ライフサイエンスコーパス: CDR1

1 CDR1 accumulates in intercellular fluid in response to p

2 CDR1 disruption had a partial effect, reducing fluconazo

3 CDR1 elements of both subunits of NITR dimers form ligan

4 ncoded complementarity determining region 1 (CDR1) and CDR2 of the V alpha element can be responsible

5 nts in complementarity-determining region 1 (CDR1) and CDR2, and less than two replacements in the fr

6 ted in complementarity-determining region 1 (CDR1) and CDR2, which exhibited higher replacement-to-si

7 chain complementarity determining region 1 (CDR1) of a humanized IgG1 monoclonal antibody.

8 30 in complementarity-determining region 1 (CDR1) of the TCR alpha-chain interacts with the I-A alph

9 ate in complementarity determining region 1 (CDR1) on zero, one, and two light chain arms.

10 er the complementarity-determining region 1 (CDR1) or CDR2 were sufficient to change selection from t

11 which complementarity-determining region 1 (CDR1), CDR2, and framework region 3 (FR3) are predicted

12 s 44-52, and one patient also responded to a CDR1 peptide.

13 We hypothesize that the V alpha CDR1 region recognizes NH2-terminal PFRs, while the V be

14 ormation of disulfide bonds between CDR3 and CDR1, FW2, or CDR2 was also observed, as described in ca

15 of CDR1 generates a small mobile signal, and CDR1 action is blocked by the protease inhibitor pepstat

16 Antisense CDR1 plants were compromised for resistance to avirulent

17 ts, the intrinsic probability of mutation at CDR1 can be almost twice that of CDR3.

18 cognizes NH2-terminal PFRs, while the V beta CDR1 region recognizes COOH-terminal PFRs.

19 termining region of the TcR beta chain (beta:CDR1) points outward and interacts with highly conserved

20 id-dependent cooperative interaction between CDR1 and CDR3 residues that are separated by more than 9

21 The epitope was recognized mainly by CDR1 and CDR2 of the heavy chain, which are highly conse

22 Movements of the CD8alpha CDR2 and CD8beta CDR1 and CDR2 loops as well as the flexibility of the H-

23 g to the anti-Id were located in heavy chain CDR1 and CDR2 and were peripheral to the residues within

24 geting non-germline hot spots in heavy chain CDR1 and CDR3 were generated but did not produce Fv with

25 ining region (CDR3) (H3) and its light chain CDR1 (L1) are closely associated.

26 human mAb; a large insert in the light chain CDR1 of mAb SN66E3 distinguished it from both CRll-351 a

27 ong HCDR3, and a deletion in the light chain CDR1.

28 interactions between the DRVIA7 light-chain CDR1 and the N terminus with N276 and V5 glycans of gp12

29 gnition was still dependent on the conserved CDR1/CDR2 residues.

30 16 microg ml(-1)) similarly show coordinate CDR1-PDH1 upregulation, and in one of these (F15) a puta

31 two parts of the CDR region here designated CDR1 and CDR2 (closest to the carboxyl end) each consist

32 ugs and express the drug efflux determinants CDR1, CDR2 and MDR1.

33 ity during Ag recognition while gene-encoded CDR1 and CDR2 contribute to the fine specificity of the

34 Within this hotspot, key germline-encoded CDR1 and CDR2 loop residues and a crucial but commonly c

35 transition state using the germline-encoded CDR1 and CDR2 loops.

36 and antibodies, whereas the germline-encoded CDR1 and CDR2 sequences are much more cross-reactive.

37 DR) loops that are either germ line-encoded (CDR1 and CDR2) or somatically rearranged (CDR3).

38 tified key positions in the VH gene encoding CDR1, CDR2, and the immunoglobulin framework that are cr

39 We found that the mRNA levels of ERG11, CDR1, CDR2, and MDR1, the candidate fluconazole resistan

40 2) of the beta-chain and, to lesser extents, CDR1 and hypervariable region 4 (HV4), bind in a cleft b

41 A few CDR1 and CDR2 amino acids dominated the most crossreacti

42 extends the database of canonical forms for CDR1 and CDR2, and has implications for antigen recognit

43 have explored the sequence requirements for CDR1 and CDR2 of the TCR alpha-chain in a human T cell r

44 chain variable region, including framework, CDR1, and CDR2 mutations.

