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1 ture to function relationship of a mammalian guanylate kinase.
2 esidues largely prevent GMP binding to yeast guanylate kinase.
3 3 domain, and a GUK domain with homology to guanylate kinase.
4 the GK domain in SAP97 encodes an authentic guanylate kinase.
5 ology motif 3, and a domain with homology to guanylate kinase.
6 h substrates and products could bind to free guanylate kinase.
7 ach other and 52-54% identity with the yeast guanylate kinase.
8 nnels and receptors, and membrane-associated guanylate kinases.
9 sequence similarity with low-molecular-mass guanylate kinases.
10 ity to CaM kinase II and membrane-associated guanylate kinases.
11 SAP90 family of membrane-associated putative guanylate kinases.
12 nylate kinase domains in membrane-associated guanylate kinases.
13 (TARPs) and PSD-95-like membrane-associated guanylate kinases.
14 itment domain-containing membrane-associated guanylate kinase 1 (CARMA1) and/or the Toll-like recepto
15 spase-recruitment domain membrane-associated guanylate kinase 1 (CARMA1) signalosome through the coor
16 K+") patient-derived cell lines and identify guanylate kinase 1 (GUK1), a guanosine diphosphate (GDP)
17 otein 1, adenosine deaminase-like protein 1, guanylate kinase 1, and nucleoside diphosphate kinase at
18 otein related to MAGUKs (membrane-associated guanylate kinases); (2) Mint1, a putative vesicular traf
19 ly, we show that MAGI-2 (membrane-associated guanylate kinase), a scaffold protein required for PTEN
20 es designed to lack either protein kinase or guanylate kinase activity are functional, indicating tha
21 indings demonstrate that membrane-associated guanylate kinase adaptor proteins can modulate ion chann
23 la enterica serovar Typhimurium, gmk encodes guanylate kinase, an essential enzyme involved in the sy
24 membrane complex with a membrane-associated guanylate kinase and AKAP5, which constitutively attenua
25 revealed that specific amino acid changes in guanylate kinase and in the beta and beta' subunits of R
27 The low molecular mass cytosolic forms of guanylate kinase are implicated primarily in the regulat
28 Most or all identified membrane-associated guanylate kinases are components of cell junctions, incl
29 analyzed the dynamic behavior of the enzyme guanylate kinase as it evolved into the GK protein inter
31 ands for the PSD-95 guanylate kinase domain, guanylate kinase-associated protein (GKAP) and MAP1A, ap
32 two-hybrid screening, a novel protein termed guanylate kinase-associated protein (GKAP) has been isol
35 nside the membrane; the scaffolding proteins guanylate kinase-associated protein and Shank lay 24-26
36 of a novel synaptic protein, termed GKAP for guanylate kinase-associated protein, that binds directly
37 partate receptor complex/membrane-associated guanylate kinase-associated signaling complex (NRC/MASC)
40 to an L27 domain in the membrane-associated guanylate kinase calcium/calmodulin-dependent serine kin
43 SD-95 is a member of the membrane-associated guanylate kinase class of proteins that forms scaffoldin
44 teraction, we have constructed a conditional guanylate-kinase-deficient Escherichia coli strain that
45 role of the Discs large/membrane-associated guanylate kinase (Dlg/MAGUK) family of scaffolding prote
46 itment Domain (CARD) and Membrane-associated GUanylate Kinase domain (MAGUK)-containing scaffold prot
48 nts revealed 2 binding surfaces on the beta4 guanylate kinase domain contributing to a 156 +/- 18 mic
49 a loss-of-function mutant mouse lacking the guanylate kinase domain of PSD-95 (PSD-95(GK)), we analy
50 A fragment comprising the SH3 domain and the guanylate kinase domain of synapse-associated protein 10
51 , 40% of the beta-SH3 domain, and 73% of the guanylate kinase domain of the putative membrane-associa
54 0-residue region within the highly conserved guanylate kinase domain that also directs AID binding.
