteinase) enzyme family

99 ment is similar to proteins belonging to the ADAM (a disintegrin and metalloproteinase) family, known

100 Wild-type and Adam (A Disintegrin And Metalloproteinase) knockout mice

101 RECK release disinhibits ADAM (a disintegrin and metalloproteinase) protease-depe

102 e type-1 matrix metalloproteinase (MT1-MMP), ADAMs (a disintegrin domain and metalloproteinases), and

103 NFATc1, nuclear factor of activated T-cells; ADAM, a disintegrin and metalloprotease domain; OTM, ort

104 2 receptors are involved in melittin-induced ADAM activation.

105 n be significantly enhanced when a canonical ADAM active site with three zinc-coordinating histidine

106 a role for meprin beta in the regulation of ADAM activities.

107 studies reveal a mechanism for regulation of ADAM activity and offer a roadmap for its modulation.

108 hrough aberrant ADAM expression or sustained ADAM activity is linked to chronic inflammation, inflamm

109 her glycosylation plays a role in modulating ADAM activity, a tumor necrosis factor alpha (TNFalpha)

110 rough initiation of protein kinase C-induced ADAM activity.

111 s that a disintegrin and metalloproteinases (ADAMs) ADAM10 and ADAM19, together with gamma-secretase,

112 Six ADAMs (ADAM8, 9, 10, 15, 17, 19) were expressed in mouse

113 ies of "adisintegrin and metalloproteinase" (ADAMs), ADAMs with thrombospondin domains (ADAM-TS), and

114 affinity between LRP-1 and a number of MMPs, ADAMs, ADAMTSs, TIMPs and metalloproteinase/TIMP complex

115 The ADAM (adisintegrin and metalloproteinase) proteases are

116 echanism for Cad6B proteolysis involving two ADAMs, along with gamma-secretase, during cranial neural

117 ADAM and Apache Spark are a performant and productive pl

118 ing a complex genome analysis application to ADAM and Spark.

119 Adam and Vidal reported sea-floor depth increasing as th

120 Jean Adams and colleagues argue that population interventions

121 ghly cited 1999 Cancer Research article from Adams and colleagues was published during the period whe

122 Of importance, both ADAMs and gamma-secretase are expressed in the appropria

123 understanding of the regulatory mechanism of ADAMs and has general implications for membrane-protein

124 tional regulation is also performed by other ADAMs and how this process may be regulated.

125 er tested Zn(2+)-dependent metalloproteases (ADAMs and meprins).

126 ed mechanism to control receptor shedding by ADAMs and reveal functions for Lrigs in neuron migration

127 Therefore, both Adams and the miR-29 family represent therapeutic target

128 s through a disintegrin and metalloprotease (ADAM) and at one beta-site through BACE1.

129 families of disintegrin metalloproteinases (ADAMs) and ADAMs with thrombospondin repeats (ADAMTSs) p

130 MPs) and a disintegrin and metalloproteases (ADAMs) and stimulate pro-atherogenic responses, endothel

131 activates disintegrin-like metalloproteases (ADAMs) and that downstream events likely contribute to t

132 trix metalloproteinases (MMPs), adamalysins (ADAMs), and adamalysins with thrombospondin motifs (ADAM

133 ace1), A disintegrin and metalloproteinases (Adams), and presenilins (Psen).

134 pply evolved magmas to Mounts St. Helens and Adams, and possibly Rainier, and could contain approxima

135 Helens, Adams, and Rainier these pathways connect subduction-ind

136 posed describing the interactions of TSST-1, ADAMs, and the EGFR that lead to establishment of a proi

137 ADAMs are cell surface metalloproteases that control mul

138 This study shows that Adams are involved in renal fibrosis and are regulated b

139 ADAMs are members of the zinc metalloproteinase superfam

140 Proteolytically active ADAMs are responsible for ectodomain shedding of membran

141 ADAMs are transmembrane metalloproteases that control ce

142 A disintegrin and metalloproteinases (ADAMs) are a family of cell surface proteases that regul

143 A Disintegrin and Metalloproteinases (ADAMs) are the principal enzymes for shedding receptor t

144 Ps) and a disintegrin and metalloproteinase (ADAMs), are critical for regulating the inflammatory res

145 Proteomic analysis also revealed several ADAMs as putative meprin beta substrates.

146 ic Reactions and the initiation of the Roger Adams Award are discussed.

147 Among the six general AMP prediction tools-ADAM, CAMPR3(RF), CAMPR3(SVM), MLAMP, DBAASP and MLAMP-w

148 Significantly, ADAMs can be targeted to specific substrates on the cell

149 The cytoplasmic domain of ADAMs can regulate the proteolytic activity by controlli

150 Disintegrin metalloproteases (Adam) can manipulate the signaling environment, however,

151 ific intra- and intermolecular inhibitors of ADAM catalytic activity.

