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1 te (PIP2) and phosphorylation of a conserved threonine residue.
2 membrane when phosphorylated at a conserved threonine residue.
3 orylation of nuclear SREBP-1c at a conserved threonine residue.
4 elated G-proteins have a conserved serine or threonine residue.
5 functional Ras GAPs, the GRD has a conserved threonine residue.
6 on by these enzymes was found to be only the threonine residue.
7 ly direct phosphorylation of the appropriate threonine residue.
8 single O-GlcNAc modification on a serine or threonine residue.
9 osphorylation of a conserved activation loop threonine residue.
10 pendent kinase (CDK) 2 at a highly conserved Threonine residue.
11 tyrosine (Y) residues in addition to serine/threonine residues.
12 orylation of conserved N-terminal serine and threonine residues.
13 peptides involves dehydration of serine and threonine residues.
14 on was clearly identified at both serine and threonine residues.
15 ating tryptophan, asparagine, glutamine, and threonine residues.
16 t of glycans to hydroxyl groups of serine or threonine residues.
17 egular outward-projecting parallel arrays of threonine residues.
18 n kinase PknB in vitro on one serine and six threonine residues.
19 tylglucosamine (GlcNAc) residue to serine or threonine residues.
20 PM and dephosphorylation of Art1 at specific threonine residues.
21 carries eight putative regulatory serine and threonine residues.
22 that attach ubiquitin to cysteine or serine/threonine residues.
23 es, including five phosphorylated serine and threonine residues.
24 e rings originate from cysteine, serine, and threonine residues.
25 ed GAG polysaccharides O-linked to serine or threonine residues.
26 horylation and O-GlcNAcylation of serine and threonine residues.
27 y for peptides containing multiple serine or threonine residues.
28 nd is regulated by phosphorylation of serine/threonine residues.
29 1 was phosphorylated on multiple serine and threonine residues.
30 edicted PP2C phosphatase specific for serine/threonine residues.
31 and the side-chain orientation angles of the threonine residues.
32 competes directly with phosphate for serine/threonine residues.
33 ively phosphorylated on serine and weakly on threonine residues.
34 osphorylation of the proline-directed serine/threonine residues.
35 I beta-turns stabilized by the aspartate and threonine residues.
36 phosphorylated endoglin on cytosolic domain threonine residues.
37 three 11-residue repeat units beginning with threonine residues.
38 gh phosphorylation of cytoplasmic serine and threonine residues.
39 iphilic ice-binding sites based on arrays of threonine residues.
40 dephosphorylation of TRPV1, specifically at threonine residues.
41 phosphorylation of NET occurs on serine and threonine residues.
42 ero-L-manno) and is beta-linked to serine or threonine residues.
43 ds between proline and phosphorylated serine/threonine residues.
44 ne residue that is alpha-linked to serine or threonine residues.
45 with and phosphorylated ATF4 at tyrosine and threonine residues.
46 omain of dense O-glycosylation on serine and threonine residues.
47 of ubiquitin oxyester formation on serine or threonine residues.
48 es with both phosphoacceptor site serine and threonine residues.
49 osphoric acid from phosphorylated serine and threonine residues.
50 osphorylate BIK1 at both tyrosine and serine/threonine residues.
51 lternatively observed on the same serine and threonine residues.
52 he phosphorylation of proteins on serine and threonine residues.
