戻る
「早戻しボタン」を押すと検索画面に戻ります。 [閉じる]

コーパス検索結果 (1語後でソート)

通し番号をクリックするとPubMedの該当ページを表示します
1 similar to the Escherichia coli SSB (EcoSSB) homotetramer.
2 d less than that seen for the unactivated SS homotetramer.
3 human ABCG2 likely exists and functions as a homotetramer.
4 ons at this residue destabilize the R67 DHFR homotetramer.
5 active site pore traverses the length of the homotetramer.
6  and then two homodimers associate to form a homotetramer.
7  catalytic domain of E. coli RNase E forms a homotetramer.
8      Full-length AbrB is shown to exist as a homotetramer.
9 ommunication between the active sites in the homotetramer.
10 ently bound to Lys318 of two subunits of the homotetramer.
11 rometry and gel electrophoresis that it is a homotetramer.
12           The active form of the enzyme is a homotetramer.
13 ates that the native form of the enzyme is a homotetramer.
14                        Thus, the enzyme is a homotetramer.
15 g revealed that 66Y likely stabilized the NA homotetramer.
16 eoprotein (NP) and self-associates to form a homotetramer.
17 tudied the folding and stability of the DCoH homotetramer.
18  heterologous assembly of BcgI, TstI forms a homotetramer.
19 ut interacts with DNA in our structures as a homotetramer.
20 le caveolin-3 nonamers bind to a single RyR1 homotetramer.
21  (M1 and M3) from another subunit within the homotetramer.
22 n the crystal structures of murine and human homotetramers.
23 heteromers by attenuating formation of GluR2 homotetramers.
24 d in Escherichia coli and purified as intact homotetramers.
25 ncentrations that specifically blocked SKCa2 homotetramers.
26 yrase regulate the formation of fully active homotetramers.
27 uired for cell surface localization of GIRK4 homotetramers.
28 are themselves capable of forming functional homotetramers.
29  and heterotetramers, with a predominance of homotetramers.
30  and 1:3 stoichiometries, in addition to the homotetramers.
31 ma membrane doubles the contribution of PIP2 homotetramers.
32 n 1 (Rom1), but retained the ability to form homotetramers.
33  sufficient to maintain ATP regulation in R2 homotetramers.
34 re tryptases but not alpha- or beta-tryptase homotetramers.
35  the same extent as that observed for mutant homotetramers.
36  attenuated Ca(2+) release when expressed as homotetramers.
37 ring analysis that PlaB forms homodimers and homotetramers.
38 t channels preferentially self-assemble into homotetramers.
39 m and the transition from ExbB homodimers to homotetramers.
40 with viral proteins NP and L or formation of homotetramers.
41 lpha-subunit rather than antagonism to Kv1.2 homotetramers.
42 no acid hydroxylase superfamily, exists as a homotetramer (236 kDa on size exclusion chromatography).
43                                     KAP is a homotetramer (38.2 kDa per subunit) and, as purified, co
44                              The enzyme is a homotetramer (42.06 kDa per subunit) and, as purified, c
45 s begins with the dissociation of the native homotetramer (a dimer of dimers) to form a monomeric int
46 ls of TRPC1 increased the formation of TRPC5 homotetramer, a highly Ca(2+)-permeable channel, and sti
47                 alpha/beta-Tryptase, but not homotetramer, activates protease-activated receptor-2 (P
48 B binds to the sinIR DNA target element as a homotetramer, affording a 4:1 protein:DNA stoichiometry.
49                                          The homotetramer (ALDH1 or ALDH2) is a dimer of dimers (A-B
50 pparent destabilization of the purified PEPC homotetramer, all were compromised catalytically in vivo
51 psilon A)]) with recombinant (C1)4 and (C2)4 homotetramers along with competition binding assays with
52                            Apo-SiRHP forms a homotetramer, also dependent on its N terminus, that is
53 ng showed that the protein was purified as a homotetramer, although nonspecific oligomerization occur
54 thyroxin-binding sites in TTR stabilizes the homotetramer and attenuates TTR amyloidosis.
