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1 itates metal coordination by a non-canonical tyrosine residue.
2 is a covalent linkage of TOP1 with DNA via a tyrosine residue.
3 preference for 2'-deoxyribosyl groups have a tyrosine residue.
4 e ATP-binding template is blocked by a bulky tyrosine residue.
5 no nucleophilic involvement of the enzymatic tyrosine residue.
6 ent N-Calpha bond cleavage N-terminal to the tyrosine residue.
7 regulated by the phosphorylation of a single tyrosine residue.
8 mo phosphorylation on a conserved C-terminal tyrosine residue.
9 involving this carboxylate and the following tyrosine residue.
10 R3/PYL8, which are characterized by a unique tyrosine residue.
11 n conjugation of PDI possibly at active site tyrosine residues.
12 scribe a voltage sensor that is comprised of tyrosine residues.
13 s as well as chromatin modifiers at critical tyrosine residues.
14 hlorination of tryptophan and bromination of tyrosine residues.
15 activity by phosphorylating their C-terminal tyrosine residues.
16 ecycling motif and all four STAT3-recruiting tyrosine residues.
17  Gads, and PLCgamma1 through its four distal tyrosine residues.
18 pon ligand binding by phosphorylation on its tyrosine residues.
19 es, and acyl adducts with lysine and several tyrosine residues.
20 dditional posttranslational modifications at tyrosine residues.
21 ng reversible phosphorylation of proteins on tyrosine residues.
22 osphorylation of the PDGFbetaR at particular tyrosine residues.
23  cross-linking of chorion proteins via their tyrosine residues.
24 depends upon phosphorylation of its multiple tyrosine residues.
25 sformations arising from oxidative stress of tyrosine residues.
26 via reduced phosphorylation of specific EGFr tyrosine residues.
27 ate, and hydrogen bonding to two active site tyrosine residues.
28 ic and reversible phosphorylation of protein tyrosine residues.
29 osttranslationally sulfated at two conserved tyrosine residues.
30 ic relevance of CD2AP phosphorylation of the tyrosine residues.
31 enesis to define the specific phosphorylated tyrosine residues.
32 ia an NPP7-specific aromatic box composed of tyrosine residues.
33 ion, which is inhibited by mutation of three tyrosine residues.
34 patially arranged redox-active tryptophan or tyrosine residues.
35 e of the Jak2(FF/FF) mouse line reveals that tyrosine residues 1007/1008 are absolutely essential for
36  targeted mutation of phosphorylated nephrin tyrosine residues 1176 and 1193 abrogated the actions of
37 fically regulates p130Cas phosphorylation at tyrosine residue 128 (Y128) in colorectal cancer (CRC) c
38 e progression by phosphorylation of Cdc28 at tyrosine residue 19.
39 y epidermal growth factor receptor (EGFR) at tyrosine residues 3, 7, and 198.
40 re, activated Fyn phosphorylated PKCdelta at tyrosine residue 311, contributing to an inflammogen-ind
41 bited ZAP-70 variant in which two regulatory tyrosine residues (315 and 319) in the SH2-kinase linker
42                              There are three tyrosine residues (32, 91, and 96) clustered in the dime
43 enous anesthesia, we have used mice in which tyrosine residues 365/7 within the gamma2 subunit are mu
