ライフサイエンスコーパス: monobody

1 favorable enthalpic contribution than the YS monobody.

2 ng methods to enable cytoplasmic delivery of monobodies.

3 unprecedented potency and selectivity using monobodies.

4 c supercharging to generate cell-penetrating monobodies.

5 constitutively binds the MLKL hinge region, Monobody-27 binds MLKL via an epitope that overlaps the

6 While Monobody-32 constitutively binds the MLKL hinge region,

7 first determined the crystal structure of a "monobody," a designed binding protein based on the fibro

8 Structure-guided point mutants and the monobody abrogated the Prdm14-Mtgr1 association and disr

9 gly, we identify a series of highly specific monobodies acting either as strong kinase inhibitors or

10 Our monobody adapter also enables a simple plug-and-play cap

11 e, we overcome this barrier by engineering a monobody adapter that presents antibodies on the NP surf

12 The monobody also directly interacted with H95, a residue no

13 The ATOM design was validated with three monobodies and one nanobody inserted into distinct fluor

14 owed by interactome analysis showed that the monobodies are essentially monospecific to SHP2.

15 These monobodies are highly selective for STAT3 and bind with

16 D-monobodies are protease-resistant, show long-term plasma

17 Monobodies are synthetic non-immunoglobulin customizable

18 Monobodies are well-established synthetic (L-)binding pr

19 ion for the SH2 domains of SHP2 and validate monobodies as potent and specific antagonists of protein

20 rochemical biosensor utilizing an engineered monobody as a biorecognition element for the detection o

21 By using the monobody as a probe for the accessibility of the PTP act

22 main, revealed that a concave surface of the monobody, as intended in our design, bound to a convex s

23 inal beta-strand of a series of supercharged monobodies, BeLaK enabled efficient inter-strand crossli

24 simultaneously occupied, and if so, whether monobodies bind independently or cooperatively to their

25 s structure illustrated a mechanism by which monobodies bind to the highly conserved SIM-binding site

26 utoinhibition and T-cell receptor signaling, monobodies binding the Src and Hck SH2 domains selective

27 An engineered monobody binding protein was immobilized onto glassy car

28 Monobody binding proteins are derived from the Fn3 domai

29 Here, we use direct monobody-binding assays and single-channel recordings of

30 s demands that the two chemically equivalent monobody-binding epitopes reside on opposite ends of the

31 anoeuvre, we show that Fluc channels present monobody-binding epitopes to both sides of the membrane.

32 An X-ray crystal structure revealed a monobody-binding site centered on the alpha4 helix of th

33 f the monobody-PTP complex revealed that the monobody bound both highly conserved residues in the act

34 mpared to the monomeric form, the pentameric monobody bound to alphavbeta3 integrin much more tightly

35 RAS mutant-selective inhibitors, the initial monobody bound to the S-II pocket, the groove between sw

36 The YSX monobody bound with higher affinity, a slower off rate a

37 We then prepare potent D-monobodies by either ligating two chemically synthesized

38 Hence, we demonstrate that functional D-monobodies can be developed readily.

39 Further, this monobody can be formatted into a genetically encoded NRA

40 single-chain VHH antibody or a supercharged monobody, CATK-1 enabled site-specific, inter-strand, or

41 maturation (ATOM) biosensors consisting of a monobody (circularly permuted at one of two positions) o

42 Most of these monobodies competed with pY ligand binding and showed st

43 monstrated by mapping the interface of a RAS-monobody complex, the surface of the NIST mAb, and the i

44 type III scaffold, termed "monobodies." One monobody contains the Tyr/Ser binary-code interface (ter

45 Here, we aimed to examine if the FN3Con monobody could take on antibody-like binding to therapeu

46 e previously developed FN3Con, a hyperstable monobody derivative with diagnostic and therapeutic pote

47 We generated a panel of high-affinity monobodies directed to each of these domains, from which

48 ion of two designed binding proteins, termed monobodies, directed to the interaction interface betwee

49 inked monobody, the orthogonally crosslinked monobody displayed improved cellular uptake and enhanced

50 The fibronectin type III (FN3) monobody domain is a promising non-antibody scaffold, wh

51 is a viable strategy for the development of monobody domains with desirable biophysical characterist

52 cells as genetically encoded reagents, these monobodies engaged selectively with KRAS(G12D) and inhib

53 ounterpart, a BeLaK-crosslinked, +18-charged monobody exhibited enhanced thermostability and greater

54 pathway and demonstrate that these FN3-based MONOBODYs (FNDYs) can be used to perturb protein activit

55 AR to identify pairs of fibronectin type III monobodies for three human proteins.

56 developed synthetic binding proteins, termed monobodies, for six of the SFK SH2 domains with nanomola

57 We have developed binding proteins, termed monobodies, for the N- and C-terminal SH2 domains of SHP

58 Intracellular expression of monobodies fused to VHL, an E3 ubiquitin ligase substrat

59 The crystal structure of a monobody generated from the new library in complex with

60 Deep mutational scanning of a monobody generated hundreds of functional and nonfunctio

61 excipients doubled the presence of monomeric monobody in accelerated stability trials.

