ライフサイエンスコーパス: ADAM

1 erial.ac.uk/bioinfsupport/resources/software/adam.

2 receptor) to chymotrypsin/trypsin or soluble ADAM.

3 e melt source region lies east towards Mount Adams.

4 hat is important for the activation of these ADAMs.

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

6 evertheless the principal sheddase when both ADAMs 10 and 17 are present.

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

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

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

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

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

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

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

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

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

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

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

22 adherin cleavage is regulated by a PKC-alpha-ADAM-10 cascade in GBM cells and may be involved in medi

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 cells with PMA induced the translocation of ADAM-10 to the cell membrane, the site at which N-cadher

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

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 such activity was seen in the placenta where ADAM-12 expression is high.

41 ng protein activity in several tissues where ADAM-12 expression is low while no such activity was see

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

58 s critical for transcriptional repression of ADAM-12.

59 f constitutive low-level expression of human ADAM-12.

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

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

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

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

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

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

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

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

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

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

70 ta1 binds a disintegrin and metalloprotease (ADAM) 17, a metalloenzyme that catalyzes ectodomain shed

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

72 Using a disintegrin and metalloprotease (ADAM)-17 radiation chimeric mice, we demonstrate for the

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

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

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

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

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

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

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

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

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

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

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

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

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

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

87 Because ADAM-8 is capable of producing the fibronectin neoepitop

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

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

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

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

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

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

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

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

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

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

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

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

100 In vascular smooth muscles, KK stimulates ADAM (a disintegrin and metalloprotease) 17 activity via

101 binding disintegrin-like domain found in the ADAM (a disintegrin and metalloprotease) family of prote

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

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

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

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

106 Like other members of the ADAM (a disintegrin and metalloproteinase) family, the i

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

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

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

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

111 2 receptors are involved in melittin-induced ADAM activation.

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

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

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

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

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

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

118 One of such non-proteinase ADAMs, ADAM22, acts as a receptor on the surface of the

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

120 The ADAM (adisintegrin and metalloproteinase) proteases are

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

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

123 Jean Adams and colleagues argue that population interventions

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

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

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

127 n, we discovered that ligand cleavage by MMP/ADAMs and HB-EGF expression is required for activation o

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

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

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

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

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

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

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

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

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

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

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

139 ADAMs are cell surface metalloproteases that control mul

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

141 ADAMs are members of the zinc metalloproteinase superfam

142 Proteolytically active ADAMs are responsible for ectodomain shedding of membran

143 ADAMs are transmembrane metalloproteases that control ce

144 a disintegrin and metalloproteinase domain (ADAM) are important in neuroinflammation, and recent stu

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

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

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

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

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

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

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

152 analysis detected the presence of a typical ADAM catalytic active site (HEXXHXXGXXHD).

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

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

155 We propose that in addition to exposing the ADAM cleavage site, activating N1 conformational changes

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

157 Analysis of ADAM cognate substrates revealed that glycosylation is o

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

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

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

161 on of HB-EGF expression and increases in MMP/ADAM-dependent HB-EGF cleavage are responsible for prote

162 ADAM-dependent proteolysis occurs outside the plasma mem

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

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

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

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

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

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

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

170 The spatial organization of the ADAM extracellular segment and its influence on the func

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

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

173 Mimicry of the ADAM family disintegrin-like domain by HCMV gB represent

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

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

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

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

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

179 Pericellular proteolysis by ADAM family metalloproteinases has been widely implicate

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

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

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

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

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

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

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

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

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

189 previously documented for inhibitors of the ADAM family.

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

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

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

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

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

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

196 al solute concentration that incorporate the Adams-Fujita assumption for composition-dependence of ac

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

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

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

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

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

202 Adam has autonomously generated functional genomics hypo

203 segment and its influence on the function of ADAMs have been unclear.

204 We found that ADAM identified adaptive mutations in laboratory-evolved

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

220 ADAM is implemented using Java and supported on Linux.

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

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

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

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

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

226 means of the biomechanical software platform ADAMS-LifeMOD.

227 Accordingly, we sought to characterize ADAM-like molecules in the fungal opportunistic pathogen

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

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

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

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

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

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

234 mapping, we identified null mutations in the ADAM metallopeptidase domain 9 (ADAM9) gene in four cons

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

236 detected two BMD candidate genes, ADAMTS18 (ADAM metallopeptidase with thrombospondin type 1 motif,

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

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

239 DAM10 and ADAM17 expression, suggesting that ADAM metalloproteases are required for P2Y(2)R-mediated

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

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

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

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

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

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

246 separate complexes of alkenyldiarylmethane (ADAM) nonnucleoside reverse transcriptase inhibitors (NN

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

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

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

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

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

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

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

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

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

256 ated "a disintegrin and metalloproteinases" (ADAMs) promote tumorigenesis by cleaving extracellular m

257 egative regulatory region (NRR) that enables ADAM protease cleavage at a juxtamembrane site that othe

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

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

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

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

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

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

264 ADAM proteases are implicated in multiple diseases, but

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

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

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

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

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

270 9-bp partial sequence with homology to known ADAM proteins, the full-length PcADAM sequence was obtai

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

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

273 ADAMs rapidly modulate key cell signaling pathways in re

274 ADAMs regulate many cellular processes associated with i

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

276 To describe Adam's research, we have developed an ontology and logic

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 ntials" neoclassical theory, originally from Adam Smith).

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

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

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

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

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

288 lity-regulation controls release of numerous ADAM substrates.

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

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

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

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

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

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

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

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

297 e report the development of Robot Scientist "Adam," which advances the automation of both.

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

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

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