Crystal structure of the Frizzled 4 receptor in a ligand-free state

Frizzled receptors (FZDs) are class-F G-protein-coupled receptors (GPCRs) that function in Wnt signalling and are essential for developing and adult organisms 1 , 2 . As central mediators in this complex signalling pathway, FZDs serve as gatekeeping proteins both for drug intervention and for the de...

Full description

Saved in:
Bibliographic Details
Published inNature (London) Vol. 560; no. 7720; pp. 666 - 670
Main Authors Yang, Shifan, Wu, Yiran, Xu, Ting-Hai, de Waal, Parker W., He, Yuanzheng, Pu, Mengchen, Chen, Yuxiang, DeBruine, Zachary J., Zhang, Bingjie, Zaidi, Saheem A., Popov, Petr, Guo, Yu, Han, Gye Won, Lu, Yang, Suino-Powell, Kelly, Dong, Shaowei, Harikumar, Kaleeckal G., Miller, Laurence J., Katritch, Vsevolod, Xu, H. Eric, Shui, Wenqing, Stevens, Raymond C., Melcher, Karsten, Zhao, Suwen, Xu, Fei
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group UK 01.08.2018
Nature Publishing Group
Subjects
101/58
119/118
13/109
13/95
631/1647/2258/1266
631/80/86
82/16
82/80
82/83
Activation
Alzheimer's disease
Atomic structure
Binding
Binding Sites
Bioinformatics
Crystal structure
Crystallography, X-Ray
Cysteine - metabolism
Dishevelled Proteins - metabolism
Free form
Frizzled protein
Frizzled Receptors - chemistry
Frizzled Receptors - genetics
G protein-coupled receptors
G proteins
Humanities and Social Sciences
Humans
Letter
Ligands
Models, Molecular
Molecular dynamics
Molecular Dynamics Simulation
multidisciplinary
Mutation
Observations
Physiological aspects
Protein Domains
Proteins
Receptor mechanisms
Receptors
Science
Science (multidisciplinary)
Signal transduction
Signaling
Structural stability
Structure
Wnt protein
Wnt Signaling Pathway
Online AccessGet full text

Cover

Abstract Frizzled receptors (FZDs) are class-F G-protein-coupled receptors (GPCRs) that function in Wnt signalling and are essential for developing and adult organisms 1 , 2 . As central mediators in this complex signalling pathway, FZDs serve as gatekeeping proteins both for drug intervention and for the development of probes in basic and in therapeutic research. Here we present an atomic-resolution structure of the human Frizzled 4 receptor (FZD4) transmembrane domain in the absence of a bound ligand. The structure reveals an unusual transmembrane architecture in which helix VI is short and tightly packed, and is distinct from all other GPCR structures reported so far. Within this unique transmembrane fold is an extremely narrow and highly hydrophilic pocket that is not amenable to the binding of traditional GPCR ligands. We show that such a pocket is conserved across all FZDs, which may explain the long-standing difficulties in the development of ligands for these receptors. Molecular dynamics simulations on the microsecond timescale and mutational analysis uncovered two coupled, dynamic kinks located at helix VII that are involved in FZD4 activation. The stability of the structure in its ligand-free form, an unfavourable pocket for ligand binding and the two unusual kinks on helix VII suggest that FZDs may have evolved a novel ligand-recognition and activation mechanism that is distinct from that of other GPCRs. The crystal structure of the Frizzled 4 receptor transmembrane domain is reported to a resolution of 2.4 Å in a ligand-free state.
AbstractList Frizzled receptors (FZDs) are class-F G-protein-coupled receptors (GPCRs) that function in Wnt signalling and are essential for developing and adult organisms.sup.1,2. As central mediators in this complex signalling pathway, FZDs serve as gatekeeping proteins both for drug intervention and for the development of probes in basic and in therapeutic research. Here we present an atomic-resolution structure of the human Frizzled 4 receptor (FZD4) transmembrane domain in the absence of a bound ligand. The structure reveals an unusual transmembrane architecture in which helix VI is short and tightly packed, and is distinct from all other GPCR structures reported so far. Within this unique transmembrane fold is an extremely narrow and highly hydrophilic pocket that is not amenable to the binding of traditional GPCR ligands. We show that such a pocket is conserved across all FZDs, which may explain the long-standing difficulties in the development of ligands for these receptors. Molecular dynamics simulations on the microsecond timescale and mutational analysis uncovered two coupled, dynamic kinks located at helix VII that are involved in FZD4 activation. The stability of the structure in its ligand-free form, an unfavourable pocket for ligand binding and the two unusual kinks on helix VII suggest that FZDs may have evolved a novel ligand-recognition and activation mechanism that is distinct from that of other GPCRs.The crystal structure of the Frizzled 4 receptor transmembrane domain is reported to a resolution of 2.4 Å in a ligand-free state.
Frizzled receptors (FZDs) are class-F G-protein-coupled receptors (GPCRs) that function in Wnt signalling and are essential for developing and adult organisms.sup.1,2. As central mediators in this complex signalling pathway, FZDs serve as gatekeeping proteins both for drug intervention and for the development of probes in basic and in therapeutic research. Here we present an atomic-resolution structure of the human Frizzled 4 receptor (FZD4) transmembrane domain in the absence of a bound ligand. The structure reveals an unusual transmembrane architecture in which helix VI is short and tightly packed, and is distinct from all other GPCR structures reported so far. Within this unique transmembrane fold is an extremely narrow and highly hydrophilic pocket that is not amenable to the binding of traditional GPCR ligands. We show that such a pocket is conserved across all FZDs, which may explain the long-standing difficulties in the development of ligands for these receptors. Molecular dynamics simulations on the microsecond timescale and mutational analysis uncovered two coupled, dynamic kinks located at helix VII that are involved in FZD4 activation. The stability of the structure in its ligand-free form, an unfavourable pocket for ligand binding and the two unusual kinks on helix VII suggest that FZDs may have evolved a novel ligand-recognition and activation mechanism that is distinct from that of other GPCRs.
Frizzled receptors (FZDs) are class-F G-protein-coupled receptors (GPCRs) that function in Wnt signalling and are essential for developing and adult organisms1,2. As central mediators in this complex signalling pathway, FZDs serve as gatekeeping proteins both for drug intervention and for the development of probes in basic and in therapeutic research. Here we present an atomic-resolution structure of the human Frizzled 4 receptor (FZD4) transmembrane domain in the absence of a bound ligand. The structure reveals an unusual transmembrane architecture in which helix VI is short and tightly packed, and is distinct from all other GPCR structures reported so far. Within this unique transmembrane fold is an extremely narrow and highly hydrophilic pocket that is not amenable to the binding of traditional GPCR ligands. We show that such a pocket is conserved across all FZDs, which may explain the long-standing difficulties in the development of ligands for these receptors. Molecular dynamics simulations on the microsecond timescale and mutational analysis uncovered two coupled, dynamic kinks located at helix VII that are involved in FZD4 activation. The stability of the structure in its ligand-free form, an unfavourable pocket for ligand binding and the two unusual kinks on helix VII suggest that FZDs may have evolved a novel ligand-recognition and activation mechanism that is distinct from that of other GPCRs.
Frizzled receptors (FZDs) are class-F G-protein-coupled receptors (GPCRs) that function in Wnt signalling and are essential for developing and adult organisms 1 , 2 . As central mediators in this complex signalling pathway, FZDs serve as gatekeeping proteins both for drug intervention and for the development of probes in basic and in therapeutic research. Here we present an atomic-resolution structure of the human Frizzled 4 receptor (FZD4) transmembrane domain in the absence of a bound ligand. The structure reveals an unusual transmembrane architecture in which helix VI is short and tightly packed, and is distinct from all other GPCR structures reported so far. Within this unique transmembrane fold is an extremely narrow and highly hydrophilic pocket that is not amenable to the binding of traditional GPCR ligands. We show that such a pocket is conserved across all FZDs, which may explain the long-standing difficulties in the development of ligands for these receptors. Molecular dynamics simulations on the microsecond timescale and mutational analysis uncovered two coupled, dynamic kinks located at helix VII that are involved in FZD4 activation. The stability of the structure in its ligand-free form, an unfavourable pocket for ligand binding and the two unusual kinks on helix VII suggest that FZDs may have evolved a novel ligand-recognition and activation mechanism that is distinct from that of other GPCRs. The crystal structure of the Frizzled 4 receptor transmembrane domain is reported to a resolution of 2.4 Å in a ligand-free state.
Frizzled receptors (FZDs) are class-F G-protein-coupled receptors (GPCRs) that function in Wnt signalling and are essential for developing and adult organisms1,2. As central mediators in this complex signalling pathway, FZDs serve as gatekeeping proteins both for drug intervention and for the development of probes in basic and in therapeutic research. Here we present an atomic-resolution structure of the human Frizzled 4 receptor (FZD4) transmembrane domain in the absence of a bound ligand. The structure reveals an unusual transmembrane architecture in which helix VI is short and tightly packed, and is distinct from all other GPCR structures reported so far. Within this unique transmembrane fold is an extremely narrow and highly hydrophilic pocket that is not amenable to the binding of traditional GPCR ligands. We show that such a pocket is conserved across all FZDs, which may explain the long-standing difficulties in the development of ligands for these receptors. Molecular dynamics simulations on the microsecond timescale and mutational analysis uncovered two coupled, dynamic kinks located at helix VII that are involved in FZD4 activation. The stability of the structure in its ligand-free form, an unfavourable pocket for ligand binding and the two unusual kinks on helix VII suggest that FZDs may have evolved a novel ligand-recognition and activation mechanism that is distinct from that of other GPCRs.