62 A 2.35-A x-ray crystal structure of a monobody in complex with its target, maltose-binding pro

63 Importantly, the new monobodies inhibited Bcr-Abl kinase activity in vitro an

64 The monobodies inhibited SUMO1/SIM interactions and, unexpec

65 , this structurally rigidified, supercharged monobody inhibited ERK1/2 phosphorylation in KYSE-520 es

66 ombinant kinases, whereas an Lck SH2-binding monobody inhibited proximal signaling events downstream

67 c homologues in complex with three different monobody inhibitors, with and without F(-) present, to a

68 Because the latter monobody inhibits processive phosphorylation by Bcr-Abl

69 Square wave voltammetry of resulting monobody-modified electrodes revealed a significant decr

70 e crystal structure of STAT3 in complex with monobody MS3-6 reveals bending of the coiled-coil domain

71 Building upon our previous studies with the monobody NS1 that recognizes HRAS and KRAS but not NRAS,

72 Two crystal structures revealed that the monobodies occupy the phosphopeptide-binding sites of th

73 lysis of single-channel recordings made with monobody on both sides of the membrane shows substantial

74 n the fibronectin type III scaffold, termed "monobodies." One monobody contains the Tyr/Ser binary-co

75 ciple, the development of a light-controlled monobody (OptoMB) that works in vitro and in cells and w

76 ked by nanomolar-affinity fibronectin-domain monobodies originally selected from phage-display librar

77 When incorporated into a monobody, PhoBIT2 allows photo-switchable inhibition of

78 FN3 domain, the scaffold for the widely used monobody platform.

79 genetically encoded reagents in cells, these monobodies potently block necroptotic cell death.

80 Domain antibodies such as monobodies provide an attractive immunoglobin fold for e

81 A crystal structure of the monobody-PTP complex revealed that the monobody bound bo

82 aring AurA bound to activating vs inhibiting monobodies reveal the atomistic mechanism underlying all

83 actome analysis of intracellularly expressed monobodies revealed that they bind SFKs but no other SH2

84 GPCR ECR, in complex with an inverse-agonist monobody, revealing a GPCR-Autoproteolysis-Inducing doma

85 By applying monobodies sequentially to the two sides of the bilayer

86 Two crystal structures of heterochiral monobody-SH2 complexes reveal targeting of the pY bindin

87 Three crystal structures of monobody-SH2 complexes unveiled different and only partl

88 revealed the molecular underpinnings of the monobody-SH2 interactions.

89 erformed combinatorial library screening of "monobodies" (small antibody mimics using the scaffold of

90 Here, we have developed monobodies, small synthetic binding proteins, that are s

91 gand complex of ER alpha, and the pattern of monobody specificity was consistent with the structural

92 We generated two monobodies, synthetic binding proteins, targeting the Pr

93 Here we have developed monobodies, synthetic binding proteins, that bind the N-

94 Here, we report Monobodies, synthetic binding proteins, that bind the ps

95 Here, we developed a monobody, synthetic binding protein, that bound to and i

96 among the largest of published structures of monobody-target complexes.

97 ld facilitate the design of cell-penetrating monobodies targeting intracellular signalling proteins.

98 When expressed in cells, monobodies targeting the N-SH2 domain disrupted the inte

99 rization interface with a novel RAS-specific monobody termed NS1.

100 Here, we report a monobody, termed 12VC1, that recognizes the active state

101 Here, we report a pan-RAS monobody, termed JAM20, that bound to all RAS isoforms w

102 oach to controlling kinase activity by using monobodies that bind to the highly specific regulatory a

103 Surprisingly, the segments of both monobodies that bind to the peptide-binding grooves run

104 SUMO-targeted library from which we obtained monobodies that bound to the SIM-binding site of human S

105 oyed small synthetic binding proteins termed monobodies that have a strong propensity to bind to func

106 library using a highly flexible loop yielded monobodies that specifically recognize a particular liga

107 te a fibronectin type III domain (FN3) based monobody that binds to the tumor-related biomarkers with

108 ot NRAS, here we report the development of a monobody that specifically binds to both GDP and GTP-bou

109 ) intrabody or a fibronectin type III domain monobody that target their respective antigens with high

110 eviously-reported synthetic proteins, termed monobodies, that bind the GPR56 ECR in a domain- and spe

111 s, we generated synthetic binding proteins, 'monobodies,' that specifically bind to Fluc homologues w

112 Compared with a non-crosslinked monobody, the orthogonally crosslinked monobody displaye

113 ting Tyr side chains are essential in the YS monobody, the YSX interface was more tolerant to mutatio

114 here could be applied to engineer other FN3 monobodies to acquire significantly improved targeting-b

115 work demonstrates significant potential for monobodies to expand the existing toolkit of electrochem

116 eted the first of the Adnectin derivative of monobodies to reach clinical trials, which was engineere

117 to the LBD increased the crossreactivity of monobodies to the apo-ER alpha-LBD, suggesting a dynamic

118 It also revealed that previously developed monobodies to the SH2 domains, ligands lacking a phospho

119 Reversible binding of monobodies to two different Fluc channel homologues is s

120 w library produced binding proteins (termed "monobodies") to multiple target proteins, generally with

121 develop synthetic antibody mimetics, termed monobodies, to interfere with STAT3 signaling.

122 selective polypeptides reported to date, the monobody used its backbone NH group to directly recogniz

123 towards possible future therapeutic use of D-monobodies when combined with emerging methods to enable

124 Indeed, the NS1 monobody, which binds the alpha4-alpha5 region within th

125 cture-guided affinity maturation resulted in monobodies with low nM K(D) values.

126 Here, we develop monobodies with nanomolar binding affinities against the

127 question, we generated new, higher affinity monobodies with single nanomolar KD values targeting the

128 trategy by fusing an alphavbeta3-binding FN3 monobody with a short COMP pentamerization domain throug

129 producing specific binding proteins (termed "monobodies") with a low-nanomolar K(d).