53 rotein receptor-related protein 6 (LRP6), at threonine residue 1479 (Thr1479) and serine residue 1490
56 tive activity through autophosphorylation at threonine residue 286 (Thr286) are thought to play a maj
57 lated by cyclin-dependent kinase 1 (CDK1) at threonine residues 345 and 487 in a cell cycle-dependent
61 X3.1 constructs with AD phosphorylation site threonine residues (89 and 93) mutated to glutamate were
62 biochemical evidence that a highly conserved threonine residue acts as a glutamate switch in the repl
64 irect phosphorylation of Cdc14 on serine and threonine residues adjacent to a nuclear localization si
69 it is phosphorylated on multiple serine and threonine residues and can be a target for phosphorylati
70 onfirmed the role of conserved extracellular threonine residues and demonstrated that FXYD7 protein,
72 phosphorylation at the Akt-regulating serine/threonine residues and induced prolonged nuclear accumul
73 catalyze both the dehydration of serine and threonine residues and the Michael-type additions of cys
74 ntly induce Vangl2 phosphorylation of serine/threonine residues and Vangl2 activities depend on its l
75 specifically counteracts phosphorylation on threonine residues, and consequently, we find that threo
80 strate that alanine substitution of a single threonine residue at position 61 (T61) in CD30v abrogate
83 oxygen species and phosphorylation of serine/threonine residues at sites in the C-terminus of the pro
84 phorylation by CKII on the identified serine/threonine residues at the N-terminal unstructured domain
85 itution mutants of the predicted beta-strand threonine residues became antagonists at the PAC1 recept
86 50cin lacks the almost universally conserved threonine residue believed to be involved in dioxygen ac
88 DKs that require phosphorylation of a serine/threonine residue by a CDK-activating kinase (CAK) for f
89 s is known about the glycosylation of serine/threonine residues by O-linked N-acetylglucosamine (O-Gl
94 of mouse (m)FFAR4 occurs at five serine and threonine residues clustered in two separable regions of
95 te Parkin, as the mutation of all serine and threonine residues conserved between Drosophila and huma
96 riptional oncoproteins at specific serine or threonine residues creates binding sites for the COP1 tu
99 phosphorylates PUB25 and PUB26 at conserved threonine residues, enhancing their E3 activity and faci
100 le-associated protein tau at specific serine/threonine residues found in paired helical filaments (PH
101 horylation of tau protein at specific Serine/Threonine residues found in paired helical filaments, su
102 posttranslational modification of serine and threonine residues functions as a critical regulator of
103 beta), we find that mutation of this surface threonine residue impacts critical Polbeta protein-prote
104 pathway, p38 MAPK, phosphorylates a critical threonine residue in ATF6 upstream of its DNA binding do
107 s well as two analogues of P-A1 in which the threonine residue in P-A1 was replaced with l-2,3-diamin
109 vivo could result in O-glycosylation of the threonine residue in question and that this could boost
112 nd rate-limiting phosphorylation occurs at a threonine residue in the activation loop (AL), which tri
113 also show that YopJ causes acetylation of a threonine residue in the activation loop of both the alp
114 activated by phosphorylation at a conserved threonine residue in the activation loop of the kinase d
115 e A-type gamma-aminobutyric acid receptor, a threonine residue in the second transmembrane domain is
116 actin assembly by AMPylation of a conserved threonine residue in the switch 1 region of Rho GTPases.
118 strong H-bonds serve to stabilize serine and threonine residues in hydrophobic environments while con
124 ost-translational modification of serine and threonine residues in nuclear and cytoplasmic proteins,
126 method allows for isomeric identification of threonine residues in peptides of arbitrary sequence.
127 indicate that phosphorylation of serine and threonine residues in proline-rich sequences induces a c
128 ngle N-acetylglucosamine sugar to serine and threonine residues in proteins by the enzyme O-linked be
130 co plants BRI1-FLAG became phosphorylated on threonine residues in response to brassinolide applicati
131 acetylglucosamine (O-GlcNAc) onto serine and threonine residues in response to stimuli or stress anal
133 ave evolved to target adjacent and essential threonine residues in switch region I of immunity-relate
134 ds to phosphorylated proline-directed serine/threonine residues in target proteins and isomerizes cis
136 me A (CoA) to modify the critical serine and threonine residues in the activation loop of MAPKK6 and
137 strate that phosphorylation of two conserved threonine residues in the activation loop of the kinase
139 singly or doubly phosphorylated at serine or threonine residues in the C-terminal sequence SSATDHT (a
140 All of the observed mutations altered serine/threonine residues in the GSK3beta binding domain in exo
141 that a poxvirus kinase phosphorylates serine/threonine residues in the human small ribosomal subunit
143 dentified several phospho-serine and phospho-threonine residues in the known TLR pathway kinases, Int
144 ignaling and that the presence of serine and threonine residues in the PAR2 C-tail hinder constitutiv
145 is revealed that a highly conserved layer of threonine residues in the pore conveys a basal K(+) sele
147 sst2A phosphorylation occurs on serine and threonine residues in the third intracellular loop and c
148 ionally important mutations of glutamine and threonine residues in the TM domain on its structure, pr
152 dopsis seedlings, whereas phosphorylation of threonine residues increased rapidly and then remained c
153 that catalyzes O-GlcNAcylation of serine or threonine residues, interacts with UBN1, modifies HIRA,
155 ent of 566 RND transporters showed that this threonine residue is conserved in about 96% of cases.