Frizzled receptors (FZDs) are class-F G-protein-coupled receptors (GPCRs) that function in Wnt signalling and are essential for developing and adult organisms . As central mediators in this complex signalling pathway, FZDs serve as gatekeeping proteins both for drug intervention and for the development of probes in basic and in therapeutic research. Here we present an atomic-resolution structure of the human Frizzled 4 receptor (FZD4) transmembrane domain in the absence of a bound ligand. The structure reveals an unusual transmembrane architecture in which helix VI is short and tightly packed, and is distinct from all other GPCR structures reported so far. Within this unique transmembrane fold is an extremely narrow and highly hydrophilic pocket that is not amenable to the binding of traditional GPCR ligands. We show that such a pocket is conserved across all FZDs, which may explain the long-standing difficulties in the development of ligands for these receptors. Molecular dynamics simulations on the microsecond timescale and mutational analysis uncovered two coupled, dynamic kinks located at helix VII that are involved in FZD4 activation. The stability of the structure in its ligand-free form, an unfavourable pocket for ligand binding and the two unusual kinks on helix VII suggest that FZDs may have evolved a novel ligand-recognition and activation mechanism that is distinct from that of other GPCRs.
Audience Academic
Author DeBruine, Zachary J.
Xu, Ting-Hai
Xu, H. Eric
He, Yuanzheng
Wu, Yiran
Pu, Mengchen
Harikumar, Kaleeckal G.
Chen, Yuxiang
Zaidi, Saheem A.
Yang, Shifan
Katritch, Vsevolod
Popov, Petr
Miller, Laurence J.
Guo, Yu
Zhang, Bingjie
Suino-Powell, Kelly
Han, Gye Won
Melcher, Karsten
Lu, Yang
Zhao, Suwen
Stevens, Raymond C.
Dong, Shaowei
de Waal, Parker W.
Shui, Wenqing
Xu, Fei
Author_xml – sequence: 1
  givenname: Shifan
  surname: Yang
  fullname: Yang, Shifan
  organization: iHuman Institute, ShanghaiTech University
– sequence: 2
  givenname: Yiran
  surname: Wu
  fullname: Wu, Yiran
  organization: iHuman Institute, ShanghaiTech University
– sequence: 3
  givenname: Ting-Hai
  surname: Xu
  fullname: Xu, Ting-Hai
  organization: Center for Cancer and Cell Biology, Innovation and Integration Program, Van Andel Research Institute
– sequence: 4
  givenname: Parker W.
  surname: de Waal
  fullname: de Waal, Parker W.
  organization: Center for Cancer and Cell Biology, Innovation and Integration Program, Van Andel Research Institute
– sequence: 5
  givenname: Yuanzheng
  surname: He
  fullname: He, Yuanzheng
  organization: HIT Center for Life Sciences, School of Life Science and Technology, Harbin Institute of Technology
– sequence: 6
  givenname: Mengchen
  surname: Pu
  fullname: Pu, Mengchen
  organization: iHuman Institute, ShanghaiTech University
– sequence: 7
  givenname: Yuxiang
  surname: Chen
  fullname: Chen, Yuxiang
  organization: iHuman Institute, ShanghaiTech University, School of Life Science and Technology, ShanghaiTech University, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, University of Chinese Academy of Sciences
– sequence: 8
  givenname: Zachary J.
  surname: DeBruine
  fullname: DeBruine, Zachary J.
  organization: Center for Cancer and Cell Biology, Innovation and Integration Program, Van Andel Research Institute
– sequence: 9
  givenname: Bingjie
  surname: Zhang
  fullname: Zhang, Bingjie
  organization: iHuman Institute, ShanghaiTech University
– sequence: 10
  givenname: Saheem A.
  surname: Zaidi
  fullname: Zaidi, Saheem A.
  organization: Departments of Biological Sciences and Chemistry, Bridge Institute, University of Southern California
– sequence: 11
  givenname: Petr
  surname: Popov
  fullname: Popov, Petr
  organization: Departments of Biological Sciences and Chemistry, Bridge Institute, University of Southern California, Moscow Institute of Physics and Technology
– sequence: 12
  givenname: Yu
  surname: Guo
  fullname: Guo, Yu
  organization: iHuman Institute, ShanghaiTech University, School of Life Science and Technology, ShanghaiTech University, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, University of Chinese Academy of Sciences
– sequence: 13
  givenname: Gye Won
  surname: Han
  fullname: Han, Gye Won
  organization: Departments of Biological Sciences and Chemistry, Bridge Institute, University of Southern California
– sequence: 14
  givenname: Yang
  surname: Lu
  fullname: Lu, Yang
  organization: HIT Center for Life Sciences, School of Life Science and Technology, Harbin Institute of Technology
– sequence: 15
  givenname: Kelly
  surname: Suino-Powell
  fullname: Suino-Powell, Kelly
  organization: Center for Cancer and Cell Biology, Innovation and Integration Program, Van Andel Research Institute
– sequence: 16
  givenname: Shaowei
  surname: Dong
  fullname: Dong, Shaowei
  organization: iHuman Institute, ShanghaiTech University, School of Life Science and Technology, ShanghaiTech University, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, University of Chinese Academy of Sciences
– sequence: 17
  givenname: Kaleeckal G.
  surname: Harikumar
  fullname: Harikumar, Kaleeckal G.
  organization: Department of Molecular Pharmacology and Experimental Therapeutics, Mayo Clinic
– sequence: 18
  givenname: Laurence J.
  surname: Miller
  fullname: Miller, Laurence J.
  organization: Department of Molecular Pharmacology and Experimental Therapeutics, Mayo Clinic
– sequence: 19
  givenname: Vsevolod
  surname: Katritch
  fullname: Katritch, Vsevolod
  organization: Departments of Biological Sciences and Chemistry, Bridge Institute, University of Southern California, Moscow Institute of Physics and Technology
– sequence: 20
  givenname: H. Eric
  surname: Xu
  fullname: Xu, H. Eric
  organization: Center for Cancer and Cell Biology, Innovation and Integration Program, Van Andel Research Institute, Key Laboratory of Receptor Research, VARI-SIMM Center, Center for Structure and Function of Drug Targets, Shanghai Institute of Materia Medica, Chinese Academy of Sciences
– sequence: 21
  givenname: Wenqing
  surname: Shui
  fullname: Shui, Wenqing
  organization: iHuman Institute, ShanghaiTech University, School of Life Science and Technology, ShanghaiTech University
– sequence: 22
  givenname: Raymond C.
  surname: Stevens
  fullname: Stevens, Raymond C.
  organization: iHuman Institute, ShanghaiTech University, School of Life Science and Technology, ShanghaiTech University
– sequence: 23
  givenname: Karsten
  surname: Melcher
  fullname: Melcher, Karsten
  organization: Center for Cancer and Cell Biology, Innovation and Integration Program, Van Andel Research Institute
– sequence: 24
  givenname: Suwen
  surname: Zhao
  fullname: Zhao, Suwen
  organization: iHuman Institute, ShanghaiTech University, School of Life Science and Technology, ShanghaiTech University
– sequence: 25
  givenname: Fei
  surname: Xu
  fullname: Xu, Fei
  email: xufei@shanghaitech.edu.cn
  organization: iHuman Institute, ShanghaiTech University, School of Life Science and Technology, ShanghaiTech University
BackLink https://www.ncbi.nlm.nih.gov/pubmed/30135577$$D View this record in MEDLINE/PubMed
