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 e reactive-site peptide bonds in eglin C and ecotin.
2 tive pathway activator, are all inhibited by ecotin.
3 y, and lectin pathway-inhibitory capacity of ecotin.
4  hydrogen bond with the P2 carbonyl group of ecotin.
5 ants (K(i)s) comparable to that of wild-type ecotin.
6 addition of a matriptase-specific variant of ecotin.
7  10(4) times stronger than that of wild-type ecotin.
8  is specific for proteins that interact with ecotin.
9                                          The ecotin 60X4 library, in which residues 67 to 70 of ecoti
10                         The structure of the ecotin 67-70A, M84R mutant bound to trypsin shows large
11                                              Ecotin 67-70A, M84R which has four alanine substitutions
12 ptide was expressed at the amino terminus of ecotin, a dimeric macromolecular serine protease inhibit
13                                              Ecotin, a dimeric serine protease inhibitor from Escheri
14 607 in complex with a substitution mutant of ecotin, a panserine protease protein inhibitor secreted
15                                              Ecotin, a potent macromolecular inhibitor of serine prot
16 f complexes of trypsin N143H, E151H bound to ecotin A86H are determined at 2.0 A resolution via X-ray
17 , suggests that the protease binding loop of ecotin adopts a conformation mimicking that of the cleav
18                  The inherent flexibility of ecotin allows it to accommodate these mutations and stil
19 ease inhibitor was realized by the use of an ecotin analogue containing allylglycine at position 84 i
20                          Iodine treatment of ecotin analogue Met84(A)Gly resulted in the deactivation
21 ld be released from the protein complex with ecotin analogue Met84(A)Gly.
22 sizing system, permitting the elaboration of ecotin analogues containing allyglycine at the desired s
23                                  The derived ecotin analogues were capable of inhibiting bovine tryps
24  with the P1 residue of the bound inhibitors ecotin and bovine pancreatic trypsin inhibitor suggested
25 filled with eight consecutive amino acids of ecotin and demonstrates thrombin's preference for specif
26 nding site the molecular recognition between ecotin and its target serine proteases was probed.
27                      The interaction between ecotin and target proteases with trypsin-like specificit
28                                              Ecotin and variant ecotins are subnanomolar inhibitors o
29  the conformation of several loop regions of ecotin are altered, resulting in the secondary site rele
30                           Ecotin and variant ecotins are subnanomolar inhibitors of the MT-SP1 activa
31 is enzyme complexed to the protein inhibitor ecotin at 2.5 A resolution reveals a large primary bindi
32 d with the dimeric serine protease inhibitor ecotin at 2.5 A resolution reveals an extended cleft pro
33  trypsin at positions 143 and 151 and one on ecotin at position 86, anchor the metals and provide ext
34 e investigated with alanine substitutions in ecotin at Trp67, Gly68, Tyr69, Asp70, Arg108, Asn110, Ly
35 s than fivefold difference in the potency of ecotin binding to rat trypsin, suggesting that the exten
36                                              Ecotin binds to proteases with a chymotrypsin fold throu
37                             Furthermore, GGH-ecotin can be cross-linked to a serine protease target,
38  Met84(A)Gly resulted in the deactivation of ecotin, caused by peptide backbone cleavage at its P1 re
39 rypsin resulted in enrichment as well as the ecotin consensus sequence WGFP at positions 67 to 70.
40 ulted in enrichment as well as the different ecotin consensus sequence WGYR at positions 67 to 70.
41  ecotin variant (mEcotin) and a single-chain ecotin dimer (scEcotin) were constructed to study the ef
42                                          The ecotin dimer binds two protease molecules, and each ecot
43 reorganization of site1 and site2 within the ecotin dimer contributes to the inhibition of each MASP
44 development of compounds capable of blocking ecotin dimer formation.
45 that has an apparent molecular mass of a GGH-ecotin dimer with no observable protein degradation.
46 o the twofold rotational symmetry within the ecotin dimer, sites 1 and 2 of a protomer bind to differ
47                         We used a variant of ecotin (ecotin-PKal), a macromolecular inhibitor of seri
48 -tetramer with three distinct interfaces: an ecotin-ecotin dimer interface, a larger primary ecotin-p
49                                  The variant ecotin encoded by this sequence inhibited rat trypsin at
50                       The protease inhibitor ecotin fails to inhibit thrombin despite its broad speci
51 e synthesized by in vitro translation of the ecotin gene containing an engineered nonsense codon (TAG
52                                    Wild-type ecotin has an affinity of 1 nM for trypsin, while the op
53 efforts was taken to create potent bidentate ecotin inhibitors for trypsin and human urokinase-type p
54                             Escherichia coli ecotin inhibits trypsin-like, chymotrypsin-like, and ela
55 ey amino acids with histidine at the trypsin-ecotin interface in the S2'/P2' pocket.