44 L fusion kinase phosphorylate human RAD51 on tyrosine residues 54 and 315.
45                       We have identified the tyrosine residues 572, 591, and 919 of FLT3 as phosphory
46 n kinase (FAK) and phosphorylation of FAK at tyrosine residues 576/577 and 925 were required for Lyn-
47 o-incubated with the IGF-1R kinase indicated tyrosine residues 60, 133, and 250 in PCNA as IGF-1R tar
48 ition blocked VE-cadherin phosphorylation at tyrosine residue 685 and the concomitant formation of bu
49 ion interface to a region around two surface tyrosine residues 71 and 73 and an adjacent prominent lo
50 imerization that releases the autoinhibitory tyrosine residue, a mechanism conserved in unrelated kin
51 , we find that both antibodies present a key tyrosine residue, albeit on different chains, that inser
52 k can be posttranslationally sulfated at two tyrosine residues, albeit as a mixture of sulfated varia
53                        Basic amino acids and tyrosine residues along this entry channel are predicted
54 ions can influence the redox reactivity of a tyrosine residue and how PCET mechanisms can be tuned by
55 rowth factor receptor; however, the specific tyrosine residue and the functional implication of this
56 orylated on one or two structurally occluded tyrosine residues and a distal threonine residue (T187),
57 ncing phosphorylation of specific C-terminal tyrosine residues and activation of downstream signaling
58 -stimulated phosphorylation of specific EGFr tyrosine residues and activation of ERK but not Akt-1.
59  demonstrate that both nitration of specific tyrosine residues and interaction of nitric oxide (NO) w
60 nal covalent oxidative modifications on four tyrosine residues and one tryptophan residue of hemopexi
61 ester bonds between the DNA 3'-phosphate and tyrosine residues and plays a major role in the repair o
62 C headgroups via cation-pi interactions with tyrosine residues and suggest that cation-pi interaction
63 calisation was observed between RNS-modified tyrosine residues and the chemokine CCL2 in diseased kid
64 ght on the distinct nature of these modified tyrosine residues, and provides a physical-chemical foun
65 nt mutagenesis of the PTB domain and the CH1 tyrosine residues, and successive substitution of these
66              Cx32 contains two intracellular tyrosine residues, and tyrosine phosphorylation of Cx32
67               The proteins with an unnatural tyrosine residue are catalytically competent.
68 avin adenine dinucleotide from a neighboring tyrosine residue are used as a sensitive probe of the fu
69 reast tumors in vivo, whereas all three ShcA tyrosine residues are required for efficient breast canc
70                                              Tyrosine residues are sensitive to oxidation and can be
71 tracytoplasmic domain, there are 2 conserved tyrosine residues arranged in a noncanonical immunorecep
72 e revealed that IL-10Rbeta uses a network of tyrosine residues as hydrophobic anchor points to engage
73 gh a 2-fork plug made of an isoleucine and a tyrosine residue at +3 and +8 positions, respectively; a
74 y required for binding to the phosphorylated tyrosine residue at codon 774 of c-Cbl, but is also esse
75 robe, Abeta(1-16)(Y10W), by substituting the tyrosine residue at position 10 in the hydrophilic domai
76 Collectively, these results suggest that the tyrosine residue at position 16 is necessary to constrai
77                                          The tyrosine residue at position 169 is strictly conserved a
78              Within the beta2-alpha2 loop, a tyrosine residue at position 169 is strictly conserved a
79 based activation motif (ITAM) phosphorylated tyrosine residue at position 204 in the tail of the immu
80 al analysis leads to identification of a key tyrosine residue at the calponin homology (CH) domain of
81 he -7 to -4 binding sites and suggest that a tyrosine residue at the tunnel entrance of HirCel7A may
82  importance because it binds to the critical tyrosine residues at the C terminus of PSTPIP2, which is
83 imerizes, followed by autophosphorylation of tyrosine residues at the intracellular domain.
84 transfected with a mutant caspase-8 in which tyrosine residues at Tyr397 or Tyr465 are replaced by no
85 peptide comprising alternating glutamate and tyrosine residues binds more tightly, which is consisten
86 linked via the oxidative quinone ring of the tyrosine residue by aryl-alkylamine addition or aryloxy
87 1, however, phosphorylation of a neighboring tyrosine residue by Src family kinases disrupts COP1 bin
88 tion of PAK1 required the phosphorylation of tyrosine residues by Etk/Bmx and protein kinase A (PKA)
89 n the discovery of CD31's 2 intracytoplasmic tyrosine residues called immunoreceptor tyrosine inhibit
90                                              Tyrosine residues can act as redox cofactors that provid
91 id gland via the secretory pathway, multiple tyrosine residues can become iodinated to form mono-iodo
92                       We show here that UL37 tyrosine residues conserved among all alphaherpesviruses
93 , also affecting exon 14, that substituted a tyrosine residue critical for MET receptor turnover and,
94 that posttranslational sulfation of specific tyrosine residues crucially modulates potency.