55                                  PpCMLE is a homotetramer and belongs to the fumarase class II superf
56                                    LpdA is a homotetramer and co-purifies with one molecule of tightl
57 lodysplastic syndromes, at the DNMT3A.DNMT3A homotetramer and DNMT3A.DNMT3L heterotetramer interfaces
58                          The NA TMD formed a homotetramer and efficiently trafficked to the plasma me
59        The C. trachomatis FabI (CtFabI) is a homotetramer and exhibited typical FabI kinetics, and it
60                    The M(2) ion channel is a homotetramer and has a 24-residue N-terminal extracellul
61 C-MS, we confirm that AbrB is assembled as a homotetramer and not as a homohexamer as previously sugg
62  5F11-scFv-streptavidin (5F11-scFv-SA) was a homotetramer and showed comparable avidity to 5F11 IgM a
63 This structure confirms that MspJI acts as a homotetramer and that the modified cytosine is flipped f
64  molecular mass of 235 kD corresponding to a homotetramer and the C-terminus was critical for this ol
65   DGAT1 can exist as either a homodimer or a homotetramer and the two forms have similar enzymatic ac
66 ation analysis suggested that RPA1 exists as homotetramers and homodimers in solution, while RPA2 and
67 e activity and consisted of cross-linked A3G homotetramers and homodimers.
68 d-type (WT) and C-terminally tagged (CT) TTR homotetramers and hybrid tetramers (i.e., tetramers cont
69 ortant structural differences between sqKv1A homotetramers and native squid channels are likely to ex
70            We tested whether purified KLP61F homotetramers and Ncd homodimers can generate a force ba
71 nd 15 (four homodimers, six homotrimers, six homotetramers and one homopentamer) had solution small-a
72 te of subunit exchange between wild-type TTR homotetramers and wild-type TTR homotetramers tagged wit
73 rs could combine to form either two types of homotetramers and/or one heterotetramer composed of both
74  protein exists in solution as a heat-stable homotetramer, and enzymatic assays reveal that the expre
75 f only 1 mol of phosphate per mole of enzyme homotetramer, and glycogen synthase kinase-3 incorporate
76 uine butyrylcholinesterase (BChE), a 364 kDa homotetramer, and the complexes were studied by (1)H NMR
77 XR is unique in that it self-associates into homotetramers, and that these tetramers dissociate rapid
78  stability and are generally assumed to form homotetramers, and this species is proposed to be the on
79 s, C-terminally disulfide-linked homodimers, homotetramers, and up to three tetramers covalently atta
80     The assembly process of the hemoglobin H homotetramer apparently follows a scenario similar to th
81 vities of the resurrected L(K41R.T51K.S302N) homotetramer are compared with its heterotetrameric form
82 Currents mediated by BK channel-forming slo1 homotetramers are consistently inhibited by increases in
83 ugh the evidence to date suggests that GIRK1 homotetramers are not functional.
84 ers in each of the expression systems with a homotetramer as a predominant form.
85 etic data reveal the dissociation of the p73 homotetramers as the rate-limiting step for heterotetram
86 entrifugation, where the active enzyme was a homotetramer at 4 degrees C but dissociated into inactiv
87 lytic portion of beta-tryptase to the active homotetramer at acid pH requires heparin.
88  we found that this peptide assembles into a homotetramer at neutral pH in contrast to the native mol
89 and incorporate subunits from labeled WT TTR homotetramers at a rate equivalent to that exhibited by
90 from Saccharomyces cerevisiae (ScRim1) forms homotetramers at high protein concentrations, whereas at
91  rates of two ligands, beta-glucuronidase (a homotetramer bearing multiple Man-6-P moieties) and IGF-
92  in the ESI mass spectrum corresponds to the homotetramer beta*4, alongside homodimeric species and m
93                                          SSB homotetramers bind ssDNA in several modes differing in o
94                                          SSB homotetramers bind ssDNA in several modes that differ in
95 nge (DeltaC(p,obs)) for Escherichia coli SSB homotetramer binding to single-stranded (ss) DNA.