152 We used in vitro GalNAc-T enzyme and ADAM cleavage assays to demonstrate that shedding of at

153 We have previously shown that these ADAMs cleave a number of extracellular proteins and modi

154 Analysis of ADAM cognate substrates revealed that glycosylation is o

155 ng evidence indicates that overexpression of ADAMs could correlate with cancer progression.

156 but mesotrione-sensitive population (ACR for Adams County mesotrione-sensitive but atrazine-resistant

157 acological inhibitors and primary cells from ADAM-deficient mice we established that endogenous IL-6R

158 ADAM-dependent proteolysis occurs outside the plasma mem

159 ovel insights into the complex regulation of ADAM-dependent TNF shedding.

160 olecules that undergo ectodomain shedding by ADAMs [e.g., ligands and receptors from epidermal growth

161 We hypothesized that the ADAM enzymes expressed by cancer cells degrades IFN-gamm

162 In this issue of Blood, Adams et al provide evidence for an important novel func

163 Adams et al. in this issue of Immunity provide evidence

164 In an accompanying article, Adams et al. used a subsample of the National Institutes

165 See related article by Adams et al., Cancer Res 1999;59:2615-22Visit the Cancer

166 gulation of these processes through aberrant ADAM expression or sustained ADAM activity is linked to

167 proteases, the matrix metalloproteinase and ADAM families, as potential targets for anticoronavirus

168 s proteolytic activation by proteases of the ADAM family and BACE1.

169 d ADAM17 are the most studied members of the ADAM family in the gastrointestinal tract.

170 rs reported to date are not specific to this ADAM family member.

171 Among ADAM family members, ADAM10 stands out as particularly i

172 Slit-Robo repulsion, we have identified the Adam family metalloprotease Kuzbanian (Kuz).

173 hich is shed from cells after cleavage by an ADAM family metalloprotease, ADAM17 (TNFalpha-converting

174 Pericellular proteolysis by ADAM family metalloproteinases has been widely implicate

175 oteinase domain 10 (Adam10), a member of the ADAM family of cell membrane-anchored proteins, has been

176 ntified ADAM22, a non-protease member of the ADAM family of disintegrins, as a direct estrogen recept

177 n if this effect involves also modulation of ADAM family of metalloproteinases, which are responsible

178 oteases, the broad spectrum inhibitor of the ADAM family of proteases, tumor necrosis factor-alpha pr

179 AM-12, a novel member of the multifunctional ADAM family of proteins is linked to cancer, arthritis a

180 d shedding of cell-surface N-cadherin by the ADAM family protease ADAM10/Kuzbanian.

181 When compared with other members of the ADAM family, ADAMDEC1 displays some unusual features.

182 in of ADAMDEC1, like in other members of the ADAM family, confers catalytic latency.

183 membrane-associated metalloproteases of the ADAM family, leading to the shedding of their ectodomain

184 previously documented for inhibitors of the ADAM family.

185 of the a-disintegrin and metalloproteinase (ADAM) family are implicated in cancer cell proliferation

186 active A Disintegrin And Metalloproteinase (ADAM) family members.

187 rs of the A Disintegrin And Metalloprotease (ADAM) family of membrane-anchored metalloproteases are s

188 se of the A disintegrin and metalloprotease (ADAM) family, can mediate NKG2D ligand cleavage and this

189 of the 'Disintegrin and Metalloproteinase' (ADAM) family, controls vital cellular functions through

190 es in the A Disintegrin And Metalloprotease (ADAM) family.

191 of the A disintegrin and A metalloprotease (ADAM) family; members of this protein family are associa

192 MMP)- and a disintegrin and metalloprotease (ADAM)-family zinc metalloproteases markedly decreased bo

193 plementation of the XHMM algorithm using the ADAM framework and Apache Spark that incorporates novel

194 Similar increases in Adam gene expression also occurred in preclinical models

195 model renal fibrosis, we observed increased Adams gene expression that was blocked by oral administr

196 In the context of the Adam-Gibbs and random first-order transition models of g

197 t in cooperative strings, and we recover the Adam-Gibbs description of glassy dynamics.

198 fragility, we show that the validity of the Adam-Gibbs relation (relating configurational entropy to

199 rovide the first evidence for involvement of ADAMs in regulating developmental switch in responsivene

200 ronment, however, the role and regulation of ADAMs in renal fibrosis remain unclear.