95 idues in Src homology 2 (SH2) domain and one tyrosine residue each in calponin homology 1 (CH1) domai
96  of CD300a depends on the phosphorylation of tyrosine residues embedded in ITIMs of the cytoplasmic t
97 ition, signaling downstream of specific ShcA tyrosine residues facilitates the survival, vascularizat
98 mon pathway to sulfate CCR5 on extracellular tyrosine residues, facilitating CCR5 recognition by the
99 onstrates the importance of domain interface tyrosine residues for interaction of small molecules wit
100 nant negative GAB1 mutants lacking canonical tyrosine residues for SHP2 and PI3K interactions or lent
101 oplasmic tail of LAT, including the critical tyrosine residues for signal propagation.
102   Finally, we show that the highly conserved tyrosine residue found in the vSAg TGXY motif is require
103 a T cell receptor stimulation time course on tyrosine residues found on upstream signaling proteins (
104 tyr at potentials high enough to oxidize the tyrosine residues have allowed the electrooxidation of N
105 ation, and nitrosylation of thiol groups and tyrosine residues, have received comparatively little at
106  Specifically, phenylalanine, tryptophan and tyrosine residues highly populate the paratope of the an
107  the importance of a catalytic glutamate vs. tyrosine residue in determining the outcome of the reduc
108 sensing agonists involves a highly conserved tyrosine residue in helix VI.
109 ween the LNK SH2 domain and a phosphorylated tyrosine residue in KIAA0157 (Abraxas2), a unique and de
110 vator of transcription 3 (STAT3) on a single tyrosine residue in response to growth factors, cytokine
111 C-IIA) as being phosphorylated in a specific tyrosine residue in response to L. monocytogenes infecti
112 we report that phosphorylation of a specific tyrosine residue in STING by the epidermal growth factor
113 onstrate that mutation of a single conserved tyrosine residue in the ankyrin-binding motif of both Ca
114 luorosulfate probe 1 reacts with a conserved tyrosine residue in the ligand-binding site of a subset
115  production by pDC is dependent on an intact tyrosine residue in the Ly49Q cytoplasmic ITIM.
116 for anti-HCV activity, whereas the conserved tyrosine residue in the N-terminal domain of IFITM2 and
117 or interaction with alpha2, with a conserved tyrosine residue in the tail (Tyr(356) in Escherichia co
118 oteins by targeting a conserved lysine and a tyrosine residue in the variable ZA or BC loops.
119 how TPSTs catalyze the sulfation of multiple tyrosine residues in a substrate protein remain unresolv
120 of OCBS, corresponding to one serine and two tyrosine residues in CBSs.
121 n the N-terminal of SOCS36E blocks access to tyrosine residues in Dome.
122                       Systematic mutation of tyrosine residues in Gly/Ser-Tyr-Gly/Ser motifs of the I
123   NO derived from iNOS mediates nitration of tyrosine residues in IRF5 protein, leading to the suppre
124 lementary to MptpA, phosphorylates these two tyrosine residues in MptpA.
125 anine substitution of serine, threonine, and tyrosine residues in ORF2 increased the steady-state pro
126 es) can introduce azide functional groups at tyrosine residues in peptide substrates.
127 on, the alkoxylation is highly selective for tyrosine residues in peptides and proteins, yet remarkab
128 opy for the identification of phosphorylated tyrosine residues in peptides.
129 n phosphorylation of the Igf1R on activating tyrosine residues in podocytes.