96 cells shows that MAT-3 predominantly forms a homotetramer but also a trimer and a dimer.
97     We show that nestin forms homodimers and homotetramers but does not form IF by itself in vitro.
98                      The E. coli enzyme is a homotetramer, but in a quaternary state between the cano
99 o note that both of these proteins behave as homotetramers, but one behaves as a more compact molecul
100  the subunit exchange reaction of p53 family homotetramers by nanoflow electrospray mass spectrometry
101 gion of contact between subunits within RyR1 homotetramer Ca2+ release channels.
102 ompetition with the other pathways, in which homotetramers can be formed either by the association of
103                                       Mutant homotetramers carry little or no K+ current despite norm
104     In oligodendrocytes, KIR4.1 appears as a homotetramer channel, in astrocytes as homo- and heterot
105 change of MnSOD's stoichiometry from a known homotetramer complex to a monomeric form.
106                               Comprised of a homotetramer complex, its function primarily is to slide
107                                  T4 Pnk is a homotetramer composed of a C-terminal phosphatase domain
108    In solution, the enzyme (EC ) exists as a homotetramer composed of non-covalently linked subunits
109 yntaxin 1A H3, four molecules associate as a homotetramer composed of two pairs of parallel helices t
110 rotein of human metapneumovirus (HMPV) forms homotetramers composed of a stable oligomerization domai
111 oltage-dependent potassium channels (Kv) are homotetramers composed of four voltage sensors and one p
112                              The enzyme is a homotetramer comprising two obligate dimers and four pyr
113  complex, indicating that the crystallin was homotetramer consisting of 38-kDa subunits.
114                   The structure of EmoB is a homotetramer consisting of four alpha/beta-single-domain
115  C-terminal region of Abeta assemble to form homotetramers consisting of two hydrogen-bonded dimers.
116                              The enzyme is a homotetramer, consisting of an alpha/beta single domain
117                 The subunit of the DAHPS(Tm) homotetramer consists of an N-terminal ferredoxin-like (
118 , the synaptic intermediate is a recombinase homotetramer containing a pair of loxP DNA target sites.
119 contain four identical subunits which form a homotetramer containing a single active site pore access
120  the E. coli enzyme, A. aeolicus KDO8PS is a homotetramer containing four distinct active sites at th
121                    Because the lac repressor homotetramer contains two DNA binding modules, it bridge
122 ly inhibits TRPC4alpha, TRPC4beta, and TRPC5 homotetramer currents and also TRPC1/4alpha, TRPC1/4beta
123  well as an experimental SAXS profile of the homotetramer D-xylose isomerase.
124 tion in non-alpha chains plays a key role in homotetramer, dimer, and monomer formation, which in tur
125  of bacterial SSB family members function as homotetramers, dimeric SSB proteins were recently discov
126                                              Homotetramers dominated in Nonidet P-40, and dimers and
127                              BK channels are homotetramers (encoded by Slo1) that possess a unique tr
128 , resulting in high-force production at both homotetramer ends.
129    Unlike the SS enzyme, however, the LS302N homotetramer enzyme is neither activated by the effector
130 tion of a population of AGPase small subunit homotetramer enzymes with enhanced affinity toward ATP a
131                         Inversely, the GIRK2 homotetramers exhibit low Ibasal and strong activation b
132                       We show that the T119M homotetramer exhibits kinetic stabilization and therefor
133  IVD protein rapidly and stably forms mature homotetramer following import, whereas Type III mutant p
134 vious evidence that peripherin/rds mice form homotetramers for outer segment targeting.