55 ort polybasic segment at the boundary of the guanylate kinase domain that slows down channel inactiva
57 -Subunits contain one Src homology 3 and one guanylate kinase domain, flanked by variable regions wit
59 ethal mutations of MAGUKs often occur in the guanylate kinase domain, indicating a critical role for
60 action between the PSD-95-associated protein guanylate kinase domain-associated protein (GKAP) and dy
61 tamatergic postsynaptic complex, GKAP/SAPAP (guanylate kinase domain-associated protein/synapse-assoc
65 se at the dynamic interaction of PDZ and SH3-guanylate kinase domains in membrane-associated guanylat
66 t although the individual Src homology 3 and guanylate kinase domains in SAP97 can interact with the
68 ramolecular interactions between the SH3 and guanylate kinase domains play a role in the stability of
69 including L27, PDZ, Src homology (SH) 3, and guanylate kinase domains that aggregate adhesion molecul
71 large/zona occludens-1), Src homology 3, and guanylate kinase domains, which regulate signaling and p
79 ket that differ between MAGUKs and authentic guanylate kinase explain this lack of binding, as swappi
80 ally called CARD11) is a membrane-associated guanylate kinase family member that is required for T ce
81 a founding member of the membrane-associated guanylate kinase family of proteins containing PostSynap
82 he leading member of the membrane-associated guanylate kinase family of proteins, which are defined b
84 ession of members of the membrane-associated guanylate kinase family of synaptic scaffolding proteins
85 id system, we isolated a membrane-associated guanylate kinase family protein with multiple PDZ domain
87 ctor that belongs to the membrane-associated guanylate kinase family, a class of proteins that functi
88 (SAP97), a member of the membrane-associated guanylate kinase family, is believed to associate with A
90 Discs Large 1, a MAGUK (Membrane Associated Guanylate Kinase) family member that is the highly conse
91 s a member of the MAGUK (membrane-associated guanylate kinase) family of scaffolding proteins, hDlg i
92 s a member of the MAGUK (membrane-associated guanylate kinase) family that functions as neurexin kina
94 the presence of a functional, plasmid-borne guanylate kinase for growth under selective conditions.
95 es of this domain share 46-52% identity with guanylate kinases from yeast, Escherichia coli, human, m
96 ed Ca(v)beta containing only the AID-binding guanylate kinase (GK) domain could fully confer voltage
97 finity in vivo interaction of PSD-93 via its guanylate kinase (GK) domain with microtubule-associated
98 ved Src homology 3 (SH3) domain, a conserved guanylate kinase (GK) domain, and a connecting variable
99 phosphorylation of PSD-95 at Ser-561 in its guanylate kinase (GK) domain, which is mediated by the p
101 In contrast, disruptions of PDZ3, SH3, or guanylate kinase (GK) domains do not affect synaptic tar
102 raction between the Src homology 3 (SH3) and guanylate kinase (GK) domains of MAGUKs is thought to pl
103 in interaction motifs including PDZ, SH3 and guanylate kinase (GK) domains, and these binding sites m
107 -subunit identified src homology 3 (SH3) and guanylate kinase (GK) motifs in a tandem arrangement rem
108 95 (PSD-95/SAP-90) is a membrane associated guanylate kinase (GK) PDZ protein that scaffolds glutama
112 The R41M and K14M mutant enzymes of yeast guanylate kinase (GKy) were studied to investigate the e
113 e molecular interaction between (p)ppGpp and guanylate kinase (GMK), revealing the importance of this
117 3 (SH3) domain, and a region of homology to guanylate kinase (GUK); the structure of this core motif
119 proteins, members of the membrane-associated guanylate kinase homolog (MAGUK) protein family, which a
124 class of proteins called membrane-associated guanylate kinase homologs (MAGUKs), which are often conc
127 s a member of the MAGUK (membrane-associated guanylate kinase homologs) family of membrane-associated
128 he multivalent nature of membrane-associated guanylate kinase homologue (MAGUK) targeting, thus begin
131 ed CASK, a member of the membrane-associated guanylate kinase homologues family of adaptor proteins.
134 ecular mass and membrane-associated forms of guanylate kinase homologues, notably found in neuronal t
137 o assess the role of specific amino acids of guanylate kinase in structure, function, drug activation
138 MP) bound to wild type and Y78F mutant yeast guanylate kinase in the complexes GKy x Mg(II)ATP, GKy x
139 s of GMP bound to R41M and K14M mutant yeast guanylate kinase in the complexes GKy.MgATP, GKy.MgADP,
140 w perspectives for understanding the role of guanylate kinases in plant cell signalling pathways.
141 GPR30 interacted with membrane-associated guanylate kinases, including SAP97 and PSD-95, and prote
142 Published X-ray crystal structures of yeast guanylate kinase indicate that K14 is part of the "P" lo
143 itment domain-containing membrane-associated guanylate kinase, initiates a unique signaling cascade v
144 ssociated protein 102, a membrane-associated guanylate kinase interacting with NR2A but lacking palmi
145 (CLMP), occludin (OCLN), membrane-associated guanylate kinase inverted 1 (MAGI1), and MAGI2 mRNA expr
146 lysates, MAGI-2/S-SCAM (membrane-associated guanylate kinase inverted 2/synaptic scaffolding molecul
147 ule (S-SCAM; also called membrane-associated guanylate kinase inverted-2 and atrophin interacting pro
148 associates with MAGI-2 (membrane-associated guanylate kinase inverted-2), a protein also known as S-
152 s with many nucleotide-metabolizing enzymes, guanylate kinase is involved in antimicrobial and antine
155 is enzymatically much less active than yeast guanylate kinase, its kinase domain is shown to compleme
157 are formed by a Src homology 3 domain and a guanylate kinase-like (GK) domain connected through a va
158 n of the Src homology 3 (SH3) domain and the guanylate kinase-like (GK) domain in the COOH-terminal h
159 GukH binds the Src homology 3 (SH3) and guanylate kinase-like (GK) protein interaction domains o
160 hare a highly homologous membrane associated guanylate kinase-like (MAGUK) domain that binds to alpha
164 ivating protein (RapGAP), interacts with the guanylate kinase-like domain of PSD-95 and forms a compl
165 ily of proteins examined, GAKIN binds to the guanylate kinase-like domain of PSD-95 but not of p55.