BookMark eNp1kt1rFDEUxYNU7Lb6B_gig33Rh6k3X5PMY1msFgqCH88hTW7GKbMz2yQD2_71ZtlqXVnJQyDndw6Xm3NCjsZpREJeUzinwPWHJKjUTQ1U1yCEqjfPyIIK1dSi0eqILABYUTRvjslJSrcAIKkSL8gxB8qlVGpBlst4n7IdqpTj7PIcsZpClX9idRn7h4cBfSWqiA7XeYpVP1a2GvrOjr4OEbG4bMaX5HmwQ8JXj_cp-XH58fvyc3395dPV8uK6dg2IXItgb6wMCF4x3_IWGejGh0A9bbVrXWu5R8uhcVRrrlUA7oMU0vMiemj4KXm3y13H6W7GlM2qTw6HwY44zckwaJnknCle0LN_0NtpjmOZzjBKGZVMCPlEdXZA049hytG6bai5kIppLgSoQtUHqA5HjHYoHxL68rzHvz3Au3V_Z_6Gzg9A5Xhc9e5g6vs9Q2EybnJn55TM1bev-yzdsS5OKUUMZh37lY33hoLZNsfsmmNKc8y2OWZTPG8eNzbfrND_cfyuSgHYDkhFGjuMTyv9f-ovh8zLDA
CitedBy_id crossref_primary_10_1001_jamaophthalmol_2022_2914
crossref_primary_10_1111_bcpt_13235
crossref_primary_10_1016_j_phrs_2024_107286
crossref_primary_10_1042_BST20220634
crossref_primary_10_1186_s10020_019_0129_7
crossref_primary_10_1038_s41598_022_21063_0
crossref_primary_10_7554_eLife_58464
crossref_primary_10_1038_s41421_023_00627_y
crossref_primary_10_1134_S0022093023070013
crossref_primary_10_1002_advs_202200750
crossref_primary_10_1186_s43556_023_00156_w
crossref_primary_10_1038_s41596_019_0259_y
crossref_primary_10_1016_j_cell_2020_11_038
crossref_primary_10_1038_s41467_021_24731_3
crossref_primary_10_1155_2019_5782536
crossref_primary_10_31857_S0044452923070021
crossref_primary_10_1038_s41594_019_0252_8
crossref_primary_10_1074_jbc_RA118_004763
crossref_primary_10_1007_s11033_021_06449_z
crossref_primary_10_1126_sciadv_abj9748
crossref_primary_10_1134_S0006297923140110
crossref_primary_10_1016_j_bcp_2021_114647
crossref_primary_10_1002_1873_3468_14903
crossref_primary_10_1016_j_pep_2020_105569
crossref_primary_10_1021_acs_jmedchem_2c01795
crossref_primary_10_1021_acs_jmedchem_0c01974
crossref_primary_10_1038_s41586_019_1286_0
crossref_primary_10_1007_s00018_021_03968_7
crossref_primary_10_1021_acs_jmedchem_9b02020
crossref_primary_10_1074_jbc_REV118_005205
crossref_primary_10_1038_s42003_022_03370_4
crossref_primary_10_1016_j_tips_2024_03_003
crossref_primary_10_1038_s41467_019_14149_3
crossref_primary_10_1126_sciadv_abj7917
crossref_primary_10_1073_pnas_2218238120
crossref_primary_10_1186_s13765_022_00735_5
crossref_primary_10_1016_j_sbi_2019_02_009
crossref_primary_10_1038_s41467_019_08630_2
crossref_primary_10_1007_s12672_021_00429_2
crossref_primary_10_1038_s41467_021_24004_z
crossref_primary_10_1042_BST20200243
crossref_primary_10_1016_j_aca_2019_12_036
crossref_primary_10_1016_j_sbi_2019_05_015
crossref_primary_10_1186_s12886_022_02252_x
crossref_primary_10_1124_pr_119_017863
crossref_primary_10_1016_j_jbc_2022_101628
crossref_primary_10_1038_s41419_020_02978_w
crossref_primary_10_1124_mol_119_117986
crossref_primary_10_3727_096504020X16014648664459
crossref_primary_10_1167_iovs_65_4_1
crossref_primary_10_7554_eLife_75751
crossref_primary_10_1016_j_tibs_2018_09_002
crossref_primary_10_1242_jcs_259547
crossref_primary_10_1016_j_devcel_2022_05_006
crossref_primary_10_1038_s41392_023_01427_2
crossref_primary_10_1039_D0OB02175J
crossref_primary_10_1038_s41392_020_00435_w
crossref_primary_10_1016_j_bios_2020_112948
crossref_primary_10_1038_s41594_019_0216_z
crossref_primary_10_1016_j_heliyon_2024_e29733
crossref_primary_10_1111_bph_16325
crossref_primary_10_3390_ph15111304
crossref_primary_10_52711_0974_360X_2023_00665
crossref_primary_10_1038_s41401_024_01270_3
crossref_primary_10_1038_s41422_021_00525_6
crossref_primary_10_1002_bies_202000297
crossref_primary_10_1016_j_jnutbio_2023_109489
crossref_primary_10_1186_s12935_021_02278_z
crossref_primary_10_3389_fonc_2022_1096134
Cites_doi 10.1038/nature12167
10.7554/eLife.34729
10.1093/bioinformatics/btk023
10.1126/science.1222879
10.1002/0471250953.bi0506s15
10.1038/nrd4233
10.1016/j.bpj.2015.08.015
10.1038/cr.2015.92
10.1016/bs.ctdb.2015.11.028
10.1111/bph.12364
10.1101/gad.298331.117
10.1107/S0907444909052925
10.1038/srep08361
10.1038/nature19799
10.1107/S0021889807021206
10.1038/celldisc.2016.26
10.1038/nature22800
10.1002/jcc.20084
10.1107/S0907444909047337
10.1038/nature22363
10.1073/pnas.1618293114
10.1093/emboj/19.18.4944
10.1073/pnas.1120068109
10.1107/S0907444911056058
10.1038/nmeth.4067
10.1126/science.1249489
10.1107/S0907444910007493
10.1021/acs.jctc.5b00935
10.1016/j.cell.2018.04.029
10.1038/ncomms16050
10.1016/j.str.2017.04.008
10.1098/rsif.2009.0142.focus
10.1016/j.softx.2015.06.001
10.1016/0263-7855(96)00018-5
10.1016/j.cell.2012.10.042
10.1016/j.cell.2012.05.012
10.1124/pr.110.002931
10.5334/1750-2187-10-6
10.1021/jp973084f
10.1038/ncomms15383
10.1016/j.cellsig.2017.06.018
10.1074/jbc.M117.789669
10.1038/nature20605
10.1038/nature10361
10.1038/nature22306
10.1016/j.cell.2017.05.016
10.1021/ci100350u
10.1002/humu.21250
10.1093/nar/gkr703
10.1093/nar/gkw408
10.1038/nature18934
10.3928/01913913-20151215-01
10.7554/eLife.06554
ContentType Journal Article
Copyright Springer Nature Limited 2018
COPYRIGHT 2018 Nature Publishing Group
Copyright Nature Publishing Group Aug 30, 2018
Copyright_xml – notice: Springer Nature Limited 2018
– notice: COPYRIGHT 2018 Nature Publishing Group
– notice: Copyright Nature Publishing Group Aug 30, 2018
DBID CGR
CUY
CVF
ECM
EIF
NPM
AAYXX
CITATION
3V.
7QG
7QL
7QP
7QR
7RV
7SN
7SS
7ST
7T5
7TG
7TK
7TM
7TO
7U9
7X2
7X7
7XB
88A
88E
88G
88I
8AF
8AO
8C1
8FD
8FE
8FG
8FH
8FI
8FJ
8FK
8G5
ABJCF
ABUWG
AFKRA
ARAPS
ATCPS
AZQEC
BBNVY
BEC
BENPR
BGLVJ
BHPHI
BKSAR
C1K
CCPQU
D1I
DWQXO
FR3
FYUFA
GHDGH
GNUQQ
GUQSH
H94
HCIFZ
K9.
KB.
KB0
KL.
L6V
LK8
M0K
M0S
M1P
M2M
M2O
M2P
M7N
M7P
M7S
MBDVC
NAPCQ
P5Z
P62
P64
PATMY
PCBAR
PDBOC
PQEST
PQQKQ
PQUKI
PSYQQ
PTHSS
PYCSY
Q9U
R05
RC3
S0X
SOI
7X8
DOI 10.1038/s41586-018-0447-x
DatabaseName Medline
MEDLINE
MEDLINE (Ovid)
MEDLINE
MEDLINE
PubMed
CrossRef
ProQuest Central (Corporate)
Animal Behavior Abstracts
Bacteriology Abstracts (Microbiology B)
Calcium & Calcified Tissue Abstracts
Chemoreception Abstracts
Proquest Nursing & Allied Health Source
Ecology Abstracts
Entomology Abstracts (Full archive)
Environment Abstracts
Immunology Abstracts
Meteorological & Geoastrophysical Abstracts
Neurosciences Abstracts
Nucleic Acids Abstracts
Oncogenes and Growth Factors Abstracts
Virology and AIDS Abstracts
Agricultural Science Collection
ProQuest Health & Medical Collection
ProQuest Central (purchase pre-March 2016)
Biology Database (Alumni Edition)
Medical Database (Alumni Edition)
Psychology Database (Alumni)
Science Database (Alumni Edition)
STEM Database
ProQuest Pharma Collection
ProQuest Public Health Database
Technology Research Database
ProQuest SciTech Collection
ProQuest Technology Collection
ProQuest Natural Science Collection
Hospital Premium Collection
Hospital Premium Collection (Alumni Edition)
ProQuest Central (Alumni) (purchase pre-March 2016)
Research Library (Alumni Edition)
Materials Science & Engineering Collection
ProQuest Central (Alumni)
ProQuest Central UK/Ireland
Advanced Technologies & Aerospace Database‎ (1962 - current)
Agricultural & Environmental Science Collection
ProQuest Central Essentials
Biological Science Collection
eLibrary
AUTh Library subscriptions: ProQuest Central
Technology Collection
Natural Science Collection
Earth, Atmospheric & Aquatic Science Collection
Environmental Sciences and Pollution Management