45 Peptides derived from CDR1 of 44aacb, CDR2 of 118.1, and CDRs 1 and 3 of MY904

46 Evaluation of candidate genes CDR1 and SOX3 did not reveal mutations in affected male

47 ed expression of multidrug transporter genes CDR1 and PDH1.

48 However, mutagenesis of H:CDR1 did not result in such a specificity change despite

49 ficity change despite the proximity of the H:CDR1 hapten contact residue Asn-35 to the cardenolide 16

50 resistance of a cka2 mutant, as expected if CDR1 and CDR2 overexpression is responsible for fluconaz

51 Finally, we show that residue 29 in CDR1 of the TCR beta-chain affects recognition of the gl

52 n requirements for particular side chains in CDR1 and CDR2 and in their relative binding contribution

53 Replacing the overlapping hotspots in CDR1 and CDR2 with neutral or cold motifs resulted in a

54 among the VH and VL segments are located in CDR1 and -3.

55 Asp27d present in CDR1 formed hydrogen bonds with the side-chain and main-

56 so, when another carbohydrate was present in CDR1, CDR2, or CDR3 of the L chain, the V(H) CDR2 glycan

57 B:9-23 or that of two amino acid residues in CDR1 and 2 of the TRAV5D-4.

58 Mutational analysis of residues in CDR1 and CDR2 of the three Valpha2 regions showed the im

59 four putative solvent-accessible residues in CDR1 to A, D, S, or Y.

60 ant bias toward replacement substitutions in CDR1; in Tm clones there was no significant bias toward

61 ctedly, every TCR mutant, including those in CDR1 and CDR2, retained remarkable peptide specificity.

62 ed both constitutive and fluconazole-induced CDR1-PDH1 expression.

63 he catalytic subunits to CipA which involves CDR1, an IRE, and calcium.

64 Two mutations, D32H (L-CDR1) and E1K (L-FR1) altered the electrostatic surface

65 ng GD2 affinity, the double mutation D32H (L-CDR1) and E1K (L-FR1) did not further improve anti-tumor

66 t in affinity of hu3F8 with a single D32H (L-CDR1) mutation translated into a approximately 12-fold i

67 to block proliferation, with the activity of CDR1 > CDR2 > CDR4.

68 Combinations of CDR1 peptide with CDR2 or CDR4 peptides allosterically e

69 is flipped into a cavity formed by Gly35 of CDR1, thereby increasing the hydrophilicity of the V(H):

70 Induction of CDR1 generates a small mobile signal, and CDR1 action is

71 studies revealed transient overexpression of CDR1 and ERG11 mRNA in the presence of fluconazole that

72 he PPR and B2542 strains, the replacement of CDR1 of fCD134 (amino acids 1 to 64) with human CD134 (h

73 Finally, alanine scanning of CDR1 and CDR2 sequences of TRBV4-1 revealed two unique r

74 tides containing the amino acid sequences of CDR1 and CDR2 (designated bCDR1 and bCDR2) were synthesi

75 cka2 mutants overexpress CDR1 and CDR2, two fluconazole efflux transporter genes,

76 Two fluconazole efflux pumps, CDR1 and CDR2, were upregulated in the in vivo biofilm-a

77 uted at the peptidic termini at the putative CDR1 contact regions show improved recognition in B6 mic

78 est that some amino acids in variable region CDR1 and CDR2s almost always react in a consistent way w

79 uence, the complementary determining regions CDR1 and CDR3 of the TCR Valpha and Vbeta domains make t

80 ermline complementarity determining regions (CDR1 and 2) in MHC restriction is not well understood.