56                                              Ecotin is a dimeric serine protease inhibitor from Esche
57                                              Ecotin is a homodimeric protein from Escherichia coli th
58                                              Ecotin is a homodimeric serine protease inhibitor produc
59    In the presence of Ni(OAc)2 and MMPP, GGH-ecotin is cross-linked to give a species that has an app
60 restricted tetranomial diversity, we created ecotin libraries that are mutated at all 20 amino acid r
61     A comparison with two recently described ecotin-like genes from other bacteria suggests that thes
62 y percent of L. major-knockout lines for the ecotin-like serine peptidase inhibitor (ISP2; Deltaisp2/
63                                 Thrombin and ecotin M84R interact in two distinct surfaces.
64 ovine thrombin is determined in complex with ecotin M84R mutant at 2.5 A resolution.
65                 A second generation library, ecotin M84R+60X4 including an additional methionine to a
66                                 Furthermore, ecotin M84R+D70R achieved a 13,680-fold preference of sp
67                                              Ecotin M84R+D70R bound to uPA at 50 pM, a 56,000-fold in
68                             The structure of ecotin M84R-FXa (M84R-FXa) also reveals the structure of
69                         We present the first ecotin:MASP-1 and ecotin:MASP-2 crystal structures, whic
70       We present the first ecotin:MASP-1 and ecotin:MASP-2 crystal structures, which provide addition
71 ence, and the structures of the rhFXI370-607-ecotin mutant complexes were determined.
72                              The presence of ecotin not only assisted in the crystallization of the e
73 ant p.G214R was inhibited poorly by eglin C, ecotin, or a CTRC-specific variant of SGPI-2, and it rea
74 nst bovine trypsin resulted in enrichment of ecotin phage but did not yield a consensus sequence.
75                                          Two ecotin phage display libraries were constructed to explo
76  to demonstrate that inhibition of PKal with ecotin-PKal delays alveolar apoptosis, adipocyte repleni
77                 We used a variant of ecotin (ecotin-PKal), a macromolecular inhibitor of serine prote
78                           Using biotinylated ecotin-PKal, we localized active PKal to connective tiss
79               The fact that the 60 s loop of ecotin plays different roles in binding to trypsin and u
80 tin-ecotin dimer interface, a larger primary ecotin-protease interface, and a smaller secondary ecoti
81 -protease interface, and a smaller secondary ecotin-protease interface.
82 he cross-linking reaction occurs between two ecotin proteins in a dimer complex.
83 dimer binds two protease molecules, and each ecotin protomer has two protease-binding sites: site1 oc
84                   A point mutation (M84R) in ecotin results in a 1.5 nM affinity for thrombin, 10(4)
85  through the use of wild-type and engineered ecotins results in inhibition of rat prostate differenti
86 sected to understand the structural basis of ecotin's broad inhibitory specificity and the role of th
87 egion-specific mutagenesis were preformed at ecotin's primary site P1 residue (84), the C-terminal di
88 rypsin and human uPA established the role of ecotin's secondary binding site in recognizing these hom
89 er secondary interaction between the partner ecotin subunit and the protease.
90                                          The ecotin surface loop that was redesigned is composed of r
91 acid substitution in the carboxy terminus of ecotin that places an engineered tyrosine within 5 A of
92 ue 99 and the C-terminus of thrombin contact ecotin through mixed polar and nonpolar interactions.
93 been developing the macromolecular inhibitor ecotin to be a "fold-specific" inhibitor that is selecti
94 using the three-dimensional structure of the ecotin-trypsin complex to guide combinatiorial design ef
95 cture of the previously determined wild-type ecotin-trypsin complex.
96 , we have solved the structure of two mutant ecotin-trypsin complexes and compared them to the struct
97  which has four alanine substitutions in the ecotin-trypsin secondary binding site, along with the M8
98 ses of the protein-protein interfaces in the ecotin-trypsin tetramer.
99 omplex shows minor structural changes in the ecotin-trypsin tetramer.
100                                              Ecotin undergoes a pronounced internal structural rearra
101                                  A monomeric ecotin variant (mEcotin) and a single-chain ecotin dimer
102   The structure of the tetrameric complex of ecotin variant M84R (M84R) with FXa has been determined
103 The contrast in the Ki values of the various ecotin variants towards bovine trypsin, rat trypsin and
104 ociation constants for monomeric and dimeric ecotin variants were determined with both trypsin and ch
105     In addition, using mutated and monomeric ecotin variants, we show that site1, site2, and dimeriza
106 rization constant (K(dim)) of wild-type (WT) ecotin was found to be picomolar by subunit exchange exp
107 Subsequently, the sequence from P5 to P2' in ecotin was mutated to the FXIa substrate sequence, and t
108 t position 84 in the primary binding site of ecotin, was generated for panning against uPA and rat tr
109  60X4 library, in which residues 67 to 70 of ecotin were randomized, was panned against rat and bovin
110                      Allylglycine-containing ecotins were synthesized by in vitro translation of the
111 trypsin at 80 pM, a 12-fold improvement over ecotin wild-type (WT).
112 nteractions of the secondary binding site of ecotin with bovine trypsin, rat trypsin and human urokin
113 ine protease factor Xa (FXa) is inhibited by ecotin with picomolar affinity.
114  56,000-fold increase in binding compared to ecotin WT.
115  nM for trypsin, while the optimized mutant, ecotin Y69F, D70P, which was found using phage display t
116                         The structure of the ecotin Y69F, D70P-trypsin complex shows minor structural

 
Page Top