ProQuest One Community College
ProQuest Materials Science Collection
ProQuest Central
Engineering Research Database
Health Research Premium Collection
Health Research Premium Collection (Alumni)
ProQuest Central Student
Research Library Prep
AIDS and Cancer Research Abstracts
SciTech Premium Collection
ProQuest Health & Medical Complete (Alumni)
Materials Science Database
Nursing & Allied Health Database (Alumni Edition)
Meteorological & Geoastrophysical Abstracts - Academic
ProQuest Engineering Collection
Biological Sciences
Agricultural Science Database
Health & Medical Collection (Alumni Edition)
Medical Database
Psychology Database
Research Library (ProQuest)
ProQuest Science Journals
Algology Mycology and Protozoology Abstracts (Microbiology C)
Biological Science Database
Engineering Database
Research Library (Corporate)
Nursing & Allied Health Premium
Advanced Technologies & Aerospace Database
ProQuest Advanced Technologies & Aerospace Collection
Biotechnology and BioEngineering Abstracts
Environmental Science Database
Earth, Atmospheric & Aquatic Science Database
Materials Science Collection
ProQuest One Academic Eastern Edition (DO NOT USE)
ProQuest One Academic
ProQuest One Academic UKI Edition
ProQuest One Psychology
Engineering Collection
Environmental Science Collection
ProQuest Central Basic
University of Michigan
Genetics Abstracts
SIRS Editorial
Environment Abstracts
MEDLINE - Academic
DatabaseTitle MEDLINE
Medline Complete
MEDLINE with Full Text
PubMed
MEDLINE (Ovid)
CrossRef
Agricultural Science Database
ProQuest One Psychology
Research Library Prep
ProQuest Central Student
Oncogenes and Growth Factors Abstracts
ProQuest Advanced Technologies & Aerospace Collection
ProQuest Central Essentials
Nucleic Acids Abstracts
elibrary
ProQuest AP Science
SciTech Premium Collection
Environmental Sciences and Pollution Management
Health Research Premium Collection
Meteorological & Geoastrophysical Abstracts
Natural Science Collection
Biological Science Collection
Chemoreception Abstracts
ProQuest Medical Library (Alumni)
Engineering Collection
Advanced Technologies & Aerospace Collection
Engineering Database
Virology and AIDS Abstracts
ProQuest Science Journals (Alumni Edition)
ProQuest Biological Science Collection
ProQuest One Academic Eastern Edition
Earth, Atmospheric & Aquatic Science Database
Agricultural Science Collection
ProQuest Hospital Collection
ProQuest Technology Collection
Health Research Premium Collection (Alumni)
Biological Science Database
Ecology Abstracts
Neurosciences Abstracts
ProQuest Hospital Collection (Alumni)
Biotechnology and BioEngineering Abstracts
Environmental Science Collection
Entomology Abstracts
Nursing & Allied Health Premium
ProQuest Health & Medical Complete
ProQuest One Academic UKI Edition
Environmental Science Database
ProQuest Nursing & Allied Health Source (Alumni)
Engineering Research Database
ProQuest One Academic
Calcium & Calcified Tissue Abstracts
Meteorological & Geoastrophysical Abstracts - Academic
University of Michigan
Technology Collection
Technology Research Database
SIRS Editorial
Materials Science Collection
ProQuest Health & Medical Complete (Alumni)
ProQuest Central (Alumni Edition)
ProQuest One Community College
Research Library (Alumni Edition)
ProQuest Natural Science Collection
ProQuest Pharma Collection
ProQuest Biology Journals (Alumni Edition)
ProQuest Central
Earth, Atmospheric & Aquatic Science Collection
Genetics Abstracts
ProQuest Engineering Collection
Health and Medicine Complete (Alumni Edition)
ProQuest Central Korea
Bacteriology Abstracts (Microbiology B)
Algology Mycology and Protozoology Abstracts (Microbiology C)
Agricultural & Environmental Science Collection
AIDS and Cancer Research Abstracts
Materials Science Database
ProQuest Research Library
ProQuest Materials Science Collection
ProQuest Public Health
ProQuest Central Basic
ProQuest Science Journals
ProQuest Nursing & Allied Health Source
ProQuest Psychology Journals (Alumni)
ProQuest SciTech Collection
Advanced Technologies & Aerospace Database
ProQuest Medical Library
ProQuest Psychology Journals
Animal Behavior Abstracts
Materials Science & Engineering Collection
Immunology Abstracts
Environment Abstracts
ProQuest Central (Alumni)
MEDLINE - Academic
DatabaseTitleList

MEDLINE - Academic



Agricultural Science Database

MEDLINE
Database_xml – sequence: 1
  dbid: NPM
  name: PubMed
  url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed
  sourceTypes: Index Database
– sequence: 2
  dbid: EIF
  name: MEDLINE
  url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search
  sourceTypes: Index Database
– sequence: 3
  dbid: 8FG
  name: ProQuest Technology Collection
  url: https://search.proquest.com/technologycollection1
  sourceTypes: Aggregation Database
DeliveryMethod fulltext_linktorsrc
Discipline Sciences (General)
Physics
EISSN 1476-4687
EndPage 670
ExternalDocumentID A572834407
10_1038_s41586_018_0447_x
30135577
Genre Research Support, Non-U.S. Gov't
Journal Article
GroupedDBID ---
--Z
-DZ
-ET
-~X
.55
.CO
.XZ
07C
0R~
0WA
123
186
1OL
1VR
29M
2KS
2XV
39C
41X
53G
5RE
6TJ
70F
7RV
7X2
7X7
7XC
85S
88A
88E
88I
8AF
8AO
8C1
8CJ
8FE
8FG
8FH
8FI
8FJ
8G5
8R4
8R5
8WZ
97F
97L
A6W
A7Z
AAEEF
AAHBH
AAHTB
AAIKC
AAKAB
AAMNW
AASDW
AAYEP
AAZLF
ABFSI
ABIVO
ABJCF
ABJNI
ABLJU
ABOCM
ABPEJ
ABPPZ
ABUWG
ABVXF
ABWJO
ABZEH
ACBEA
ACBWK
ACGFO
ACGFS
ACGOD
ACIWK
ACKOT
ACMJI
ACNCT
ACPRK
ACWUS
ADBBV
ADFRT
ADUKH
AENEX
AFFNX
AFKRA
AFLOW
AFRAH
AFRQD
AFSHS
AGAYW
AGEZK
AGHSJ
AGHTU
AGNAY
AGSOS
AHMBA
AHSBF
AIDAL
AIDUJ
ALFFA
ALIPV
ALMA_UNASSIGNED_HOLDINGS
AMTXH
ARAPS
ARMCB
ASPBG
ATCPS
ATWCN
AVWKF
AXYYD
AZFZN
AZQEC
B-7
BBNVY
BCU
BEC
BENPR
BGLVJ
BHPHI
BIN
BKEYQ
BKKNO
BKSAR
BPHCQ
BVXVI
CCPQU
CJ0
CS3
D1I
D1J
D1K
DU5
DWQXO
E.-
E.L
EAP
EBS
EE.
EJD
EMH
EPS
ESX
EX3
EXGXG
F20
F5P
FEDTE
FQGFK
FSGXE
FYUFA
GNUQQ
GUQSH
HCIFZ
HG6
HMCUK
HVGLF
HZ~
I-F
IAO
ICQ
IEA
IEP
IGS
IH2
IHR
INH
INR
IOF
IPY
ISR
ITC
K6-
KB.
KOO
L6V
L7B
LK5
LK8
LSO
M0K
M0L
M1P
M2M
M2O
M2P
M7P
M7R
M7S
N9A
NAPCQ
NEJ
NEPJS
O9-
OBC
OES
OHH
OMK
OVD
P2P
P62
PATMY
PCBAR
PDBOC
PQQKQ
PROAC
PSQYO
PSYQQ
PTHSS
PYCSY
Q2X
R05
RND
RNS
RNT
RNTTT
RXW
S0X
SC5
SHXYY
SIXXV
SJFOW
SJN
SNYQT
SV3
TAE
TAOOD
TBHMF
TDRGL
TEORI
TN5
TSG
TWZ
U5U
UIG
UKHRP
UKR
UMD
UQL
VQA
VVN
WH7
WOW
X7M
XIH
XKW
XZL
Y6R
YAE
YCJ
YFH
YNT
YOC
YQT
YR2
YXB
YZZ
ZCA
ZE2
~02
~7V
~88
~KM
.-4
.GJ
.HR
00M
08P
0B8
1CY
1VW
354
3EH
3O-
3V.
4.4
41~
42X
4R4
663
79B
9M8
A8Z
AAJYS
AAKAS
AAVBQ
AAYOK
AAYZH
ABAWZ
ABDBF
ABEFU
ABTAH
ACBNA
ACBTR
ACTDY
ADRHT
ADYSU
ADZCM
AFBBN
AFFDN
AFHKK
AGCDD
AIYXT
AJUXI
APEBS
ARTTT
B0M
BCR
BDKGC
BES
BKOMP
BLC
CGR
CUY
CVF
DB5
DO4
EAD
EAS
EAZ
EBC
EBD
EBO
ECC
ECM
EIF
EMB
EMF
EMK
EMOBN
EPL
ESE
ESN
ESTFP
FA8
FAC
G8K
J5H
L-9
LGEZI
LOTEE
MVM
N4W
NADUK
NPM
NXXTH
ODYON
OHT
P-O
PEA
PM3
PV9
QS-
R4F
RHI
SKT
TH9
TUD
TUS
UAO
UBY
UHB
USG
VOH
X7L
XOL
YJ6
YQI
YQJ
YV5
YXA
YYP
YYQ
ZCG
ZGI
ZHY
ZKB
ZKG
ZY4
~8M
~G0
AAYXX
CITATION
AADEA
AAEXX
ABEEJ
ADFPY
ADZGE
AADWK
AAJMP
AAYJO
ABGIJ
ACBMV
ACBRV
ACBYP
ACIGE
ACTTH
ACVWB
ADMDM
ADQMX
AEDAW
AEFTE
AFNRJ
AGGBP
AGPPL
AHGBK
AJDOV
AMRJV
I-U
U1R
XFK
ZA5
AAPBV
ABGFU
ABPTK
7QG
7QL
7QP
7QR
7SN
7SS
7ST
7T5
7TG
7TK
7TM
7TO
7U9
7XB
8FD
8FK
C1K
FR3
H94
K9.
KL.