81 second complementarity determining regions (CDR1 and CDR2) of this Valpha are shorter than the CDRs

82 identified constitutive disease resistance (CDR1) encoding an apoplastic aspartic protease, the over

83 diverse peptides, and moderately diverse TCR CDR1 and CDR2 regions contact moderately diverse MHC alp

84 -MHC (pMHC) was mainly recognized by the TCR CDR1 and CDR2 loops in an MHC-centric manner.

85 In contrast, it has been argued that CDR1 and CDR2 are involved to a greater extent than CDR3

86 We propose that CDR1 mediates a peptide signal system involved in the ac

87 he TCRs in complex with QL9-L(d) showed that CDR1, CDR2, and CDR3beta conformations and docking orien

88 The CDR1 and CDR2 therefore represent new canonical forms th

89 The CDR1, CDR2 and CDR4 peptides were each able to block pro

90 of a VL, domain, which terminates before the CDR1 region.

91 unit(s) in the heterodimer or homodimer, the CDR1 loop of CD8beta tilts away from its corresponding C

92 The sequences in the CDR1 alpha and CDR2 alpha correlate with differential ex

93 This study shows that residues in the CDR1 and CDR2 regions are primary determinants for MHC c

94 identified and implies that residues in the CDR1 and CDR2-equivalent loops of CD8beta are occluded u

95 Other substitutions in the CDR1 loop and mutations spanning the CDR2 and DE loops h

96 hat alanine substitutions of residues in the CDR1 loop of CD8beta have no effect on CD8alphabeta core

97 rangement by aspartic acid residue 31 in the CDR1 on the light chain.

98 If the overlapping hotspots in the CDR1 or CDR2 did not undergo mutation, the frequency of

99 ally, 8 of 9 of these events occurred in the CDR1 or CDR2, following a pattern consistent with select

100 beta mutants and identified mutations in the CDR1, CDR2, and CDR3 loops that decreased binding to MHC

101 e conservative F substitution of Y 26 in the CDR1-like region also reduced binding to CD80 and CD86.

102 share a lysine to glutamate mutation in the CDR1.

103 nment of the V region, and especially of the CDR1 and CDR2, is highly evolved to recruit mutations to

104 gs are inconsistent with the notion that the CDR1 and CDR2 loops of the TCR are responsible for MHC r

105 We conclude that the CDR1 and CDR3 regions contribute to a common binding sit

106 all conformational changes, localized to the CDR1 contact regions, may play a significant role in TCR

107 of homologous peptides corresponding to the CDR1 segments of human Vbeta gene products, a major epit

108 ay play a role through interactions with the CDR1.

109 erminal of the MYPPPY region, and within the CDR1-like region of CTLA-4, eliminated both CD80 and CD8

110 and neonate in the first 6 weeks have unique CDR1 and CDR2 sequences, permitting each to be identifie

111 owever, so-called "hybrid" VH genes that use CDR1 of one VH gene and the CDR2 of another are frequent

112 en interacts with some portion of the Valpha CDR1 or CDR2 region.

113 utations in the first residue of the Valpha, CDR1, CDR2, or CDR3 were isolated.

114 volutionarily selected germline Valpha/Vbeta CDR1/CDR2 loops to create highly MHC/peptide cross-react

115 In the current studies, such CDRs were CDR1 of the heavy chain (H1) and CDR2 of the light chain

116 , RSB1, RPN4, YLR346c and YMR102c along with CDR1, PDH1 and PDR1 itself) or downregulated (PDR12); ro

117 lementarity-determining regions (CDRs), with CDR1 and CDR2 encoded by the V segment and CDR3 encoded

118 exclusively bearing VDJ rearrangements with CDR1, CDR2, and nearly intact DH segments in germline co

119 a germline hot spot (Ser(30)-Asn(31)) within CDR1 of the antibody light chain was mutated.

120 a specific asparagine residue located within CDR1 and occurs with complete loss of CDR2.