130                 Stable oxidation products of tyrosine residues in proteins may reflect the oxidative
131 PTPs) are enzymes that remove phosphate from tyrosine residues in proteins.
132 29 cells led to the local phosphorylation of tyrosine residues in protrusions, a signaling event that
133                  We observe three classes of tyrosine residues in PYP that exhibit very different pK(
134  the role of nitration at single or multiple tyrosine residues in regulating alpha-syn structure, mem
135 identify proteins that are phosphorylated on tyrosine residues in response to Listeria-induced T-cell
136                     NO mediates nitration of tyrosine residues in RORgammat, leading to the suppressi
137                 Phosphorylation at different tyrosine residues in SH3 domains has been reported previ
138                   However, the role of these tyrosine residues in signaling and transformation mediat
139 f Shc where Jak3 directly phosphorylated two tyrosine residues in Src homology 2 (SH2) domain and one
140 s known to be governed by phosphorylation of tyrosine residues in the activation loop of the kinase d
141 on with alphakap, with substitution of three tyrosine residues in the alpha-dbn C terminus with pheny
142 orylation of critical serine, threonine, and tyrosine residues in the C terminus of this protein.
143 f the AP-2 clathrin adaptor complex and ITIM tyrosine residues in the cytoplasmic domain of 3DL1.
144 les induces the phosphorylation of conserved tyrosine residues in the cytoplasmic tails of tetherin d
145 ril formation in vitro and in vivo Some nine tyrosine residues in the fibromodulin N-terminal domain
146                                Thus, the two tyrosine residues in the Kv11.1 S4S5 linker play critica
147 bserved enhanced phosphorylation of FCRL4 on tyrosine residues in the presence of the HCK p59 or FGR.
148 t aspartate, cysteine, serine, threonine, or tyrosine residues in the rgfC mutant.
149 y of PG9 and RSH is the presence of sulfated tyrosine residues in their antigen-binding regions.
150 re commonly post-translationally sulfated on tyrosine residues in their N-terminal regions, the initi
151 ngly, VEGF-Ax induces phosphorylation of key tyrosine residues in VEGFR-2.
152 usly shown that cortactin phosphorylation at tyrosine residues, in particular tyrosine 421, promotes
153 ons of proteins, particularly bromination of tyrosine residues, in peroxidasin-expressing PFHR9 cells
154  that phosphorylation at distinct serine and tyrosine residues inhibits PDHA1 through distinct mechan
155 gs suggest that phosphorylation at different tyrosine residues inhibits PDP1 through independent mech
156 roduced for incorporating the fluorosulfated tyrosine residue into peptides of interest.
157 irected mutagenesis of RCAR1 showed that its tyrosine residue is critical for AHG1 interaction and re
158  conclude that this previously unappreciated tyrosine residue is key to anchoring the intercalating l
159              We further demonstrate that the tyrosine residue is phosphorylated by Src family kinases
160 that is present in methanofuran cofactors, a tyrosine residue is present in methylofuran, which was f
161        Direct polymer conjugation at peptide tyrosine residues is described.
162 ted that the presence of at least one of the tyrosine residues is essential for efficient catalysis b
163 in phosphorylation on serine, threonine, and tyrosine residues is essential for fast, specific, and a
164 ithin domain 1 of NS5A, but not of any other tyrosine residue, is crucial for complex formation.
165 or di-iodotyrosine (DIT); however, selective tyrosine residues lead to preferential formation of T(4)
166                       In the absence of this tyrosine residue, levels of DM remained unchanged irresp
167                  Results demonstrated that a tyrosine residue located on a catalytic loop proximal to
168 bstrate interaction is mediated by conserved tyrosine residues located in flexible loops in nucleotid
169 ases (SFKs) and that this occurs on multiple tyrosine residues located within its negative regulatory
170  Tyr-lock peptide family, is stabilized by a tyrosine residue locked into three-dimensional space.
171  only AL-09 favors dimer conformations where tyrosine residues mediate crucial interactions for amylo
172 is the first kinase to phosphorylate the key tyrosine residue needed to maintain BAK in an inactive c
173 ntA mediates the transfer of three AMPs to a tyrosine residue next to the RNase domain of HepT in She
174 stically, we found that the phosphorylatable tyrosine residues of alpha-dbn are essential for the sta
175  and efficient phosphorylation of C-terminal tyrosine residues of alpha-syn remain to be identified.
176 l that MPO chlorinates and nitrates specific tyrosine residues of apoA-I, the major HDL protein.