M7N
MBDVC
P64
PQEST
PQUKI
Q9U
RC3
SOI
7X8
ID FETCH-LOGICAL-c604t-4faba5fe0d72d939e2086dff1d198c9c9a3dea306c188387f03df545d3c9cd063
IEDL.DBID 8C1
ISSN 0028-0836
IngestDate Fri Aug 16 01:00:37 EDT 2024
Thu Oct 10 21:00:56 EDT 2024
Thu Feb 22 23:54:46 EST 2024
Fri Feb 02 05:17:04 EST 2024
Tue Dec 12 21:19:46 EST 2023
Fri Feb 02 04:23:22 EST 2024
Thu Aug 01 20:36:06 EDT 2024
Thu Sep 12 16:52:24 EDT 2024
Wed Oct 16 00:47:28 EDT 2024
Fri Oct 11 20:35:27 EDT 2024
IsPeerReviewed true
IsScholarly true
Issue 7720
Language English
LinkModel DirectLink
MergedId FETCHMERGED-LOGICAL-c604t-4faba5fe0d72d939e2086dff1d198c9c9a3dea306c188387f03df545d3c9cd063
Notes ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
PMID 30135577
PQID 2112152445
PQPubID 40569
PageCount 5
ParticipantIDs proquest_miscellaneous_2092533273
proquest_journals_2112152445
gale_infotracmisc_A572834407
gale_infotracgeneralonefile_A572834407
gale_infotraccpiq_572834407
gale_infotracacademiconefile_A572834407
gale_incontextgauss_ISR_A572834407
crossref_primary_10_1038_s41586_018_0447_x
pubmed_primary_30135577
springer_journals_10_1038_s41586_018_0447_x
PublicationCentury 2000
PublicationDate 2018-08-00
PublicationDateYYYYMMDD 2018-08-01
PublicationDate_xml – month: 08
  year: 2018
  text: 2018-08-00
PublicationDecade 2010
PublicationPlace London
PublicationPlace_xml – name: London
– name: England
PublicationSubtitle International weekly journal of science
PublicationTitle Nature (London)
PublicationTitleAbbrev Nature
PublicationTitleAlternate Nature
PublicationYear 2018
Publisher Nature Publishing Group UK
Nature Publishing Group
Publisher_xml – name: Nature Publishing Group UK
– name: Nature Publishing Group
References Yan (CR52) 2017; 292
Chen (CR53) 2015; 5
Lee (CR45) 2016; 12
Janda, Waghray, Levin, Thomas, Garcia (CR10) 2012; 337
Cherezov (CR31) 2009; 6
Smart (CR35) 2012; 68
Zheng (CR27) 2016; 540
Pettersen (CR42) 2004; 25
Clevers, Nusse (CR2) 2012; 149
Dijksterhuis, Petersen, Schulte (CR3) 2014; 171
McCoy (CR33) 2007; 40
Pau, Gao, Malbon, Wang, Bertalovitz (CR37) 2015; 10
Umbhauer (CR15) 2000; 19
Humphrey, Dalke, Schulten (CR50) 1996; 14
Nikopoulos (CR22) 2010; 31
McGibbon (CR49) 2015; 109
Xu (CR51) 2016; 2
Wang (CR17) 2013; 497
Wang (CR20) 2012; 151
MacKerell (CR44) 1998; 102
Zhang (CR18) 2017; 8
Zhang (CR24) 2017; 546
Yuan, Pei, Lai (CR39) 2011; 51
Popov (CR29) 2018; 7
Nusse, Clevers (CR1) 2017; 169
Strakova (CR23) 2017; 38
Kabsch (CR32) 2010; 66
Ashkenazy (CR41) 2016; 44
Adams (CR34) 2010; 66
Ma (CR30) 2017; 25
CR11
Abraham (CR43) 2015; 1–2
Rasmussen (CR28) 2011; 477
Emsley, Lohkamp, Scott, Cowtan (CR36) 2010; 66
Janda (CR13) 2017; 545
Byrne (CR16) 2016; 535
Wu (CR26) 2014; 344
Huang (CR47) 2017; 14
Wang, Chang, Rattner, Nathans (CR5) 2016; 117
Nile, Mukund, Stanger, Wang, Hannoush (CR8) 2017; 114
Schulte (CR4) 2010; 62
Tao (CR7) 2016; 538
Jazayeri (CR25) 2017; 546
Zhang (CR21) 2017; 8
Lomize, Pogozheva, Joo, Mosberg, Lomize (CR46) 2012; 40
Huang (CR19) 2018; 174
Kahn (CR6) 2014; 13
DeBruine (CR9) 2017; 31
Gurney (CR14) 2012; 109
Eswar (CR48) 2006; 15
Shen (CR12) 2015; 25
Lomize, Lomize, Pogozheva, Mosberg (CR40) 2006; 22
Kramer, Say, Shields (CR38) 2016; 53
P Huang (447_CR19) 2018; 174
G Schulte (447_CR4) 2010; 62
A Gurney (447_CR14) 2012; 109
CY Janda (447_CR10) 2012; 337
H Ashkenazy (447_CR41) 2016; 44
H Wu (447_CR26) 2014; 344
H Clevers (447_CR2) 2012; 149
C Zhang (447_CR21) 2017; 8
Y Ma (447_CR30) 2017; 25
PD Adams (447_CR34) 2010; 66
ZJ DeBruine (447_CR9) 2017; 31
MJ Abraham (447_CR43) 2015; 1–2
EFX Byrne (447_CR16) 2016; 535
MA Lomize (447_CR46) 2012; 40
A Jazayeri (447_CR25) 2017; 546
W Kabsch (447_CR32) 2010; 66
TH Xu (447_CR51) 2016; 2
J Lee (447_CR45) 2016; 12
GD Kramer (447_CR38) 2016; 53
W Humphrey (447_CR50) 1996; 14
AJ McCoy (447_CR33) 2007; 40
RT McGibbon (447_CR49) 2015; 109
C Wang (447_CR17) 2013; 497
Y Wang (447_CR20) 2012; 151
V Cherezov (447_CR31) 2009; 6
MS Pau (447_CR37) 2015; 10
K Strakova (447_CR23) 2017; 38
P Emsley (447_CR36) 2010; 66
P Popov (447_CR29) 2018; 7
Y Yan (447_CR52) 2017; 292
G Shen (447_CR12) 2015; 25
CY Janda (447_CR13) 2017; 545
Y Wang (447_CR5) 2016; 117
N Eswar (447_CR48) 2006; 15
H Zhang (447_CR24) 2017; 546
SG Rasmussen (447_CR28) 2011; 477
OS Smart (447_CR35) 2012; 68
X Chen (447_CR53) 2015; 5
AH Nile (447_CR8) 2017; 114
Y Zheng (447_CR27) 2016; 540
AD MacKerell (447_CR44) 1998; 102
447_CR11
X Zhang (447_CR18) 2017; 8
Y Yuan (447_CR39) 2011; 51
M Kahn (447_CR6) 2014; 13
MA Lomize (447_CR40) 2006; 22
M Umbhauer (447_CR15) 2000; 19
R Nusse (447_CR1) 2017; 169
K Nikopoulos (447_CR22) 2010; 31
L Tao (447_CR7) 2016; 538
EF Pettersen (447_CR42) 2004; 25
JP Dijksterhuis (447_CR3) 2014; 171
J Huang (447_CR47) 2017; 14
References_xml – volume: 497
  start-page: 338
  year: 2013
  end-page: 343
  ident: CR17
  article-title: Structure of the human smoothened receptor bound to an antitumour agent
  publication-title: Nature
  doi: 10.1038/nature12167
  contributor:
    fullname: Wang
– volume: 7
  year: 2018
  ident: CR29
  article-title: Computational design of thermostabilizing point mutations for G protein-coupled receptors
  publication-title: eLife
  doi: 10.7554/eLife.34729
  contributor:
    fullname: Popov
– volume: 22
  start-page: 623
  year: 2006
  end-page: 625
  ident: CR40
  article-title: OPM: Orientations of Proteins in Membranes database
  publication-title: Bioinformatics
  doi: 10.1093/bioinformatics/btk023
  contributor:
    fullname: Mosberg
– volume: 337
  start-page: 59
  year: 2012
  end-page: 64
  ident: CR10
  article-title: Structural basis of Wnt recognition by Frizzled
  publication-title: Science
  doi: 10.1126/science.1222879
  contributor:
    fullname: Garcia
– volume: 15
  start-page: 5.6.1
  year: 2006
  end-page: 5.6.30
  ident: CR48
  article-title: Comparative protein structure modeling using Modeller
  publication-title: Curr. Protoc. Bioinformatics
  doi: 10.1002/0471250953.bi0506s15
  contributor:
    fullname: Eswar
– volume: 13
  start-page: 513
  year: 2014
  end-page: 532
  ident: CR6
  article-title: Can we safely target the WNT pathway?
  publication-title: Nat. Rev. Drug Discov.
  doi: 10.1038/nrd4233
  contributor:
    fullname: Kahn
– volume: 109
  start-page: 1528
  year: 2015
  end-page: 1532
  ident: CR49
  article-title: MDTraj: a modern open library for the analysis of molecular dynamics trajectories
  publication-title: Biophys. J.
  doi: 10.1016/j.bpj.2015.08.015
  contributor:
    fullname: McGibbon
– volume: 25
  start-page: 1078
  year: 2015
  end-page: 1081
  ident: CR12
  article-title: Structural basis of the Norrin–Frizzled 4 interaction
  publication-title: Cell Res.
  doi: 10.1038/cr.2015.92
  contributor:
    fullname: Shen
– volume: 117
  start-page: 113
  year: 2016
  end-page: 139
  ident: CR5
  article-title: Frizzled receptors in development and disease
  publication-title: Curr. Top. Dev. Biol.
  doi: 10.1016/bs.ctdb.2015.11.028
  contributor:
    fullname: Nathans
– volume: 171
  start-page: 1195
  year: 2014
  end-page: 1209
  ident: CR3
  article-title: WNT/Frizzled signalling: receptor-ligand selectivity with focus on FZD-G protein signalling and its physiological relevance: IUPHAR Review 3
  publication-title: Br. J. Pharmacol.
  doi: 10.1111/bph.12364
  contributor:
    fullname: Schulte
– volume: 31
  start-page: 916
  year: 2017
  end-page: 926
  ident: CR9
  article-title: Wnt5a promotes Frizzled-4 signalosome assembly by stabilizing cysteine-rich domain dimerization
  publication-title: Genes Dev.
  doi: 10.1101/gad.298331.117
  contributor:
    fullname: DeBruine
– volume: 66
  start-page: 213
  year: 2010
  end-page: 221
  ident: CR34
  article-title: PHENIX: a comprehensive Python-based system for macromolecular structure solution
  publication-title: Acta Crystallogr. D
  doi: 10.1107/S0907444909052925
  contributor:
    fullname: Adams
– volume: 53
  start-page: e1
  year: 2016
  end-page: e5
  ident: CR38
  article-title: Simultaneous novel mutations of LRP5 and TSPAN12 in a case of familial exudative vitreoretinopathy
  publication-title: J. Pediatr. Ophthalmol. Strabismus
  contributor:
    fullname: Shields
– volume: 5
  year: 2015
  ident: CR53
  article-title: A ligand-observed mass spectrometry approach integrated into the fragment based lead discovery pipeline
  publication-title: Sci. Rep.
  doi: 10.1038/srep08361
  contributor:
    fullname: Chen
– volume: 538
  start-page: 350
  year: 2016
  end-page: 355
  ident: CR7
  article-title: Frizzled proteins are colonic epithelial receptors for toxin B
  publication-title: Nature
  doi: 10.1038/nature19799
  contributor:
    fullname: Tao
– volume: 40
  start-page: 658
  year: 2007
  end-page: 674
  ident: CR33
  article-title: crystallographic software
  publication-title: J. Appl. Crystallogr.
