S. Maeda

发表

Structure of the μ Opioid Receptor-Gi Protein Complex

Naomi R. Latorraca, Joseph M. Paggi, R. Dror, 2018, Nature.

Structure of the gap junction channel and its implications for its biological functions

Tomitake Tsukihara, T. Tsukihara, S. Maeda, 2011, Cellular and Molecular Life Sciences.

Cryo-EM structure of the rhodopsin-Gαi-βγ complex reveals binding of the rhodopsin C-terminal tail to the Gβ subunit

H. Stahlberg, T. Flock, R. Dawson, 2019, bioRxiv.

Structures of the M1 and M2 muscarinic acetylcholine receptor/G-protein complexes

M. J. Robertson, G. Skiniotis, B. Kobilka, 2019, Science.

Figures and figure supplements Cryo-EM structure of the rhodopsin-G a i-bg complex reveals binding of the rhodopsin C-terminal tail to the g b subunit

H. Stahlberg, T. Flock, R. Dawson, 2019 .

Roles of Met-34, Cys-64, and Arg-75 in the Assembly of Human Connexin 26

Y. Fujiyoshi, K. Mitsuoka, S. Maeda, 2003, The Journal of Biological Chemistry.

Cryo-EM structure of the rhodopsin-Gαi-βγ complex reveals binding of the rhodopsin C-terminal tail to the gβ subunit

H. Stahlberg, T. Flock, R. Dawson, 2019, bioRxiv.

Structural and functional studies of gap junction channels.

T. Tsukihara, S. Maeda, So Nakagawa, 2010, Current opinion in structural biology.

Structure of the Gap Junction Channel

S. Maeda, 2010 .

Membrane phosphoinositides regulate GPCR-β-arrestin complex assembly and dynamics

B. Kobilka, A. Inoue, M. Zastrow, 2022, Cell.

Structure of the mu-opioid receptor-Giprotein complex.

Naomi R. Latorraca, Joseph M. Paggi, R. Dror, 2018 .

Membrane phosphoinositides regulate GPCR-β-arrestin complex assembly and dynamics

B. Kobilka, A. Inoue, M. Zastrow, 2022, Cell.

Local membrane charge regulates β2 adrenergic receptor coupling to Gi3

B. Kobilka, D. Hilger, S. Maeda, 2019, Nature Communications.

Conformational Complexity and Dynamics in a Muscarinic Receptor Revealed by NMR Spectroscopy.

B. Kobilka, Hongwei Li, C. Jin, 2019, Molecular cell.

Activation of the α2B adrenoceptor by the sedative sympatholytic dexmedetomidine

B. Kobilka, P. Gmeiner, Zhongmin Liu, 2020, Nature Chemical Biology.

Structure Analysis of Poly(propylene-β-d oxide) by Proton Nuclear Magnetic Resonance Spectroscopy

S. Maeda, N. Oguni, H. Tani, 1973 .

Atypical structural snapshots of human cytomegalovirus GPCR interactions with host G proteins

Hideaki E. Kato, R. Dror, G. Skiniotis, 2022, Science advances.

Structure of the connexin 26 gap junction channel at 3.5 Å resolution

So Nakagawa, Yoshinori Fujiyoshi, Tomitake Tsukihara, 2009, Nature.

Probing Gαi1 protein activation at single–amino acid resolution

Tilman Flock, Dawei Sun, M Madan Babu, 2015, Nature Structural &Molecular Biology.

Structural basis for the constitutive activity and immunomodulatory properties of the Epstein-Barr virus-encoded G protein-coupled receptor BILF1.

K. Garcia, M. Rosenkilde, G. Skiniotis, 2021, Immunity.

Structure of a Signaling Cannabinoid Receptor 1-G Protein Complex

Ron O. Dror, Brian K. Kobilka, Naomi R. Latorraca, 2019, Cell.

Ligand Binding of the Second PDZ Domain Regulates Clustering of PSD-95 with the Kv1.4 Potassium Channel*

Y. Fujiyoshi, S. Maeda, T. Doi, 2002, The Journal of Biological Chemistry.

Development of an antibody fragment that stabilizes GPCR/G-protein complexes

G. Skiniotis, B. Kobilka, Hongli Hu, 2018, Nature Communications.

A description of the structural determination procedures of a gap junction channel at 3.5 Å resolution

E. Yamashita, T. Tsukihara, S. Maeda, 2009, Acta crystallographica. Section D, Biological crystallography.

Structure and selectivity engineering of the M1 muscarinic receptor toxin complex

K. Garcia, R. Sunahara, B. Kobilka, 2020, Science.

Structural mechanism underlying primary and secondary coupling between GPCRs and the Gi/o family

K. Chung, S. Maeda, Yang Du, 2020, Nature Communications.

Structure of the µ-opioid receptor–Gi protein complex

Naomi R. Latorraca, Joseph M. Paggi, G. Skiniotis, 2018, Nature.

Structural and dynamic insights into supra-physiological activation and allosteric modulation of a muscarinic acetylcholine receptor

B. Kobilka, A. Inoue, S. Maeda, 2023, Nature Communications.

Cryo-EM structure of the rhodopsin-Gαi-βγ complex reveals binding of the rhodopsin C-terminal tail to the gβ subunit

H. Stahlberg, T. Flock, R. Dawson, 2019, bioRxiv.

Crystallization Scale Preparation of a Stable GPCR Signaling Complex between Constitutively Active Rhodopsin and G-Protein

Gebhard F. X. Schertler, Dawei Sun, Dmitry B. Veprintsev, 2014, PloS one.

Development of an antibody fragment that stabilizes GPCR/G-protein complexes

G. Skiniotis, B. Kobilka, Hongli Hu, 2018, Nature Communications.

Asparagine 175 of Connexin32 Is a Critical Residue for Docking and Forming Functional Heterotypic Gap Junction Channels with Connexin26*

T. Tsukihara, Yuhua Dong, S. Maeda, 2011, The Journal of Biological Chemistry.

Structural insights into the subtype-selective antagonist binding to the M2 muscarinic receptor

N. Vaidehi, B. Kobilka, S. Iwata, 2018, Nature Chemical Biology.

Production of GPCR and GPCR complexes for structure determination.

G. Schertler, S. Maeda, Gebhard F X Schertler, 2013, Current opinion in structural biology.

Crystal structure of rationally thermostabilized M2 muscarinic acetylcholine receptor bound with NMS (Hg-derivative)

N. Vaidehi, B. Kobilka, S. Iwata, 2018 .

Oxidation Driven Reversal of PIP2-dependent Gating in GIRK2 Channels

C. Nichols, S. Maeda, Sun-Joo Lee, 2023, Function.

Oxidation driven reversal of PIP2-dependent gating in GIRK2 channels.

C. Nichols, S. Maeda, Sun Joo Lee, 2023, Biophysical journal.

Purification, complete amino acid sequence and structural characterization of the heat-stable sweet protein, mabinlin II.

Z. Hu, S. Maeda, Xiaozhu Liu, 1993, European journal of biochemistry.