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Showing 1 - 50 of 222 items for (author: wang & jc)

EMDB-41895:
(N3Occluded Local CORE1 Map) - "Mechanism of dual pharmacological correction and potentiation of human CFTR"

EMDB-41896:
(N3Occluded Local ABC1 Map) - "Mechanism of dual pharmacological correction and potentiation of human CFTR"

EMDB-41898:
(N3Occluded Local ABC2 Map) - "Mechanism of dual pharmacological correction and potentiation of human CFTR"

EMDB-41901:
(N3Occluded Composite Map) - "Mechanism of dual pharmacological correction and potentiation of human CFTR"

EMDB-41902:
(N3Occluded Consensus Map) - "Mechanism of dual pharmacological correction and potentiation of human CFTR"

EMDB-42180:
(V17) - "Mechanism of dual pharmacological correction and potentiation of human CFTR"

EMDB-41717:
(N3Shifted Consensus Map) - "Mechanism of dual pharmacological correction and potentiation of human CFTR"

EMDB-41719:
(N3Shifted Local CORE1 Map) - "Mechanism of dual pharmacological correction and potentiation of human CFTR"

EMDB-41722:
(N3Shifted Local ABC2 Map) - "Mechanism of dual pharmacological correction and potentiation of human CFTR"

EMDB-41723:
(N3Shifted Local CORE2 Map) - "Mechanism of dual pharmacological correction and potentiation of human CFTR"

EMDB-41724:
(N3 Shifted Local ABC2 Map) - "Mechanism of dual pharmacological correction and potentiation of human CFTR"

EMDB-41726:
(N3Shifted Composite Map) - "Mechanism of dual pharmacological correction and potentiation of human CFTR"

EMDB-42177:
(Local CORE2) - "Mechanism of dual pharmacological correction and potentiation of human CFTR"

EMDB-42178:
(Local ABC2) - "Mechanism of dual pharmacological correction and potentiation of human CFTR"

EMDB-42179:
(Composite) - "Mechanism of dual pharmacological correction and potentiation of human CFTR"

EMDB-41900:
(Local CORE2 Map) - "Mechanism of dual pharmacological correction and potentiation of human CFTR"

EMDB-41980:
(Consensus Map) - "Mechanism of dual pharmacological correction and potentiation of human CFTR"

EMDB-41981:
(Local hNBD1 Map) - "Mechanism of dual pharmacological correction and potentiation of human CFTR"

EMDB-37637:
Structural basis for the nucleosome binding and chromatin compaction by the linker histone H5

EMDB-37638:
Structural basis for the nucleosome binding and chromatin compaction by the linker histone H5

EMDB-38407:
Structural basis for the linker histone H5-nucleosome binding and chromatin compaction

EMDB-41849:
Structure of 310-18A5 Fab in complex with A/Solomon Islands/3/2006(H1N1) influenza virus hemagglutinin

EMDB-41854:
Structure of Human Mitochondrial Chaperonin V72I Mutant

EMDB-36914:
Cryo-EM structure of Streptomyces coelicolor transcription initiation complex with the global transcription factor AfsR

EMDB-43011:
Phosphorylated, ATP-bound, E1371Q human cystic fibrosis transmembrane conductance regulator (E1371Q-CFTR)

EMDB-43014:
Phosphorylated, ATP-bound, inhibitor 172-bound E1371Q human cystic fibrosis transmembrane conductance regulator

EMDB-29330:
N332-GT5 SOSIP in complex with base polyclonal Fabs isolated at day 42 from protein immunized wild type mice

EMDB-29333:
N332-GT5 SOSIP in complex with base polyclonal Fabs isolated at day 42 from protein immunized BG18HCgl knock-in mice

EMDB-29334:
N332-GT5 SOSIP in complex with V1V3 polyclonal Fabs isolated at day 16 from mRNA immunized wild type mice

EMDB-29335:
N332-GT5 SOSIP in complex with V1V3 polyclonal Fabs isolated at day 42 from mRNA immunized BG18HCgl knock-in mice

EMDB-43191:
N332-GT5 SOSIP in complex with V1V3 polyclonal Fabs isolated at day 14 from N332-GT2 nanoparticle-immunized BG18HCgl knock-in mice

EMDB-43192:
N332-GT5 SOSIP in complex with V1V3 polyclonal Fabs isolated at day 15 from N332-GT5 nanoparticle-immunized BG18HCgl knock-in mice

EMDB-40825:
10E8-GT10.2 immunogen in complex with human Fab 10E8 and mouse Fab W6-10

EMDB-28937:
N332-GT5 SOSIP in complex with V1V3 polyclonal Fabs isolated at day 42 from protein immunized wild type mice

EMDB-28938:
N332-GT5 SOSIP in complex with V1V3 and base polyclonal Fabs isolated at day 16 from protein immunized BG18HCgl knock-in mice

EMDB-28939:
N332-GT5 SOSIP in complex with V1V3 polyclonal Fabs isolated at day 42 from mRNA immunized wild type mice

EMDB-28940:
N332-GT5 SOSIP in complex with V1V3 polyclonal Fabs isolated at day 16 from mRNA immunized BG18HCgl knock-in mice

EMDB-28941:
HIV Env BG505_MD39_B11 SOSIP boosting trimer in complex with B11_d77.7 mouse Fab and RM20A3 Fab

EMDB-28942:
HIV Env germline targeting BG505_MD64_N332-GT5 SOSIP in complex with V3-glycan polyclonal Fab isolated from immunized BG18HCgl knock-in mice

EMDB-28945:
HIV Env germline targeting BG505_MD64_N332-GT5 SOSIP in complex with V3-glycan polyclonal Fab isolated from immunized wild type mice, and NHP monoclonal Fab RM20A3

EMDB-43190:
HIV Env BG505_MD39_B16 SOSIP boosting trimer in complex with B16_d77.5 mouse Fab and RM20A3 Fab

EMDB-40180:
MsbA bound to cerastecin C

EMDB-29941:
HPV16 E6-E6AP-p53 complex

EMDB-41048:
Lassa GPC Trimer in complex with Fab 8.11G and nanobody D5

EMDB-28728:
Structure of 3A10 Fab in complex with A/Moscow/10/1999 (H3N2) influenza virus neuraminidase

EMDB-28729:
Structure of 1F04 Fab in complex with A/Moscow/10/1999 (H3N2) influenza virus neuraminidase

EMDB-28730:
Structure of 3C08 Fab in complex with A/Moscow/10/1999 (H3N2) influenza virus neuraminidase

EMDB-40571:
Cryo-EM structure of PAPP-A2

EMDB-41302:
Lassa GPC trimer in complex with Fab GP23

EMDB-40048:
Empty HBV Cp183 capsid with importin-beta

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Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

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Oct 5, 2021. Nobel Prize for mechanically activated and temperature-gated ion channels

Nobel Prize for mechanically activated and temperature-gated ion channels

  • The Nobel Prize in Physiology or Medicine 2021 was awarded jointly to David Julius and Ardem Patapoutian "for their discoveries of receptors for temperature and touch."
  • EM Navigator can help to find cryo-EM structure data by both pioneers.

External links:The Nobel Prize in Physiology or Medicine 2021 - NobelPrize.org / Structure data by Ardem Patapoutian / Structure data by David Julius

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