135            The structure of OsGAPDH showed a homotetramer form with each monomer comprising three dom
136                                        GIRK4 homotetramers form channels with unusual single channel
137 a(112Thr,116Ile) chains showed homodimer and homotetramer formation like gamma-globin chains which co
138 on of betaB1DeltaN56 increased, resulting in homotetramer formation, and heteromolecular association
139  modeling predictions for ASL heterotetramer/homotetramer formation.
140 herichia coli RNase E protein functions as a homotetramer formed by Zn linkage of dimers within a reg
141 -electron microscopy structures of the GluA1 homotetramer, fully occupied with TARPgamma3 auxiliary s
142                       GIRK channels exist as homotetramers (GIRK2 and GIRK4) or heterotetramers with
143                                    The E487K homotetramers had 8% specific activity of the Glu487 enz
144 tose-1,6-bisphosphate aldolase (EC 4.1.2.13) homotetramer has been destabilized by site-directed muta
145  data reveal that the C10S/V30M and V30M TTR homotetramers have identical amyloidogenicity and stabil
146          The map shows that the protein is a homotetramer, having a low-density region on the 4-fold
147 man gamma2 tetramers as well as human gamma4 homotetramers (hemoglobin Bart's).
148 tor (RXR) can regulate transcription through homotetramers, homodimers, and heterodimers with other n
149 s30 and Tyr166 from adjacent subunits in the homotetramer human manganese superoxide dismutase (Mn-SO
150                              The enzyme is a homotetramer in its functional state, and the symmetry o
151 2-6His shows that it associates as a 196-kDa homotetramer in vitro, a result that is significant in l
152                          KDO8P synthase is a homotetramer in which each monomer has the fold of a (be
153 cture of the apoenzyme form of LmFBPase is a homotetramer in which the dimer of dimers adopts a plana
154                Structural studies revealed a homotetramer in which the quaternary arrangement of subu
155                  Rabbit muscle aldolase is a homotetramer in which the subunits have a classical alph
156 ctions in purine biosynthesis, is normally a homotetramer in which three subunits contribute to each
157 cinate lyase (ASL) of Bacillus subtilis is a homotetramer in which three subunits contribute to each
158 present closed-state structures of GluK2 KAR homotetramers in complex with ion channel blockers NpTx-
159 ansport protein (GLUT1) forms homodimers and homotetramers in detergent micelles and in cell membrane
160                          Structures of GluA2 homotetramers in distinct functional states, together wi
161     We also show that GIRK subunits may form homotetramers in expression systems, although the eviden
162  ABCD1 and its homolog ABCD2 exist mainly as homotetramers in the peroxisomal membrane.
163 ) currents generated by N-type alpha-subunit homotetramers inactivate rapidly because an N-terminal b
164 in three human TTR single amino acid variant homotetramers including two familial amyloidotic polyneu
165 rents during UBP-310 dissociation from GluK1 homotetramers, indicating that antagonist dissociation p
166 amyloid by acid-mediated dissociation of the homotetramer into monomers.
167                          Each subunit of the homotetramer is characterized by a five-stranded anti-pa
168 etin is not amyloidogenic because the native homotetramer is kinetically stable under physiologic con
169                       We show that the DCoH1 homotetramer is kinetically trapped, meaning once it for
170                          Each subunit of the homotetramer is made up of three distinct domains with o
171          This suggests that the formation of homotetramers is a common feature of NAP-1 fold histone
172 erotrimer) or Mer2 (a coiled-coil-containing homotetramer) is monodispersed in solution, but they ind
173                         KIF11 encodes EG5, a homotetramer kinesin motor.
174                      In the self-inactivated homotetramer, KLHDC2's C-terminal Gly-Ser motif mimics a
175         In solution, native CelF exists as a homotetramer (M(w), approximately 200,000) composed of n
176 esidues, but exhibits neither the functional homotetramer nor the homodimer that distinguish all SDRs
177 trophoresis to provide evidence that it is a homotetramer of 110-kDa subunits.
