ライフサイエンスコーパス: monobody

1 favorable enthalpic contribution than the YS monobody.

2 unprecedented potency and selectivity using monobodies.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

27 The monobodies inhibited SUMO1/SIM interactions and, unexpec

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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