  doi: 10.1107/S0021889807021206
  contributor:
    fullname: McCoy
– volume: 2
  start-page: 16026
  year: 2016
  ident: CR51
  article-title: Alzheimer’s disease-associated mutations increase amyloid precursor protein resistance to γ-secretase cleavage and the Aβ42/Aβ40 ratio
  publication-title: Cell Discov.
  doi: 10.1038/celldisc.2016.26
  contributor:
    fullname: Xu
– ident: CR11
– volume: 546
  start-page: 254
  year: 2017
  end-page: 258
  ident: CR25
  article-title: Crystal structure of the GLP-1 receptor bound to a peptide agonist
  publication-title: Nature
  doi: 10.1038/nature22800
  contributor:
    fullname: Jazayeri
– volume: 25
  start-page: 1605
  year: 2004
  end-page: 1612
  ident: CR42
  article-title: UCSF Chimera—a visualization system for exploratory research and analysis
  publication-title: J. Comput. Chem.
  doi: 10.1002/jcc.20084
  contributor:
    fullname: Pettersen
– volume: 66
  start-page: 125
  year: 2010
  end-page: 132
  ident: CR32
  article-title: Xds
  publication-title: Acta Crystallogr. D
  doi: 10.1107/S0907444909047337
  contributor:
    fullname: Kabsch
– volume: 546
  start-page: 259
  year: 2017
  end-page: 264
  ident: CR24
  article-title: Structure of the full-length glucagon class B G-protein-coupled receptor
  publication-title: Nature
  doi: 10.1038/nature22363
  contributor:
    fullname: Zhang
– volume: 114
  start-page: 4147
  year: 2017
  end-page: 4152
  ident: CR8
  article-title: Unsaturated fatty acyl recognition by Frizzled receptors mediates dimerization upon Wnt ligand binding
  publication-title: Proc. Natl Acad. Sci. USA
  doi: 10.1073/pnas.1618293114
  contributor:
    fullname: Hannoush
– volume: 19
  start-page: 4944
  year: 2000
  end-page: 4954
  ident: CR15
  article-title: The C-terminal cytoplasmic Lys-Thr-X-X-X-Trp motif in Frizzled receptors mediates Wnt/β-catenin signalling
  publication-title: EMBO J.
  doi: 10.1093/emboj/19.18.4944
  contributor:
    fullname: Umbhauer
– volume: 109
  start-page: 11717
  year: 2012
  end-page: 11722
  ident: CR14
  article-title: Wnt pathway inhibition via the targeting of Frizzled receptors results in decreased growth and tumorigenicity of human tumors
  publication-title: Proc. Natl Acad. Sci. USA
  doi: 10.1073/pnas.1120068109
  contributor:
    fullname: Gurney
– volume: 68
  start-page: 368
  year: 2012
  end-page: 380
  ident: CR35
  article-title: Exploiting structure similarity in refinement: automated NCS and target-structure restraints in BUSTER
  publication-title: Acta Crystallogr. D
  doi: 10.1107/S0907444911056058
  contributor:
    fullname: Smart
– volume: 14
  start-page: 71
  year: 2017
  end-page: 73
  ident: CR47
  article-title: CHARMM36m: an improved force field for folded and intrinsically disordered proteins
  publication-title: Nat. Methods
  doi: 10.1038/nmeth.4067
  contributor:
    fullname: Huang
– volume: 344
  start-page: 58
  year: 2014
  end-page: 64
  ident: CR26
  article-title: Structure of a class C GPCR metabotropic glutamate receptor 1 bound to an allosteric modulator
  publication-title: Science
  doi: 10.1126/science.1249489
  contributor:
    fullname: Wu
– volume: 66
  start-page: 486
  year: 2010
  end-page: 501
  ident: CR36
  article-title: Features and development of Coot
  publication-title: Acta Crystallogr. D
  doi: 10.1107/S0907444910007493
  contributor:
    fullname: Cowtan
– volume: 12
  start-page: 405
  year: 2016
  end-page: 413
  ident: CR45
  article-title: CHARMM-GUI input generator for NAMD, GROMACS, AMBER, OpenMM, and CHARMM/OpenMM simulations using the CHARMM36 additive force field
  publication-title: J. Chem. Theory Comput.
  doi: 10.1021/acs.jctc.5b00935
  contributor:
    fullname: Lee
– volume: 174
  start-page: 312
  year: 2018
  end-page: 324.e16
  ident: CR19
  article-title: Structural basis of Smoothened activation in Hedgehog signaling
  publication-title: Cell
  doi: 10.1016/j.cell.2018.04.029
  contributor:
    fullname: Huang
– volume: 8
  year: 2017
  ident: CR21
  article-title: Norrin-induced Frizzled4 endocytosis and endo-lysosomal trafficking control retinal angiogenesis and barrier function
  publication-title: Nat. Commun.
  doi: 10.1038/ncomms16050
  contributor:
    fullname: Zhang
– volume: 25
  start-page: 858
  year: 2017
  end-page: 866.e4
  ident: CR30
  article-title: Structural basis for apelin control of the human apelin receptor
  publication-title: Structure
  doi: 10.1016/j.str.2017.04.008
  contributor:
    fullname: Ma
– volume: 6
  start-page: S587
  year: 2009
  end-page: S597
  ident: CR31
  article-title: Rastering strategy for screening and centring of microcrystal samples of human membrane proteins with a sub-µm size X-ray synchrotron beam
  publication-title: J. R. Soc. Interface
  doi: 10.1098/rsif.2009.0142.focus
  contributor:
    fullname: Cherezov
– volume: 1–2
  start-page: 19
  year: 2015
  end-page: 25
  ident: CR43
  article-title: GROMACS: High performance molecular simulations through multi-level parallelism from laptops to supercomputers
  publication-title: SoftwareX
  doi: 10.1016/j.softx.2015.06.001
  contributor:
    fullname: Abraham
– volume: 14
  start-page: 33
  year: 1996
  end-page: 38
  ident: CR50
  article-title: VMD: Visual molecular dynamics
  publication-title: J. Mol. Graphics
  doi: 10.1016/0263-7855(96)00018-5
  contributor:
    fullname: Schulten
– volume: 151
  start-page: 1332
  year: 2012
  end-page: 1344
  ident: CR20
  article-title: Norrin/Frizzled4 signaling in retinal vascular development and blood brain barrier plasticity
  publication-title: Cell
  doi: 10.1016/j.cell.2012.10.042
  contributor:
    fullname: Wang
– volume: 149
  start-page: 1192
  year: 2012
  end-page: 1205
  ident: CR2
  article-title: Wnt/β-catenin signaling and disease
  publication-title: Cell
  doi: 10.1016/j.cell.2012.05.012
  contributor:
    fullname: Nusse
– volume: 62
  start-page: 632
  year: 2010
  end-page: 667
  ident: CR4
  article-title: International union of basic and clinical pharmacology. LXXX. The class Frizzled receptors
  publication-title: Pharmacol. Rev.
  doi: 10.1124/pr.110.002931
  contributor:
    fullname: Schulte
– volume: 10
  year: 2015
  ident: CR37
  article-title: The intracellular loop 2 F328S Frizzled-4 mutation implicated in familial exudative vitreoretinopathy impairs Dishevelled recruitment
  publication-title: J. Mol. Signal.
  doi: 10.5334/1750-2187-10-6
  contributor:
    fullname: Bertalovitz
– volume: 102
  start-page: 3586
  year: 1998
  end-page: 3616
  ident: CR44
  article-title: All-atom empirical potential for molecular modeling and dynamics studies of proteins
  publication-title: J. Phys. Chem. B
  doi: 10.1021/jp973084f
  contributor:
    fullname: MacKerell
– volume: 8
  year: 2017
  ident: CR18
  article-title: Crystal structure of a multi-domain human smoothened receptor in complex with a super stabilizing ligand
  publication-title: Nat. Commun.
  doi: 10.1038/ncomms15383
  contributor:
    fullname: Zhang
– volume: 38
  start-page: 85
  year: 2017
  end-page: 96
  ident: CR23
  article-title: The tyrosine Y250 in Frizzled 4 defines a conserved motif important for structural integrity of the receptor and recruitment of Disheveled
  publication-title: Cell. Signal.
  doi: 10.1016/j.cellsig.2017.06.018
  contributor:
    fullname: Strakova
– volume: 292
  start-page: 15826
  year: 2017
  end-page: 15837
  ident: CR52
  article-title: Dimerization of the transmembrane domain of amyloid precursor protein is determined by residues around the γ-secretase cleavage sites
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M117.789669
  contributor:
    fullname: Yan
– volume: 540
  start-page: 458
  year: 2016
  end-page: 461
  ident: CR27
  article-title: Structure of CC chemokine receptor 2 with orthosteric and allosteric antagonists
  publication-title: Nature
  doi: 10.1038/nature20605
  contributor:
    fullname: Zheng
– volume: 477
  start-page: 549
  year: 2011
  end-page: 555
  ident: CR28
  article-title: Crystal structure of the β adrenergic receptor-Gs protein complex
  publication-title: Nature
  doi: 10.1038/nature10361
  contributor:
    fullname: Rasmussen
– volume: 545
  start-page: 234
  year: 2017
  end-page: 237
  ident: CR13
  article-title: Surrogate Wnt agonists that phenocopy canonical Wnt and β-catenin signalling
  publication-title: Nature
  doi: 10.1038/nature22306
  contributor:
    fullname: Janda
– volume: 169
  start-page: 985
  year: 2017
  end-page: 999
  ident: CR1
  article-title: Wnt/β-catenin signaling, disease, and emerging therapeutic modalities
  publication-title: Cell
  doi: 10.1016/j.cell.2017.05.016
  contributor:
    fullname: Clevers
– volume: 51
  start-page: 1083
  year: 2011
  end-page: 1091
  ident: CR39
  article-title: LigBuilder 2: a practical de novo drug design approach
  publication-title: J. Chem. Inf. Model.