178 eptomyces lividans KcsA potassium channel, a homotetramer of 17.6 kDa subunits, was found to contain
179  manganese superoxide dismutase (MnSOD) is a homotetramer of 22 kDa subunits, a dimer of dimers conta
180 of human Mn superoxide dismutase (hMnSOD), a homotetramer of 22 kDa, reveals a functional role for th
181                The tumor suppressor p53 is a homotetramer of 4 x 393 residues.
182       Cardiac ryanodine receptor (RyR2) is a homotetramer of 560 kDa polypeptides regulated by calmod
183                      The native enzyme was a homotetramer of 58-kDa subunits and exhibited a pI of 4.
184                              The enzyme is a homotetramer of about 50 kDa subunits and is not subject
185                                    AqpZ is a homotetramer of four water-conducting channels that faci
186 residues in each of the four subunits of the homotetramer of human MnSOD was replaced with 3-fluoroty
187 H-1 (the homotetramer of LDHB) or LDH-5 (the homotetramer of LDHA), respectively.
188 etramers and leaving T cells with LDH-1 (the homotetramer of LDHB) or LDH-5 (the homotetramer of LDHA
189  report that the rat BCKD kinase exists as a homotetramer of M(r) = 185,000, based on results of gel
190 nt FA796 protein, which is predicted to be a homotetramer of the 1Fe-SOR class, can reduce superoxide
191 c GABA(B(1,2)) receptors that associate with homotetramers of auxiliary KCTD8, -12, -12b, or -16 (nam
192 nsing and pore-forming domains, but they are homotetramers of four identical subunits, rather than ps
193 e among bacterial SSBs, which typically form homotetramers of single-OB domain subunits.
194 nin is a monomeric protein that forms stable homotetramers on addition of BLA to the protein.
195 ndence of activation and/or inactivation, as homotetramers or when coexpressed with wild-type K(V) 2.
196 se allosteric interactions that exist in the homotetramer phosphofructokinase from Bacillus stearothe
197              The crystal conformation of the homotetramer points to the fact that, in the absence of
198                                         This homotetramer possesses a single active site pore and exa
199  high-resolution crystal structure shows the homotetramer possesses exact 222 symmetry.
200                                   The LS302N homotetramer possesses very little enzyme activity at a
201                             This enzyme is a homotetramer possessing 222 symmetry, and a single activ
202 nomers (78 amino acids long) assemble into a homotetramer possessing 222 symmetry.
203 e 78 amino acids long, which assemble into a homotetramer possessing 222 symmetry.
204                                R67 DHFR is a homotetramer possessing a single active site pore.
205          The active form of the protein is a homotetramer possessing D(2) symmetry and a single activ
206                          Thus, beta-tryptase homotetramers probably account for active enzyme detecte
207     GAC activation requires the formation of homotetramers, promoted by anionic allosteric activators
208  glucose to concanavalin A (ConA), a 106 KDa homotetramer protein, in free solution using picomoles o
209 cture of the full-length AMPA receptor GluA2 homotetramer, provide unique insights into the mechanism
210               We demonstrate herein that TTR homotetramers reassemble by an unusual monomer-dimer-tri
211 etal muscle Ca(2+) release channel (RyR1), a homotetramer, regulates the release of Ca(2+) from the s
212 er (Solanum tuberosum) AGPase (small subunit homotetramer) reported previously by others revealed tha
213 tion conditions for a group of eight protein homotetramers, representing a broad sample of protein st
214 w, in single molecule assays, that kinesin-5 homotetramers require the nonmotor C terminus for crossl
215 y kinetics of (35)S label incorporation into homotetramers showed a lag period corresponding to the t
216 contains a single Mis18 isoform that forms a homotetramer, showing tetrameric Mis18 is conserved from
217   During export in Escherichia coli, SecB, a homotetramer structurally organized as a dimer of dimers
218    The Lys 30 --> Nle variant forms a stable homotetramer (T(m) = 60 degrees C).
219 6/Lys 30 --> Nle variant forms a very stable homotetramer (T(m) = 80 degrees C).