177              We have identified the specific tyrosine residues of CitK that are phosphorylated and sh
178                   Mutation analysis of known tyrosine residues of FGFR1 reveals that tyrosine 653/654
179 orylate extracellular serine, threonine, and tyrosine residues of numerous proteins have been identif
180 rc-dependent phosphorylation of two critical tyrosine residues of p130CAS, leading to the assembly of
181 oxyribozymes, DNA enzymes) can phosphorylate tyrosine residues of peptides.
182 serve as docking elements to dephosphorylate tyrosine residues of target proteins.
183 ates that the 3-fluorosialyl moiety modifies tyrosine residues of the sialidases.
184 -processing sites contains several conserved tyrosine residues, of which some are post-translationall
185     Here, we show that nitration of a single tyrosine residue on a small proportion of 90-kDa heat-sh
186         EGFR-mediated phosphorylation of one tyrosine residue on the Fzd9b intracellular tail in resp
187 unctional implications of previously unknown tyrosine residues on beta-catenin phosphorylated by Jak3
188       Upon stimulation, FGFR2 phosphorylates tyrosine residues on Grb2, promoting dissociation from t
189  in a ligand-dependent manner through unique tyrosine residues on IL-17RB.
190 , was associated with several phosphorylated tyrosine residues on nephrin.
191 ulose surface, leading to alignment of three tyrosine residues on the binding face of the enzyme with
192 aling events initiated by phosphorylation of tyrosine residues on the long form of the leptin recepto
193 he direct intracellular dephosphorylation of tyrosine residues on the receptor target.
194  finding of BAK1 to be autophosphorylated at tyrosine residues, our results unveiled the tyrosine pho
195 es SHP-1 and causes dephosphorylation of SPL tyrosine residues, PGI2 and forskolin cause phosphorylat
196 e show M13 phage genetically engineered with tyrosine residues precisely fused to the major coat prot
197 here both the distal Cu and the redox-active tyrosine residue present in CcO are modelled.
198 tes and covalent modification of a bystander tyrosine residue present in Ral and Ras GTPases provide
199 P apparently clashes with a highly conserved tyrosine residue, preventing the formation of a correct
200 ce, whereas mimicking phosphorylation of the tyrosine residue promoted internalization and reduced ce
201 osition 33, but not in any of the other four tyrosine residues prone to nitration in Hsp90, was suffi
202 lalanines that can be selectively mutated to tyrosine residues, provides an ideal protein with which
203          Protein phosphorylation at distinct tyrosine residues (pY) is essential for fast, specific,
204                             This reaction on tyrosine residues required both the TGF-beta1-dependent
205 rm crucial hydrogen bonds with glutamate and tyrosine residues, respectively.
206 hese potential phosphorylation sites and the tyrosine residue result in dramatically slower activatio
207 abilizes the deprotonation of an active-site tyrosine residue, resulting in a very large isotope effe
208 atase (TCPTP) dephosphorylated TbetaRII tail tyrosine residues, resulting in inhibition of TbetaR-dep
209 T constructs with combinatorial mutations of tyrosine residues reveal a previously unidentified allos
210    Site-directed mutagenesis targeting these tyrosine residues revealed that their phosphorylation mo
211  caused a fairly indiscriminate nitration of tyrosine residues, reversible modifications of protein t
212 ed by a cluster of four manganese ions and a tyrosine residue that comprise the redox-active componen
213  may interact with Y529, a conserved R-helix tyrosine residue that forms part of the CLC ion conducti
214       We show that EgtB contains a conserved tyrosine residue that reacts via proton-coupled electron
215 on of insulin receptor substrate 1 (IRS1) on tyrosine residues that activate PI3K.
216  controlled this process as well as the EGFR tyrosine residues that are involved.
