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1 en bond donors from the guanidinium group of argininamide.
2 osen for its nanomolar range affinity, and l-argininamide (1OLD) to show the versatility of our appro
3 ical shift mapping experiments, we show that argininamide, a ligand mimic of TAR's cognate protein bi
4                              The ligands are argininamide, a linear peptide mimic of the Tat basic do
5  as compared to single-charge lysinamide and argininamide adsorbents of matched total charge.
6 ed in and around the known binding sites for argininamide and a BIV Tat arginine-rich peptide, respec
7  was remarkably similar to that obtained for argininamide and is evidence for guanidinoneomycin bindi
8                                              Argininamide and its analogs are known to bind to the ha
9 o-axially stack and the critical U23 and the argininamide are located in the major groove.
10 ncy virus type-1 (HIV-1) bound to the ligand argininamide (ARG) has been characterized using a combin
11  TAR RNA and its interaction with the ligand argininamide (ARG), a mimic of TAR's cognate protein bin
12 s) both in free form and bound to the ligand argininamide (ARG).
13 xo -1,2-diphenyl-3H-1,2,4-triazol-4-yl]ethyl]argininamide (BIIE0246) not only blocked the effects of
14                                              Argininamide binding is stabilized by stacking of the gu
15 hat the base triple is required for specific argininamide binding.
16 ple mutant of the three base bulge HIV-1 TAR-argininamide complex demonstrated that the base triple i
17                The dynamics of the HIV-2 TAR-argininamide complex was investigated by measurements of
18 e high resolution structure of the HIV-2 TAR-argininamide complex, confirming that a base triple is a
19  frequencies of base motion in the HIV-2 TAR-argininamide complex.
20 n the HIV-2 transactivation response element-argininamide complex.
21 gh resolution NMR structure of the HIV-2 TAR-argininamide complex.
22 ved than in earlier studies of the HIV-1 TAR-argininamide complex.
23 mine the solution structure of the HIV-2 TAR-argininamide complex.
24                                          The argininamide guanidium group hydrogen bonds to the major
25                                   Binding of argininamide induces formation of one Watson-Crick and t
26                  The studies reveal that the argininamide inhibitory mechanism involves a shift of th
27 e data suggest a molecular mechanism wherein argininamide inhibits NC-facilitated TAR RNA/DNA anneali
28 se triple is an important feature of the TAR-argininamide interaction.
29                         Here, we explore how argininamide modulates the annealing kinetics and second
30 d to examine how a model inhibitor of HIV-1, argininamide, modulates the nucleic acid chaperone activ
31  result contradicts the belief that a single argininamide residue is responsible for stabilising the
32 between the bases of A22 and U23, forming an argininamide sandwich.
33                      The complex of TAR with argininamide serves as a model for the RNA conformation
34                             Analogues of the argininamide-type NPY Y1 receptor (Y1R) antagonist BIBP3
35  Y Y(1) receptor (Y(1)R) in complex with the argininamide-type Y(1)R selective antagonist UR-MK299 (2
36 ergoes the largest dynamic change on binding argininamide, while U25 remains flexible, reflecting the