220 ild-type TTR homotetramers and wild-type TTR homotetramers tagged with an N-terminal acidic flag tag
221                       Purified ssA-TIBF is a homotetramer that binds one substrate molecule and conta
222 ed DNA binding protein (SSB) is an essential homotetramer that binds ssDNA and recruits multiple prot
223 hat hKif15 is a plus-end-directed processive homotetramer that can step against loads of up to 3.5 pN
224    Dihydrodipicolinate reductase (DHPR) is a homotetramer that catalyzes reduction of dihydrodipicoli
225                     Transthyretin (TTR) is a homotetramer that circulates in both blood and cerebrosp
226                          The M2 protein is a homotetramer that contains four 19-residue transmembrane
227                          The M2 protein is a homotetramer that contains in its aqueous pore a histidi
228 r short-chain acyl-CoA derivatives to form a homotetramer that covers the binding cavity and locks Co
229                          KLP61F is a bipolar homotetramer that cross-links spindle microtubules [4].
230                                R67 DHFR is a homotetramer that exhibits numerous characteristics of a
231 hermophilus phosphofructokinase (BsPFK) is a homotetramer that is allosterically inhibited by phospho
232                 The dimers form a functional homotetramer that is fashioned through contacts between
233 ring mass spectrometry revealed AmpR to be a homotetramer that is stabilized by DNA containing the T-
234 stal structure data reveals this enzyme is a homotetramer that possesses a single active site pore.
235 pha3 chain the novel long chains assemble to homotetramers that are incorporated into mixed microfibr
236 embrane (TM) helix, which associates to form homotetramers that bind the anti-influenza drug amantadi
237 ceptor potential (TRP) channel subunits form homotetramers that function in sensory transduction.
238 ro, recombinant AIRE can form homodimers and homotetramers that were also detected in thymic protein
239 recombinant cav-3 nonamers and purified RyR1 homotetramers that would imply that at least one of the
240                                  EcSSB forms homotetramers that wrap ssDNA in multiple conformations
241 laevis, and Xenopus tropicalis formed stable homotetramers, the mtSSBs from Candida albicans and Cand
242   Together, we demonstrate that ACLY forms a homotetramer through the C terminus to facilitate CoA bi
243 ull-length ACAT1 converted the enzyme from a homotetramer to a homodimer.
244 lies on kinesin-5 motors that act as bipolar homotetramers to crosslink microtubules.
245  structural network adopted by a sialic acid homotetramer, used as a model for a,2-8 linked polysacch
246    Unlike the other ACADs, which are soluble homotetramers, VLCAD is a homodimer associated with the
247               The subunit size of the native homotetramer was determined to be 34,000 Da.
248                       A model for the DNMT3A homotetramer was developed via computational interface s
249 ng pattern of Gbetagamma attachment to GIRK4 homotetramers was consistent with the binding of one, tw
250                                     Putative homotetramers were also observed.
251                                              Homotetramers were identified for the type III IP3R; how
252 ified for the type III IP3R; however, type I homotetramers were undetectable.
253     These GIRK4 complexes, most likely GIRK4 homotetramers, were previously not seen because of their
254               Both form enzymatically active homotetramers when overexpressed in Escherichia coli.
255 e sequence TRPC4beta < TRPC4alpha < TRPC5 in homotetramers, whereas when forming heterotetramers with
256 us with the TPP enzymes having arisen from a homotetramer which subsequently diverged into an alpha(2
257  absence of ligand, RXR self-associates into homotetramers which are transcriptionally silent, and th
258  behavior similar to that of the E. coli SSB homotetramer, which also shows binding mode transitions,
259 quitously expressed enzyme, functioning as a homotetramer, which catalyzed the rate-limiting step in
260  of free RI crystallizes in a domain-swapped homotetramer, which likely works as a sink for RI molecu
261 ramer of immature proteoid roots into a p107 homotetramer while significantly increasing the enzyme's
262 omodimers or heterodimers, but it also forms homotetramers whose function is poorly defined.