166 in protein consisting of a carboxyl-terminal guanylate kinase-like domain, an SH3 domain, and three s
167 , a synaptic protein that interacts with the guanylate kinase-like domain, and unlike GKAP, the bindi
173 Deletion of PSD-95's Src homology 3 and guanylate kinase-like domains, as well as a point mutati
179 ween the Src homology 3 (SH3) domain and the guanylate-kinase-like (GUK) domain-prevented association
180 Lin-2 (mLin-2)/CASK is a membrane-associated guanylate kinase (MAGUK) and contains multidomain module
181 ement reminiscent of the membrane-associated guanylate kinase (MAGUK) class of scaffolding proteins.
182 adaptor proteins of the membrane-associated guanylate kinase (MAGUK) family and raises the possibili
183 ibrary yielded CARD11, a membrane-associated guanylate kinase (MAGUK) family member containing CARD,
184 compartmentalization and membrane-associated guanylate kinase (MAGUK) family molecular scaffolds func
185 n-110 is a member of the membrane-associated guanylate kinase (MAGUK) family of PDZ domain-containing
186 P-90) is a member of the membrane-associated guanylate kinase (MAGUK) family of proteins that assembl
187 s, the discs large (DLG)-membrane-associated guanylate kinase (MAGUK) family of scaffolding proteins
188 ptic density-95 (PSD-95) membrane-associated guanylate kinase (MAGUK) family of scaffolding proteins
192 teins that belong to the membrane-associated guanylate kinase (MAGUK) family, a class of proteins tha
194 ecruitment domain (CARD) membrane-associated guanylate kinase (MAGUK) protein 1/B-cell CLL-lymphoma 1
195 termined previously that membrane-associated guanylate kinase (MAGUK) protein discs large homolog 5 (
196 teins are members of the membrane-associated guanylate kinase (MAGUK) protein family and are likely t
197 of the Discs large (DLG)-membrane-associated guanylate kinase (MAGUK) protein family regulate these p
199 l of PMCA2b isolated the membrane-associated guanylate kinase (MAGUK) protein SAP97/hDlg as a binding
203 otein PSD-95 and related membrane-associated guanylate kinase (MAGUK) proteins assemble signal transd
206 t excitatory synapses by membrane-associated guanylate kinase (MAGUK) proteins regulates synapse deve
207 he zonula occludens (ZO) membrane-associated guanylate kinase (MAGUK) proteins ZO-1, -2, and -3.
208 e p55 Stardust family of membrane-associated guanylate kinase (MAGUK) proteins, was found in a tripar
210 he PDZ domain-containing Membrane-associated Guanylate Kinase (MaGUK) PSD93 as a direct ZDHHC14 inter
212 ptors and enzymes around Membrane Associated Guanylate Kinase (MAGUK) scaffold proteins are a paradig
215 ic member in a family of membrane-associated guanylate kinase (MAGUK) scaffolding proteins that inter
216 reported to bind to the membrane-associated guanylate kinase (MAGUK) scaffolding proteins, as well a
217 (hDlg), a member of the membrane-associated guanylate kinase (MAGUK) superfamily, interacts with K(+
218 yn-110, a novel membrane-associated putative guanylate kinase (MAGUK) that binds directly to N-methyl
219 ens-1) domain-containing membrane-associated guanylate kinase (MAGUK) that functions as a scaffold to
220 naptic density (PSD) and membrane-associated guanylate kinase (MAGUK)-associated signaling complexes
221 2B-calcineurin (CaN) to membrane-associated guanylate kinase (MAGUK)-linked AMPA receptors (AMPARs)
223 CASK is a member of the membrane-associated guanylate kinases (MAGUK) homologs, a family of proteins
227 nsity (PSD)-95 family of membrane-associated guanylate kinases (MAGUKs) are major scaffolding protein
229 ludens (ZO) subfamily of membrane-associated guanylate kinases (MAGUKs) are scaffolding molecules tho
232 dance of PSD-95 or other membrane-associated guanylate kinases (MAGUKs) drives the bidirectional chan
236 s with the three related membrane-associated guanylate kinases (MAGUKs) PSD-95/SAP90, PSD-93/chapsyn-
239 (discs large) family of membrane-associated guanylate kinases (MAGUKs) that are components of the po
240 require the function of membrane-associated guanylate kinases (MAGUKs) that contain the PDZ protein-
241 ctly bind to a family of membrane-associated guanylate kinases (MAGUKs) that regulate surface and syn
242 nits and are anchored by membrane-associated guanylate kinases (MAGUKs), but it is unknown whether pa