201 However, the role of ADAMs in the chemoresistance of cancer cells has rarely

202 disintegrin and metalloproteinase proteins (ADAMs) in PNS myelination, but there is no evidence if t

203 es for A Disintigrin and Metalloproteinases (ADAMs), including ADAM-10, ADAM-17 and ADAM-33, which su

204 lpha or Avpr2 antagonists, namely SR49059 or ADAM, increased osteoblastogenesis, as did the genetic d

205 in multiple diseases, but no drugs based on ADAM inhibition exist.

206 in multiple diseases, but no drugs based on ADAM inhibition exist.

207 TAPI-1 (an ADAM inhibitor) completely abrogates all observed sheddi

208 We studied the effects of pharmacological ADAM inhibitors as well as ADAM10 and ADAM17 siRNA downr

209 Most of the ADAM inhibitors developed to date feature zinc-binding m

210 Most of the ADAM inhibitors developed to date feature zinc-binding m

211 tial as a general strategy for the design of ADAM inhibitors.

212 ADAM is able to index many commonly used file formats ge

213 lection among numerous substrates of a given ADAM is determined by ICD modification of the substrate.

214 ADAM is implemented using Java and supported on Linux.

215 The removal of the pro-domain of ADAMs is currently thought to depend on processing at a

216 ins by A disintegrin and metalloproteinases (ADAMs) is highly regulated, and its dysregulation has be

217 rsors by a-disintegrin-and-metalloproteases (ADAMs) is regulated with high substrate-specificity.

218 These findings can help in the discovery of ADAM isoform- and substrate-specific inhibitors.

219 t guidance errors of proprioceptive axons in ADAM knockouts that are consistent with enhanced respons

220 means of the biomechanical software platform ADAMS-LifeMOD.

221 target of A disintegrin and metalloprotease (ADAM)-mediated ectodomain shedding resulting in a solubl

222 mmary, we describe Tim-3 as novel target for ADAM-mediated ectodomain shedding and suggest a role of

223 smembrane protein Lrig2 negatively regulates ADAM-mediated guidance receptor proteolysis in neurons.

224 Our data indicate that ADAM-mediated shedding and corin autocleavage are import

225 -6R proteins phenocopying hyperactivation of ADAM-mediated shedding of IL-6R as single substrate.

226 inhibitor batimastat (BB94) or inhibition of ADAM metallopeptidase domain 10 (ADAM10) and ADAM17 with

227 Moreover, inhibition of the overexpressed ADAM metallopeptidase domain 10 (ADAM10) in the resistan

228 tetraspanin 33, and the alpha-toxin receptor ADAM metallopeptidase domain 10 (ADAM10) promotes juncti

229 trix metalloproteinase 2), MMP9, and ADAM10 (ADAM metallopeptidase domain 10) levels.

230 ected, the reaction could be inhibited by an ADAM metallopeptidase domain 17 (Adam 17) active site in

231 MerTK is susceptible to ADAM metallopeptidase domain 17 (ADAM17)-mediated cell-s

232 al cord lead concentration and expression of ADAM metallopeptidase domain 9 (ADAM9), reticulon 4 (RTN

233 y without known mechanism, such as ADAMTS13 (ADAM metallopeptidase with thrombospondin type 1 motif,

234 ains of A disintegrin and metalloproteinase (ADAM) metallopeptidases can act as highly specific intra

235 s study shows that the cytoplasmic domain of ADAM metalloproteases can perform essential functions in

236 f several a disintegrin and metalloprotease (ADAM) metalloproteases, and understanding the regulation

237 of a disintegrin and metalloprotease domain (ADAM) metalloproteases, including ADAM17.

238 studies demonstrate that ADAM10 is the major ADAM metalloproteinase responsible for the constitutive

239 We recently found that Xenopus ADAM13, an ADAM metalloproteinase, is required for activation of ca

240 nd messengers, and interact with Tolloid and ADAM metalloproteinases, thereby repressing their activi

241 C., Li, R., Adams, N., Winuthayanon, W., Hamilton, K.

242 posed by a father and two affected sibs with Adams Oliver syndrome (AOS) (OMIM 100300).

243 Adams-Oliver syndrome (AOS) is a rare developmental diso

244 Adams-Oliver syndrome (AOS) is a rare disorder character

245 OTCH1 variants in unrelated individuals with Adams-Oliver syndrome (AOS), a rare disease with major f

246 BPJ) in two independent families affected by Adams-Oliver syndrome (AOS), a rare multiple-malformatio

247 tigated a recognized developmental disorder, Adams-Oliver syndrome (AOS), characterized by the combin

248 (i) gain-of-function CdGAP mutants found in Adams-Oliver Syndrome patients strongly destabilize cell

249 function variants in DLL4 are known to cause Adams-Oliver syndrome, this is the first report of a hyp

250 Two patients demonstrated features of Adams-Oliver syndrome, with genetic testing identifying

251 screening agents for discovery of selective ADAM probes and therapeutics.