159 lucosamine (O-GlcNAc) modification of serine/threonine residues is an abundant posttranslational modi
160 Pah1 phosphorylation on multiple serine/threonine residues is complex and catalyzed by diverse p
163 ed with N-acetyl-galactosamine on serine and threonine residues, is regulated by the substrate specif
166 ptor at the so-called T6' ring, wherein five threonine residues line the permeation pathway of the pe
168 but depends on phosphorylation of the serine/threonine residues located in the C-terminal domain of P
169 tion sites, including a conserved cluster of threonine residues located in the N-terminus of the prot
171 ce-binding proteins, which present arrays of threonine residues (matched to the ice lattice) that ord
172 have hydroxyl groups of specific serine and threonine residues modified by the monosaccharide N-acet
174 In addition to disruption of key serine and threonine residues, mutations are frequently reported in
178 f N-Acetylglucosamine (GlcNAc) on serine and threonine residues (O-GlcNAcylation) is an essential pro
179 on by which GlcNAc is attached to the serine/threonine residues of a protein via an O-linked glycosid
182 sylation (O-GlcNAcylation) of the serine and threonine residues of cellular proteins is a dynamic pro
183 fication on hydroxyl groups of serine and/or threonine residues of cytosolic and nuclear proteins.
184 c) sugar moiety to hydroxyl groups of serine/threonine residues of cytosolic and nuclear proteins.
185 ynamic and reversible modification of serine/threonine residues of different cellular proteins cataly
186 Ac moiety from UDP-GlcNAc to specific serine/threonine residues of hundreds of nuclear and cytoplasmi
187 a-N-acetylglucosamine (GlcNAc) to serine and threonine residues of intracellular proteins (O-GlcNAc),
188 GlcNAc) modification found on the serine and threonine residues of intracellular proteins is an induc
189 iology through phosphorylation of serine and threonine residues of many proteins in most cell types.
190 inkage of beta-N-acetylglucosamine to serine/threonine residues of membrane, cytosolic, and nuclear p
191 rmal conditions, the proline-directed serine/threonine residues of neurofilament tail-domain repeats
192 n role in adding beta-O-GlcNAc to serine and threonine residues of nuclear and cytoplasmic proteins,
193 tion of an N-acetylglucosamine to serine and threonine residues of nuclear and cytosolic proteins (O-
194 OGTs add a GlcNAc monosaccharide to serine/threonine residues of nuclear and cytosolic proteins.
195 samine (termed O-GlcNAcylation) on serine or threonine residues of nuclear or cytoplasmic proteins se
196 cetylglucosamine beta-O-linked to serine and threonine residues of nucleocytoplasmic proteins (O-GlcN
197 posttranslational modification of serine and threonine residues of nucleocytoplasmic proteins by beta
201 mes: OGT, which transfers O-GlcNAc to serine/threonine residues of numerous cellular proteins, and TE
202 lglucosamine sugar molecule on serine and/or threonine residues of protein chains is referred to as O
204 T), which attaches O-GlcNAc to serine and/or threonine residues of proteins and by O-GlcNAcase, which
206 the addition of a GlcNAc group to serine and threonine residues of TET proteins and thereby decreases
207 Our results suggest C-terminal serine and threonine residues of the FPR represent a combinatorial
210 S could act to covalently modify a conserved threonine residue on Rho, Rac, and Cdc42 with adenosine
211 n-dependent kinase 1 (CDK1) phosphorylated a threonine residue on the catalytic subunit of the phosph
212 N-acetylglucosamine (O-GlcNAc) at serine and threonine residues on myriad nuclear and cytoplasmic pro
214 pectrometric identification of 17 serine and threonine residues on SHIP1 as being phosphorylated by P
216 rylation of tau and APP on certain serine or threonine residues preceding proline affects tangle form
219 ng triggers transphosphorylation of critical threonine residues proximal to the CaM-binding site lead
220 amine linkage (O-GlcNAcylation) to serine or threonine residues regulates numerous biological process
221 -N-acetylglucosamine (O-GlcNAc) to serine or threonine residues regulates numerous metazoan cellular
222 clear and cytoplasmic proteins at serine and threonine residues, regulates some aspects of mitotic ch
223 ed a surprisingly high substitution rate for threonine residues, resulting in a reduction of threonin
226 the RD kinase, PktA5, autophosphorylated on threonine residue(s) and phosphorylated the artificial s
227 kinase cascade, which phosphorylates MrpC on threonine residue(s) located in its extreme amino-termin
230 phosphorylating highly conserved serine and threonine residues (S359/T360) within the activation loo
231 (rich in proline, glutamic acid, serine, and threonine residues) sequence in NFkappaB stripping, a mu
232 more than 50 phosphorylated IRS1 serine and threonine residues (Ser(P)/Thr(P) residues) in IRS1 from
233 N-terminal region that is rich in serine and threonine residues, several of which are reportedly phos
234 BC membranes reveals 9 phosphorylated serine/threonine residues, suggesting that activation of atNHE1
235 ed by phosphorylation of the most C-terminal threonine residue, switching them from an activated to a
237 ally occluded tyrosine residues and a distal threonine residue (T187), triggering degradation of p27.