263          The AQP1 water channel protein is a homotetramer with 28 kDa subunits containing six transme
264                         It forms a symmetric homotetramer with a central pore which functions as the
265                            MAO-N exists as a homotetramer with a large channel at its centre and shar
266                                     FOR is a homotetramer with a mass of 280 kDa and contains approxi
267                             This enzyme is a homotetramer with a molecular mass of 108 kDa.
268                             This enzyme is a homotetramer with a monomer molecular mass of 42 kDa.
269                                 ACLY forms a homotetramer with a rigid citrate synthase homology (CSH
270      Short chain acyl-CoA dehydrogenase is a homotetramer with a subunit mass of 43 kDa and crystalli
271          The membrane-associated enzyme is a homotetramer with a subunit molecular mass of 49,500 Da.
272 ole in excitation-contraction coupling, is a homotetramer with a subunit molecular mass of 565 kDa.
273                   Thus, CorA appears to be a homotetramer with a TM segment of one monomer physically
274  the principal ion observed corresponds to a homotetramer with an average molecular mass of 86,844 Da
275 -C6H4)-OCH2CH2NH2 PLL was discovered to be a homotetramer with an intersubunit disulfide bridge.
276 ped protomers assemble into a C(4)-symmetric homotetramer with an open central core and a surface con
277 gral membrane protein whose active form is a homotetramer with each polypeptide chain containing 96-a
278                The enzyme from S. typhi is a homotetramer with each subunit containing 339 amino acid
279                           SSB functions as a homotetramer with each subunit possessing a DNA binding
280 cal characterization indicates TtHGXPRT as a homotetramer with excellent activity and stability acros
281 chia coli phosphofructokinase 1 (EcPFK) is a homotetramer with four active and four allosteric sites.
282 ctokinase from Escherichia coli (EcPFK) is a homotetramer with four active sites and four allosteric
283 ctokinase from Escherichia coli (EcPFK) is a homotetramer with four active sites, which bind the subs
284  exchange rates in rabbit muscle aldolase, a homotetramer with M(r) = 157,000.
285  enzyme for treatment of hyperuricemia, is a homotetramer with multiple surface lysines, limiting con
286                                  HMPV P is a homotetramer with regions of intrinsic disorder and has
287               The asymmetric unit contains a homotetramer with substrate/product bound in two monomer
288            IscA exists as an (alpha1alpha2)2 homotetramer with the (alpha1alpha2) dimer comprising th
289                       The enzyme forms a 222 homotetramer with the PLP cofactor bound via a Schiff-ba
290 n of seven different forms of a streptavidin homotetramer with variations of N-terminal methionine re
291                                    RyRs form homotetramers with a mushroom-like shape, consisting of
292                                     They are homotetramers with dimeric motor and tail domains at bot
293    Voltage-gated potassium (Kv) channels are homotetramers with each subunit constructed from six tra
294 bipolar mitotic spindle in eukaryotes, forms homotetramers with two pairs of motor domains positioned
295                                      It is a homotetramer, with each monomer consisting of a transmem
296                                  SOR forms a homotetramer, with each subunit adopting an immunoglobul
297                           The enzyme forms a homotetramer, with the dinucleotide binding at the monom
298                                    RmlA is a homotetramer, with the monomer consisting of three funct
299  of bacterial SSB family members function as homotetramers, with each monomer contributing a single O
300 bifidobacterial GH38 alpha-mannosidases form homotetramers, with the N-terminal jelly roll domain con

 
Page Top