252 Because ADAM prodomains can act as specific inhibitors, we postu

253 e is important for the maturation of several ADAM proenzymes.

254 ain cleavage by meprin beta caused increased ADAM protease activities, as observed by peptide-based c

255 bone marrow-derived macrophages, meprin beta/ADAM protease interactions likely influence inflammatory

256 stion of which substrate features can affect ADAM protease specificity.

257 only a few reports of potential exosites in ADAM protease structures.

258 ntify the structural features that determine ADAM protease substrate specificity.

259 hat conformation plays a role in determining ADAM protease substrate specificity.

260 ne an endocytic recycling pathway needed for ADAM protease trafficking and regulation of cell-cell ju

261 AMDEC1 is unique by being the only mammalian ADAM protease with a non-histidine zinc ligand, having a

262 ADAM proteases are implicated in multiple diseases, but

263 extracellular matrix proteins related to the ADAM proteases but devoid of proteolytic activity.

264 ecule inhibitors and siRNA knockdown of both ADAM proteases confirmed these results.

265 Direct interaction of meprin beta and ADAM proteases could be shown by immunofluorescence micr

266 We found that all ADAM proteases tested (i.e., ADAM10, 12, and 17) signifi

267 ovel proteolytic pathway of meprin beta with ADAM proteases to control protease activities at the cel

268 ished protein half-life, whereas cleavage by ADAM proteases was not modified.

269 In contrast, without activation of ADAM proteases, IL-6 in complex with membrane-bound IL-6

270 A disintegrin and metalloprotease (ADAM) proteases are implicated in multiple diseases, but

271 ls the cleavage of the PTK7 ectodomain by an ADAM proteinase was coupled with the membrane type-1 mat

272 ad6B by a disintegrin and metalloproteinase (ADAM) proteins and gamma-secretase generates intracellul

273 pecific a disintegrin and metalloproteinase (ADAM) proteins inhibit reprogramming, and the disintegri

274 ADAMs rapidly modulate key cell signaling pathways in re

275 ADAMs regulate many cellular processes associated with i

276 vage by A-disintegrin and -metalloproteases (ADAMs) releases many important biologically active subst

277 As a disintegrin and metalloprotease (ADAM)s have been implicated in chemokine shedding, we so

278 termed the conserved stalk region "Conserved ADAM seventeen dynamic interaction sequence" (CANDIS).

279 demonstrate that intervening with endogenous ADAM sheddase modulatory mechanisms holds potential as a

280 mpede our understanding of context-dependent ADAM "sheddase" function and our ability to predictably

281 Although ADAMs showed substrate preference (ADAM17, TGFalpha and

282 macological compounds to the AMPK alpha/beta-ADaM site enabling activator screening.

283 In the eighteenth century, Daniel Bernoulli, Adam Smith and Jeremy Bentham proposed that economic cho

284 AM17 as major sheddases of Tim-3 as shown by ADAM-specific inhibitors and the ADAM10 pro-domain in HE

285 Potential exosites in ADAM structures have been reported, but no studies descr

286 rm of the Aneurysm Detection and Management (ADAM) study conducted by the Veterans Affairs Cooperativ

287 al, the Arginine Deiminase and Mesothelioma (ADAM) study, was conducted between March 2, 2011, and Ma

288 by the A Disintegrin And Metalloproteinase (ADAM) subfamily of proteases and in particular ADAM17.

289 lity-regulation controls release of numerous ADAM substrates.

290 mechanism underlying proenzyme maturation of ADAMs that is independent of processing at the previousl

291 lurant 0.5 mg was inferior to placebo in the ADAMs total score.

292 using the Anxiety Depression and Mood Scale (ADAMS) total score.

293 1) is a secreted protein that interacts with ADAM transmembrane proteins, and its mutations are linke

294 (ADAMs), ADAMs with thrombospondin domains (ADAM-TS), and Astacins are now recognized as key signali

295 se embryonic fibroblasts that lack different ADAMs, we show that induced cleavage of EGF ligands can

296 in the Aging, Demographic, and Memory Study (ADAMS) were evaluated for cognitive impairment using a c

297 itor of metalloproteinases 3, which inhibits ADAMs, were not.

298 adisintegrin and metalloproteinase" (ADAMs), ADAMs with thrombospondin domains (ADAM-TS), and Astacin

299 For ADAMs with ThromboSpondin domains (ADAMTSs), there are b

300 f disintegrin metalloproteinases (ADAMs) and ADAMs with thrombospondin repeats (ADAMTSs) play a cruci

301 Overexpression or depletion of either ADAM within premigratory neural crest cells prematurely