244 brain plasticity of two membrane-associated guanylate kinases (MAGUKs), SAP102 and PSD95, which form
251 e domain of the putative membrane-associated guanylate kinases module, and helix alpha3 of the alpha1
252 beta-interaction domain, membrane-associated guanylate kinases module, and the alpha1-subunit binding
253 id mechanism to identify not only functional guanylate kinase mutants but also those that result in d
254 nserved mLin-7 binding domain in addition to guanylate kinase, PDZ (postsynaptic density 95/discs lar
255 itment domain-containing membrane-associated guanylate kinase protein (CARMA)3 is specifically expres
256 t serine protein kinase; membrane-associated guanylate kinase protein (MAGI)-1, MAGI-2, and MAGI-3],
257 itment domain-containing membrane-associated guanylate kinase protein 1 (CARMA1)-B-cell lymphoma/leuk
259 , the only member of the membrane-associated guanylate kinase protein family that contains a Ca2+/cal
260 and other members of the membrane-associated guanylate kinase protein family, as well as Scribble.
262 , we have identified the membrane-associated guanylate kinase protein membrane palmitoylated protein
265 amily of synaptic MAGUK (membrane-associated guanylate kinase) proteins have been shown to interact,
266 single PDZ domain MAGUK (membrane-associated guanylate kinase) proteins that are expressed in all pri
267 tify novel MAGUK-family (membrane-associated guanylate kinase) proteins that are similar to Nagie oko
269 teins of the PSD-95-like membrane-associated guanylate kinase (PSD-MAGUK) family are vital for traffi
270 we show that PSD-95-like membrane-associated guanylate kinases (PSD-MAGUKs) mediate this synaptic tar
272 protein-97 (SAP97) is a membrane-associated guanylate kinase scaffolding protein expressed in cardio
273 occludens-1] domains of membrane-associated guanylate kinase scaffolding proteins PSD-93 or PSD-95.
274 nd recruitment of MAGUK (membrane-associated guanylate kinase) scaffolding proteins or NMDA receptors
275 major glutamate receptor membrane-associated guanylate kinase scaffolds expressed in the young superf
276 le is a common feature of membrane associate guanylate kinase scaffolds such as Dlg, and these result
278 ed sequence homology with the Src homology 3-guanylate kinase (SH3-GK) module of membrane-associated
279 t affinity for GMP but may have retained the guanylate kinase structure to accommodate a related regu
281 d inositol trisphosphate receptor-associated guanylate kinase substrate (IRAG, Mrvi1, and Jaw1L) are
282 lustering by cytoplasmic membrane-associated guanylate kinases such as postsynaptic density 95 (PSD-9
283 AGI) 3, a novel inverted membrane-associated guanylate kinase that localizes to epithelial cell tight
284 esent a new subfamily of membrane-associated guanylate kinases that allow for multiple targeting comp
285 n-binding domain found in membrane associate guanylate kinases that function in mitotic spindle orien
286 n in and of itself does not encode an active guanylate kinase, that it cannot be activated by its bin
289 th cDNA clones encoding enzymatically active guanylate kinase were isolated from mouse B-cell lymphom
290 binds to a PDZ domain of membrane-associated guanylate kinase with inverted orientation (MAGI) 3, a n
291 identify members of the membrane-associated guanylate kinase with inverted orientation (MAGI) and PS
292 scaffold protein called membrane-associated guanylate kinase with inverted orientation (Magi)-1.
293 ntaining protein MAGI-1 (membrane-associated guanylate kinase with inverted orientation protein-1) an
294 e homolog of GASP, i.e., membrane-associated guanylate kinase with inverted orientation-1 (MAGI-1), i
295 LPA(2) interacts with membrane-associated guanylate kinase with inverted orientation-3 (MAGI-3) an
296 TF, the association of "membrane-associated guanylate kinase-with inverted configuration" (MAGI)1-3
297 s, we found that loss of membrane associated guanylate kinase, WW and PDZ domain containing 2 and pro
298 ning to identify MAGI-2 (membrane associated guanylate kinase, WW and PDZ domain containing 2) as a n
299 ase-causing mutations in membrane-associated guanylate kinase, WW, and PDZ domain-containing 2 (MAGI2
300 similarity in amino acid sequence with yeast guanylate kinase (yGMPK), is the least characterized MAG