  doi: 10.1021/ci100350u
  contributor:
    fullname: Lai
– volume: 31
  start-page: 656
  year: 2010
  end-page: 666
  ident: CR22
  article-title: Overview of the mutation spectrum in familial exudative vitreoretinopathy and Norrie disease with identification of 21 novel variants in , , and
  publication-title: Hum. Mutat.
  doi: 10.1002/humu.21250
  contributor:
    fullname: Nikopoulos
– volume: 40
  start-page: D370
  year: 2012
  end-page: D376
  ident: CR46
  article-title: OPM database and PPM web server: resources for positioning of proteins in membranes
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gkr703
  contributor:
    fullname: Lomize
– volume: 44
  start-page: W344
  year: 2016
  end-page: W350
  ident: CR41
  article-title: ConSurf 2016: an improved methodology to estimate and visualize evolutionary conservation in macromolecules
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gkw408
  contributor:
    fullname: Ashkenazy
– volume: 535
  start-page: 517
  year: 2016
  end-page: 522
  ident: CR16
  article-title: Structural basis of Smoothened regulation by its extracellular domains
  publication-title: Nature
  doi: 10.1038/nature18934
  contributor:
    fullname: Byrne
– volume: 40
  start-page: D370
  year: 2012
  ident: 447_CR46
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gkr703
  contributor:
    fullname: MA Lomize
– volume: 68
  start-page: 368
  year: 2012
  ident: 447_CR35
  publication-title: Acta Crystallogr. D
  doi: 10.1107/S0907444911056058
  contributor:
    fullname: OS Smart
– volume: 8
  year: 2017
  ident: 447_CR21
  publication-title: Nat. Commun.
  doi: 10.1038/ncomms16050
  contributor:
    fullname: C Zhang
– volume: 12
  start-page: 405
  year: 2016
  ident: 447_CR45
  publication-title: J. Chem. Theory Comput.
  doi: 10.1021/acs.jctc.5b00935
  contributor:
    fullname: J Lee
– volume: 114
  start-page: 4147
  year: 2017
  ident: 447_CR8
  publication-title: Proc. Natl Acad. Sci. USA
  doi: 10.1073/pnas.1618293114
  contributor:
    fullname: AH Nile
– volume: 14
  start-page: 71
  year: 2017
  ident: 447_CR47
  publication-title: Nat. Methods
  doi: 10.1038/nmeth.4067
  contributor:
    fullname: J Huang
– volume: 40
  start-page: 658
  year: 2007
  ident: 447_CR33
  publication-title: J. Appl. Crystallogr.
  doi: 10.1107/S0021889807021206
  contributor:
    fullname: AJ McCoy
– volume: 14
  start-page: 33
  year: 1996
  ident: 447_CR50
  publication-title: J. Mol. Graphics
  doi: 10.1016/0263-7855(96)00018-5
  contributor:
    fullname: W Humphrey
– volume: 2
  start-page: 16026
  year: 2016
  ident: 447_CR51
  publication-title: Cell Discov.
  doi: 10.1038/celldisc.2016.26
  contributor:
    fullname: TH Xu
– volume: 546
  start-page: 259
  year: 2017
  ident: 447_CR24
  publication-title: Nature
  doi: 10.1038/nature22363
  contributor:
    fullname: H Zhang
– volume: 25
  start-page: 1605
  year: 2004
  ident: 447_CR42
  publication-title: J. Comput. Chem.
  doi: 10.1002/jcc.20084
  contributor:
    fullname: EF Pettersen
– volume: 31
  start-page: 916
  year: 2017
  ident: 447_CR9
  publication-title: Genes Dev.
  doi: 10.1101/gad.298331.117
  contributor:
    fullname: ZJ DeBruine
– volume: 292
  start-page: 15826
  year: 2017
  ident: 447_CR52
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M117.789669
  contributor:
    fullname: Y Yan
– volume: 53
  start-page: e1
  year: 2016
  ident: 447_CR38
  publication-title: J. Pediatr. Ophthalmol. Strabismus
  doi: 10.3928/01913913-20151215-01
  contributor:
    fullname: GD Kramer
– volume: 117
  start-page: 113
  year: 2016
  ident: 447_CR5
  publication-title: Curr. Top. Dev. Biol.
  doi: 10.1016/bs.ctdb.2015.11.028
  contributor:
    fullname: Y Wang
– volume: 66
  start-page: 125
  year: 2010
  ident: 447_CR32
  publication-title: Acta Crystallogr. D
  doi: 10.1107/S0907444909047337
  contributor:
    fullname: W Kabsch
– volume: 545
  start-page: 234
  year: 2017
  ident: 447_CR13
  publication-title: Nature
  doi: 10.1038/nature22306
  contributor:
    fullname: CY Janda
– volume: 13
  start-page: 513
  year: 2014
  ident: 447_CR6
  publication-title: Nat. Rev. Drug Discov.
  doi: 10.1038/nrd4233
  contributor:
    fullname: M Kahn
– volume: 19
  start-page: 4944
  year: 2000
  ident: 447_CR15
  publication-title: EMBO J.
  doi: 10.1093/emboj/19.18.4944
  contributor:
    fullname: M Umbhauer
– volume: 344
  start-page: 58
  year: 2014
  ident: 447_CR26
  publication-title: Science
  doi: 10.1126/science.1249489
  contributor:
    fullname: H Wu
– volume: 497
  start-page: 338
  year: 2013
  ident: 447_CR17
  publication-title: Nature
  doi: 10.1038/nature12167
  contributor:
    fullname: C Wang
– volume: 7
  year: 2018
  ident: 447_CR29
  publication-title: eLife
  doi: 10.7554/eLife.34729
  contributor:
    fullname: P Popov
– volume: 38
  start-page: 85
  year: 2017
  ident: 447_CR23
  publication-title: Cell. Signal.
  doi: 10.1016/j.cellsig.2017.06.018
  contributor:
    fullname: K Strakova
– volume: 51
  start-page: 1083
  year: 2011
  ident: 447_CR39
  publication-title: J. Chem. Inf. Model.
  doi: 10.1021/ci100350u
  contributor:
    fullname: Y Yuan
– volume: 337
  start-page: 59
  year: 2012
  ident: 447_CR10
  publication-title: Science
  doi: 10.1126/science.1222879
  contributor:
    fullname: CY Janda
– volume: 8
  year: 2017
  ident: 447_CR18
  publication-title: Nat. Commun.
  doi: 10.1038/ncomms15383
  contributor:
    fullname: X Zhang
– volume: 62
  start-page: 632
  year: 2010
  ident: 447_CR4
  publication-title: Pharmacol. Rev.
  doi: 10.1124/pr.110.002931
  contributor:
    fullname: G Schulte
– volume: 169
  start-page: 985
  year: 2017
  ident: 447_CR1
  publication-title: Cell
  doi: 10.1016/j.cell.2017.05.016
  contributor:
    fullname: R Nusse
– volume: 151
  start-page: 1332
  year: 2012
  ident: 447_CR20
  publication-title: Cell
  doi: 10.1016/j.cell.2012.10.042
  contributor:
    fullname: Y Wang
– volume: 10
  year: 2015
  ident: 447_CR37
  publication-title: J. Mol. Signal.
  doi: 10.5334/1750-2187-10-6
  contributor:
    fullname: MS Pau
– volume: 5
  year: 2015
  ident: 447_CR53
  publication-title: Sci. Rep.
  doi: 10.1038/srep08361
  contributor:
    fullname: X Chen
– volume: 6
  start-page: S587
  year: 2009
  ident: 447_CR31
  publication-title: J. R. Soc. Interface
  doi: 10.1098/rsif.2009.0142.focus
  contributor:
    fullname: V Cherezov
– volume: 535
  start-page: 517
  year: 2016
  ident: 447_CR16
  publication-title: Nature
  doi: 10.1038/nature18934
  contributor:
    fullname: EFX Byrne
– ident: 447_CR11
  doi: 10.7554/eLife.06554
– volume: 546
  start-page: 254
  year: 2017
  ident: 447_CR25
  publication-title: Nature
  doi: 10.1038/nature22800
  contributor:
    fullname: A Jazayeri
– volume: 25
  start-page: 858
  year: 2017
  ident: 447_CR30
  publication-title: Structure
  doi: 10.1016/j.str.2017.04.008
  contributor:
    fullname: Y Ma
– volume: 66
  start-page: 213
  year: 2010
  ident: 447_CR34
  publication-title: Acta Crystallogr. D
  doi: 10.1107/S0907444909052925
  contributor:
    fullname: PD Adams
– volume: 109
  start-page: 1528
  year: 2015
  ident: 447_CR49
  publication-title: Biophys. J.
  doi: 10.1016/j.bpj.2015.08.015
  contributor:
    fullname: RT McGibbon
– volume: 149
  start-page: 1192
  year: 2012
  ident: 447_CR2
  publication-title: Cell
  doi: 10.1016/j.cell.2012.05.012
  contributor:
    fullname: H Clevers
– volume: 109
  start-page: 11717
  year: 2012
  ident: 447_CR14
  publication-title: Proc. Natl Acad. Sci. USA
  doi: 10.1073/pnas.1120068109
  contributor:
    fullname: A Gurney
– volume: 15
  start-page: 5.6.1
  year: 2006
  ident: 447_CR48
  publication-title: Curr. Protoc. Bioinformatics
  doi: 10.1002/0471250953.bi0506s15
  contributor:
    fullname: N Eswar
– volume: 538
  start-page: 350
  year: 2016
  ident: 447_CR7
  publication-title: Nature
  doi: 10.1038/nature19799
  contributor:
    fullname: L Tao
– volume: 171
  start-page: 1195
  year: 2014
  ident: 447_CR3
  publication-title: Br. J. Pharmacol.