238 t casein kinase 2 phosphorylates a conserved threonine residue (T22) in alpha helix-1 of the yeast Hs
242 Using mass spectrometry, we identified a threonine residue, T346, as the main autoacetylation sit
243 ty was observed with a mutant of a conserved threonine residue, T370S, also implicated to participate
244 ls is the phosphorylation status of a single threonine residue (T389) within the extensive ( approxim
245 ence that PKC eta phosphorylates occludin on threonine residues (T403 and T404) and plays a crucial r
246 effect of CaMKII was abolished by mutating a threonine residue (T425) at a consensus CaMKII phosphory
247 sphorylates the Par-1 kinases on a conserved threonine residue (T595) to regulate localization and ki
248 PLK1 phosphorylates NDR1 at three putative threonine residues (T7, T183 and T407) at mitotic entry,
249 P2X7R, a loop insertion (residues 73-79) and threonine residues T90 and T94, are required for high af
250 ce that Akt-mediated phosphorylation of USP8 threonine residue T907 contributes to USP8 stability.
251 with the carbonyl oxygen at C4, a conserved threonine residue that forms hydrogen bonds with N5, and
252 ydrogen bonds with N5, and another conserved threonine residue that forms hydrogen bonds with the car
253 eoformans crystal structure, in particular a threonine residue that may serve as an additional point
254 TNF-alpha induced ERM phosphorylation on the threonine residue that required activation of p38, PKC i
255 ciniphila cleaves N-terminally to serine and threonine residues that are modified with (preferably as
256 IRG, and 2) it alters the orientation of two threonine residues that are targeted by the Toxoplasma S
257 ct with proteins phosphorylated on serine or threonine residues that precede prolines (pS/T-P), such
258 ically highly non-random gain of serines and threonines, residues that are potential substrates of po
259 e in the peptide core instead of a serine or threonine residue, the inclusion of a non-heme iron, alp
260 tosolic G6PD6 on an evolutionarily conserved threonine residue, thereby stimulating its activity.
262 n, but phosphorylation of a highly conserved threonine residue (Thr(328)) in the activation loop is t
263 AMP or ADP binding and phosphorylation of a threonine residue (Thr-172) within the activation loop o
264 factor that is phosphorylated on a critical threonine residue (Thr-72) by the Ras/MAPK pathway in th
266 he mediator Mrc1 function to phosphorylate a threonine residue, Thr(11), in the SQ/TQ domain of Cds1.
269 Cdr2 through phosphorylation of a conserved threonine residue (Thr166) in the activation loop of the
270 mutagenesis of Ee;CDKF;1 indicated that two threonine residues (Thr291 and Thr296) were mutually res
271 The specific contributions of a conserved threonine residue (Thr380) to autoprocessing and hydrola
273 proteins are phosphorylated on this critical threonine residue through TNF-alpha-induced activation o
275 esidue and the PTX molecule, we mutated this threonine residue to serine, valine, and tyrosine to cha
278 s of individual and combinatorial serine and threonine residues to internalization, desensitization,
279 rtance of individual and combined serine and threonine residues to these processes is not well unders
280 osphorylation, which primarily occurred on a threonine residue, was accompanied by a 50% decrease in
281 some organization, phosphorylated serine and threonine residues were identified and changed to alanin
282 To assess the loop's role in catalysis, two threonine residues were mutated to alanine: QFR Thr-A244
283 94R) induce dephosphorylation of occludin on threonine residues, whereas active PKC eta elevates occl
284 t 2.4-A resolution, reveals a phosphorylated threonine residue, which provides clues about the cataly
285 the phosphorylation of several nearby serine/threonine residues, which constitute a phosphorylation h
287 ay facilitate the glycosylation of serine or threonine residues, which occur in sequence contexts tha
288 e non-canonical H-bond formed by a serine or threonine residue whose hydroxyl side chain H-bonds to a
289 transmembrane helices contain serine and/or threonine residues whose side chains form intrahelical H
290 ified by O-linked glycosylation of serine or threonine residues with beta-N-acetylglucosamine (O-GlcN
291 tudy the rotational energy profiles of these threonine residues with the use of molecular mechanics (
292 hosphorylated by CKII on multiple serine and threonine residues, with the former being major sites.
294 riggering Cdk2-mediated phosphorylation of a threonine residue within the flexible C-terminus of p27.
297 protein kinase that phosphorylates serine or threonine residues within extracellular cadherin domains
298 Subsequently, phosphorylation of serine/threonine residues within five repeating signature PPPSP
299 asmic proteins are glycosylated at serine or threonine residues within the specific three-amino acid
300 sulted in the identification of eight serine/threonine residues within the third cytoplasmic loop of