217 I1 compared to wild-type FLI1 and depends on tyrosine residues that are necessary for phase transitio
218 mical inhibitors, we identified the specific tyrosine residues that are phosphorylated on IQGAP1 and
219 ction by acting as a molecular shield of key tyrosine residues that are targets for the tyrosine phos
220 sion of this chemistry for the activation of tyrosine residues that project into solution from the N
221 sine kinases involves autophosphorylation of tyrosine residues that recruit Src-homology 2 (SH2)-doma
222                               GluN2A harbors tyrosine residues that, when phosphorylated by Src famil
223                             The oxidation of tyrosine residues to generate o,o'-dityrosine cross-link
224 er (HAT) pathway with a pair of cysteine and tyrosine residues to regenerate SAM.
225 3'-phospho-adenosine-5'-phospho-sulfate onto tyrosine residues, TPST1 and TPST2, are anchored to the
226 ed activation of TRPV4, which requires a key tyrosine residue (TRPV4-Tyr-110).
227 phosphorylation status of two well conserved tyrosine residues, typically located in the D-loop, regu
228    Here, we report that phosphorylation of a tyrosine residue Tyr-301 also inhibits PDH alpha 1 (PDHA
229 teracts with DEF6 and phosphorylates DEF6 at tyrosine residues Tyr(210) and Tyr(222).
230 ugh the phosphorylation of the specific SHCA tyrosine residues Tyr-239, Tyr-240, and Tyr-313.
231  results from insertion of a conserved CHMP5 tyrosine residue (Tyr(182)) at the core of LIP5NTD struc
232 single nitration site in Akt1 located at the tyrosine residue (Tyr(350)) located within the client-bi
233 tes NMHC-IIA in a previously uncharacterized tyrosine residue (Tyr-158) located in its motor domain n
234       Crystal structures of GltPh revealed a tyrosine residue (Tyr-33) that we propose interacts with
235  an aryl sulfonyl fluoride electrophile at a tyrosine residue (Tyr-82) inhibits guanine exchange fact
236                           We identified four tyrosine residues (Tyr-649, Tyr-671, Tyr-734, and Tyr-81
237 on the phosphorylation of a highly conserved tyrosine residue, Tyr 57, in histone H2A and is mediated
238 re we report that phosphorylation at another tyrosine residue, Tyr-94, inhibits PDP1 by reducing the
239                    M2 has two closely spaced tyrosine residues, Tyr(120) and Tyr(129), which are phos
240 anization is governed, on one side, by three tyrosine residues, Tyr(194), Tyr(196), and Tyr(199), whi
241 he crystal structure of VAO reveals that two tyrosine residues, Tyr-108 and Tyr-503, are positioned t
242 ements show that mutation of two pore-lining tyrosine residues, Tyr-23 and Tyr-149 in sheep AQP0, to
243 cts of mutations in the two highly conserved tyrosine residues, Tyr-2387 and Tyr-2391, in the Polthet
244 to study radical formation in DHP when three tyrosine residues, Tyr-28, Tyr-34, and Tyr-38, were repl
245 sequence motif in EL5 containing a conserved tyrosine residue (Tyr293) whose aromatic side chain is e
246 g results in the unique conformations of two tyrosine residues, Tyr9(1.35) and Tyr271(7.36), which ar
247 rmed by covalent ortho-ortho coupling of two tyrosine residues under conditions of oxidative stress b
248 studies reveal that Dbl is phosphorylated on tyrosine residues upon stimulation by growth factors and
249 ning phosphocholinated serine, threonine, or tyrosine residues using preformed functional amino acid
250  [(18)F]CF(3) incorporation at tryptophan or tyrosine residues using unmodified peptides as complex a
251 one of which is covalently cross-linked to a tyrosine residue via a post-translational modification (
252 in, where Jak3 directly phosphorylated three tyrosine residues, viz.
