نتائج البحث

Structural bases for stoichiometry-selective calcium potentiation of a neuronal nicotinic receptor.

• Authors : Mazzaferro S; Department of Physiology and Biomedical Engineering, Mayo Clinic, Rochester, Minnesota, USA.; Wellcome Trust - Medical Research Council Institute of Metabolic Science, University of Cambridge, Cambridge, UK.

Subjects: Receptors, Nicotinic*/Receptors, Nicotinic*/Receptors, Nicotinic*/metabolism ; Receptors, Nicotinic*/Receptors, Nicotinic*/Receptors, Nicotinic*/chemistry ; Receptors, Nicotinic*/Receptors, Nicotinic*/Receptors, Nicotinic*/genetics

• Source: British journal of pharmacology [Br J Pharmacol] 2024 Jul; Vol. 181 (13), pp. 1973-1992. Date of Electronic Publication: 2024 Mar 07.Publisher: Wiley Country of Publication: England NLM ID: 7502536 Publication Model: Print-Electronic Cited Medium:

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Automated cryoelectron microscopy of 'single particles' applied to the 26S proteasome

• Authors : Stephan Nickell; Florian Beck; Wolfgang Baumeister

Subjects: Models, Molecular; Proteasome Endopeptidase Complex; 0303 health sciences

• Source: FEBS Letters. 581:2751-2756

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Cryoelectron microscopy reveals new features in the three‐dimensional structure of phosphorylase kinase

• Authors : Edward P. Gogol; Owen W. Nadeau; Gerald M. Carlson

Subjects: Models, Molecular; 0303 health sciences; 03 medical and health sciences

• Source: Protein Science. 14:914-920

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Vitrification of cryoelectron microscopy specimens revealed by high‐speed photographic imaging

• Authors : Kasas, S.; Dumas, G.; Dietler, G.

Subjects: 0301 basic medicine; 03 medical and health sciences; Time Factors

• Source: Journal of Microscopy. 211:48-53

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A cryoelectron microscopy study of the interaction of the Escherichia coli F1‐ATPase with subunit b dimer

• Authors : Roderick A. Capaldi; Stephan Wilkens; Stanley D. Dunn

Subjects: Cryopreservation; 0303 health sciences; F1-ATPase

• Source: FEBS Letters. 354:37-40

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Structural Study of Heterogeneous Biological Samples by Cryoelectron Microscopy and Image Processing.

• Authors : White HE; Institute of Structural and Molecular Biology, University College London and Birkbeck, Malet Street, London WC1E 7HX, UK.; Ignatiou A

Subjects: Cryoelectron Microscopy/Cryoelectron Microscopy/Cryoelectron Microscopy/*methods ; Image Processing, Computer-Assisted/Image Processing, Computer-Assisted/Image Processing, Computer-Assisted/*methods; Animals

• Source: BioMed research international [Biomed Res Int] 2017; Vol. 2017, pp. 1032432. Date of Electronic Publication: 2017 Jan 15.Publisher: Wiley Country of Publication: United States NLM ID: 101600173 Publication Model: Print-Electronic Cited Medium:

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Cryo‐EM structure of a novel α‐synuclein filament subtype from multiple system atrophy

• Authors : Nicholas L. Yan; Francisco Candido; Eric Tse

Subjects: cryo‐electron microscopy; 0301 basic medicine; α‐synuclein

• Source: FEBS LettFEBS Letters, vol 599, iss 1

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Cryo‐EM structure and biochemical analyses of the nucleosome containing the cancer‐associated histone H3 mutation E97K

• Authors : Tomoaki Kimura; Seiya Hirai; Tomoya Kujirai

Subjects: Histones; 0301 basic medicine; 03 medical and health sciences

• Source: Genes Cells

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cryoelectron microscopy

• Source: Dictionary of Microbiology & Molecular Biology.

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Cryo‐EM reveals transition states of the Acinetobacter baumanniiF1‐ATPase rotary subunits γ and ε, unveiling novel compound targets

• Authors : Khoa Cong Minh Le; Chui Fann Wong; Volker Müller

Subjects: Acinetobacter baumannii; Models, Molecular; Proton-Translocating ATPases

• Source: FASEB J

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