  doi: 10.1111/bph.12364
  contributor:
    fullname: JP Dijksterhuis
– volume: 31
  start-page: 656
  year: 2010
  ident: 447_CR22
  publication-title: Hum. Mutat.
  doi: 10.1002/humu.21250
  contributor:
    fullname: K Nikopoulos
– volume: 25
  start-page: 1078
  year: 2015
  ident: 447_CR12
  publication-title: Cell Res.
  doi: 10.1038/cr.2015.92
  contributor:
    fullname: G Shen
– volume: 540
  start-page: 458
  year: 2016
  ident: 447_CR27
  publication-title: Nature
  doi: 10.1038/nature20605
  contributor:
    fullname: Y Zheng
– volume: 102
  start-page: 3586
  year: 1998
  ident: 447_CR44
  publication-title: J. Phys. Chem. B
  doi: 10.1021/jp973084f
  contributor:
    fullname: AD MacKerell
– volume: 1–2
  start-page: 19
  year: 2015
  ident: 447_CR43
  publication-title: SoftwareX
  doi: 10.1016/j.softx.2015.06.001
  contributor:
    fullname: MJ Abraham
– volume: 66
  start-page: 486
  year: 2010
  ident: 447_CR36
  publication-title: Acta Crystallogr. D
  doi: 10.1107/S0907444910007493
  contributor:
    fullname: P Emsley
– volume: 477
  start-page: 549
  year: 2011
  ident: 447_CR28
  publication-title: Nature
  doi: 10.1038/nature10361
  contributor:
    fullname: SG Rasmussen
– volume: 44
  start-page: W344
  year: 2016
  ident: 447_CR41
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gkw408
  contributor:
    fullname: H Ashkenazy
– volume: 174
  start-page: 312
  year: 2018
  ident: 447_CR19
  publication-title: Cell
  doi: 10.1016/j.cell.2018.04.029
  contributor:
    fullname: P Huang
– volume: 22
  start-page: 623
  year: 2006
  ident: 447_CR40
  publication-title: Bioinformatics
  doi: 10.1093/bioinformatics/btk023
  contributor:
    fullname: MA Lomize
SSID ssj0005174
Score 2.5677643
Snippet Frizzled receptors (FZDs) are class-F G-protein-coupled receptors (GPCRs) that function in Wnt signalling and are essential for developing and adult organisms...
Frizzled receptors (FZDs) are class-F G-protein-coupled receptors (GPCRs) that function in Wnt signalling and are essential for developing and adult...
SourceID proquest
gale
crossref
pubmed
springer
SourceType Aggregation Database
Index Database
Publisher
StartPage 666
SubjectTerms 101/58
119/118
13/109
13/95
631/1647/2258/1266
631/80/86
82/16
82/80
82/83
Activation
Alzheimer's disease
Atomic structure
Binding
Binding Sites
Bioinformatics
Crystal structure
Crystallography, X-Ray
Cysteine - metabolism
Dishevelled Proteins - metabolism
Free form
Frizzled protein
Frizzled Receptors - chemistry
Frizzled Receptors - genetics
G protein-coupled receptors
G proteins
Humanities and Social Sciences
Humans
Letter
Ligands
Models, Molecular
Molecular dynamics
Molecular Dynamics Simulation
multidisciplinary
Mutation
Observations
Physiological aspects
Protein Domains
Proteins
Receptor mechanisms
Receptors
Science
Science (multidisciplinary)
Signal transduction
Signaling
Structural stability
Structure
Wnt protein
Wnt Signaling Pathway
Title Crystal structure of the Frizzled 4 receptor in a ligand-free state
URI https://link.springer.com/article/10.1038/s41586-018-0447-x
https://www.ncbi.nlm.nih.gov/pubmed/30135577
https://www.proquest.com/docview/2112152445
https://search.proquest.com/docview/2092533273
Volume 560
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
link http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwfV3da9swEBdry2AvY-2-vHZBG2NfxdSWZUt-Gl1o1g1WRrdC3oSijxAIdmon0Pav78mW2zhse_HLnYU4351-5zvdIfTOtWgDVSBhxqQJKbE52BzPQqvJhKkJSUyTLvh5lp1e0B_jdOx_uNW-rLLziY2j1qVy_8iPIFBxI1gpTb8sLkM3NcplV_0IjS20E4NiutENfLhW4rHRhbnLaib8qIaDi7tYGiiUsvCqdy5teue142kjX9ocQ6Mn6LHHj_i4_eC76IEp9tDDpo5T1Xto19tqjT_6htKfnqLhsLoGEDjHbbPYVWVwaTEgPzyqZjc3c6MxxeD5zAICcDwrsMTz2VQWOrSVMbi5c_QMXYxO_gxPQz88IVRZRJchtXIiU2sizYjOk9wQCF60tbGOc65ylctEGwkBg4o5TzizUaItwCmdAFEDcHmOtouyMC8RttKomKlYK5JTrXme0dSCpWc6NlaqOECfO9GJRdsjQzS57YSLVs4C5CycnMVVgN464QrXe6JwxS1Tuapr8f33uThOGXFjPyIWoA-eyZbLSirp7wrAfly7qh7nfo9TLWaXYo36vkedtpL_2zIHPUawMdUnd6ogvI3X4l4jA_TmjuzedHVrhSlXwBPlBAA1YMQAvWhV6E5E4FoB7DFY_LDTqfvF_ym_V__fyj56RBqldiWKB2gb9Mq8Bti0nAzQFhuzQWMh7jn6NkA7X0_Ofp3fAmQEEs4
link.rule.ids 315,786,790,12083,12250,12792,21416,27955,27956,31752,31753,33299,33300,33406,33407,33777,33778,43343,43612,43633,43838,74100,74369,74390,74657
linkProvider ProQuest
linkToHtml http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwfV3rb9NADLegE4IviI1X2YADIZ6Kllwur09oVKs62Co0NmnfTtd7VJWqpEtaaeyvx5dc1qUCPts9Rb_avp9jxwZ4Z0e0oSlQL06E9hg1GfpcGntG0UkiJzTUdbngZByPztn3i-jCvXCrXFtlGxPrQK0Kad-R72OiYlewMhZ9XVx6dmuUra66FRp3YcuO3Ex7sPXtcPzzdN3ksTGHua1rhul-hVdXarNplDCWeFedm2kzPt-6oDYqpvVFNHwEDx2DJAfNX74Nd3S-A_fqTk5Z7cC289aKfHQjpT89hsGg_I00cE6acbGrUpPCEOR-ZFjOrq_nWhFGMPbpBabgZJYTQeazqciVZ0qtSf3V0RM4Hx6eDUaeW5_gydhnS48ZMRGR0b5KqMrCTFNMX5QxgQqyVGYyE6HSAlMGGaSIXWL8UBkkVCpEoULq8hR6eZHr50CM0DJIZKAkzZhSaRazyKCvxyrQRsigD59b6PiimZLB6-p2mPIGZ444c4szv-rDWwsut9MnctveMhWrquJHv075QZRQu_jDT_rwwSmZYlkKKdzXAvg8dmBVR3O3oykXs0t-S_q-I502yP_tmL2OInqZ7IpbU-DOyyu-tsk-vLkR21_azrVcFyvU8TOKlBpZYh-eNSZ0AxEGV6R7CR7-pbWp9eH_xO_F_x_lNdwfnZ0c8-Oj8Y9deEBrA7cNi3vQQxvTL5FELSevnKf8ARltE_s
linkToPdf http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwfV1Zb9NAEB5BEYgXRMsVWmBBiFNW7PXaaz-hKhC1HBUCKuVttdkjihTZqZ1Ipb-eWXvd1BHwPOOVNZ7jG8_sDMBLN6INVYEGKZcmYNTmaHNZGlhNp1xNaWyacsG3k_TolH2eJBPf_1T7tsrOJzaOWpfK_SMfYqLiVrAylgytb4v4_nH8YXkWuA1SrtLq12lchxsYJUO3xoFP-KbdY2sic1fhjLNhjUEsc3k1UhjjwXkvRm176iuhaqt22oSk8V2447EkOWw__i5cM8Ue3Gx6OlW9B7vebmvyxg-XfnsPRqPqNwLCBWkHx64rQ0pLEAWScTW_uFgYTRhBL2iWmIyTeUEkWcxnstCBrYwhzf2j-3A6_vRrdBT4RQqBSkO2CpiVU5lYE2pOdR7nhmIio62NdJRnKle5jLWRmDyoKMvijNsw1hahlY6RqBHEPICdoizMIyBWGhVxFWlFc6Z1lqcssWj1qY6MlSoawLtOdGLZzssQTZ07zkQrZ4FyFk7O4nwAL5xwhZtDUbgvOpPruhbHP3-Iw4RTtwIk5AN47Zlsuaqkkv7eAL6PG13V49zvcarl_Excob7qUWet5P92zEGPEe1N9cmdKghv77XYaOcAnl-S3ZOuh60w5Rp5wpwiuEa8OICHrQpdigjdLAI_joe_73Rqc_g_5ff4_6_yDG6hiYivxydf9uE2bfTbdS4ewA6qmHmCaGo1fdqYyR9_4Ba4
openUrl ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Crystal+structure+of+the+Frizzled+4+receptor+in+a+ligand-free+state&rft.jtitle=Nature+%28London%29&rft.au=Yang%2C+Shifan&rft.au=Wu%2C+Yiran&rft.au=Xu%2C+Ting-Hai&rft.au=de+Waal%2C+Parker+W&rft.date=2018-08-01&rft.pub=Nature+Publishing+Group&rft.issn=0028-0836&rft.eissn=1476-4687&rft.volume=560&rft.issue=7720&rft.spage=666&rft_id=info:doi/10.1038%2Fs41586-018-0447-x&rft.externalDBID=ISR&rft.externalDocID=A572834407
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0028-0836&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0028-0836&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0028-0836&client=summon