253 ex on evolutionarily conserved threonine and tyrosine residues was recently identified and shown to b
254 e-specifically nitrate calmodulin at its two tyrosine residues, we assessed the effects of these alte
255            In addition to contributions from tyrosine residues, we find that glutamine residues also
256 nation position is restricted by a conserved tyrosine residue, whereas access to this same position s
257 s change is accompanied by a conversion of a tyrosine residue, which is identified as the formation o
258                       It was photocaged on a tyrosine residue, which required the exchange of phenyla
259 holipase Cgamma2, a protein reported to bind tyrosine residues, which are absent in the cytoplasmic d
260 hat sequence specificity is conferred by two tyrosine residues, which insert into the minor groove of
261                                      Several tyrosine residues with elevated phosphorylation (i.e. Ty
262             Moreover, we have identified two tyrosine residues with opposing regulatory functions: on
263  genetic site-specific replacement of single tyrosine residues with photocaged tyrosine, in an antibo
264 oxynitrite-mediated nitration of a conserved tyrosine residue within B56delta (B56delta(Y289)).
265           Pre-steady-state kinetics reveal a tyrosine residue within the intercalating loop (Y269) th
266 o-step phosphorylation mechanism involving a tyrosine residue within the kinase inhibitory domain and
267             Itk catalyzes phosphorylation on tyrosine residues within a number of its natural substra
268 tory receptors, phosphorylation of cytosolic tyrosine residues within ITIMs results in recruitment of
269 h c-Abl and underwent phosphorylation on two tyrosine residues within its regulatory activation funct
270     Previous studies have shown that several tyrosine residues within JAK2 are phosphorylated on grow
271 how that a triad of strongly hydrogen-bonded tyrosine residues within the active site of the enzyme k
272 y interactions with conserved asparagine and tyrosine residues within the binding pocket.
273 te-directed mutagenesis showed that specific tyrosine residues within the ChtA CR domain were critica
274 aRII-induced signaling; however, there are 5 tyrosine residues within the cytoplasmic tail that could
275 o the extracellular domain of MPL and that 3 tyrosine residues within the intracellular domain of MPL
276 inker, and we show that two highly conserved tyrosine residues within the KCNH subfamily of channels
277                                              Tyrosine residues within the PrLD are important for gran
278 ted with actin, can be phosphorylated on two tyrosine residues within the switch regions, suggesting
279                                   Lysine and tyrosine residues within this binding site interact with
280 pletely abolishes the phosphorylation of all tyrosine residues, without measurable effects on recepto
281                         The highly conserved tyrosine residue Y(7.53) undergoes transitions between t
282  HIPK2 by phosphorylating a highly conserved tyrosine residue Y-361 within the kinase domain.
283 ate electron transfer pathways there are two tyrosine residues, Y(Z) and Y(D).
284  GIRK phosphorylation at this amino terminal tyrosine residue (Y12) enhances channel deactivation.
285                         We also identified a tyrosine residue (Y152) within the HPM motif of HIP1 tha
286                               Importantly, a tyrosine residue (Y203) is essential for ligand recognit
287 elded from the substrate or the solvent by a tyrosine residue (Y224).
288 S. aureus AgrA identifies a highly conserved tyrosine residue, Y229, as a major amino acid determinan
289     Alanine mutation of a conserved H-I loop tyrosine residue, Y232, prevents regulation demonstratin
290  is frequently phosphorylated at a conserved tyrosine residue, Y240, in GBM clinical samples.
291 re examined in a mutant of the key I4R motif tyrosine residue (Y325F) and different gammaC truncation
292 ere, we have shown that phosphorylation of a tyrosine residue (Y36) present in ERbeta, but not in ERa
293 which are contingent on phosphorylation of a tyrosine residue (Y380) found in the linker region betwe
294 rylation sites, including a highly conserved tyrosine residue (Y382), into alanines also delayed the
295 III in domain IV of TetM, revealing that the tyrosine residues Y506 and Y507 are not responsible for
296  In addition, the NDV F CT has two conserved tyrosine residues (Y524 and Y527) and a dileucine motif
297                        In OprP there are two tyrosine residues, Y62 and Y114, whereas the correspondi
298                  Phosphorylation of a single tyrosine residue, Y836, is required for activation of EF
299  gB/gH-gL-induced cell-cell fusion in vitro, tyrosine residues Y881 and Y920 in the gBcyt were substi
300 ting this point, we observed that one of the tyrosine residues (Y954) located in the C-terminal lobe

 
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