structure prediction software alphafold Search Results


90
GraphPad Software Inc graphpad prism 8
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DNASTAR alphafold 2
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Deepmind Technologies Ltd alphafold protein structure database
Subcellular localization and structure of SmNAC28 . ( A ) Subcellular localization of 35S- SmNAC28 -GFP and the double mutant 35S- SmNAC28 C25+28S -GFP. The 35S-GFP construct served as the control. (Scale bars = 20 μm). Using plasma membrane (PM) and nucleus (NC) markers as reference ( B ) <t>AlphaFold-predicted</t> protein structure of SmNAC28 . The overall protein structure is shown in red; the inset highlights a zoomed-in view of the region containing residues C25 and C28. ( C ) Effect of stress treatment on SmNAC28 localization. GFP fluorescence, bright-field, and merged images of 35S- SmNAC28 -GFP under Mock, NH 2 OH (hydroxylamine treatment), and Salt (100 mM NaCl) conditions are presented. Arrows indicate the relocalization of SmNAC28 from the membrane to the nucleus following NH 2 OH treatment. (Scale bars = 20 μm).
Alphafold Protein Structure Database, supplied by Deepmind Technologies Ltd, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Deepmind Technologies Ltd alphafold repository
Subcellular localization and structure of SmNAC28 . ( A ) Subcellular localization of 35S- SmNAC28 -GFP and the double mutant 35S- SmNAC28 C25+28S -GFP. The 35S-GFP construct served as the control. (Scale bars = 20 μm). Using plasma membrane (PM) and nucleus (NC) markers as reference ( B ) <t>AlphaFold-predicted</t> protein structure of SmNAC28 . The overall protein structure is shown in red; the inset highlights a zoomed-in view of the region containing residues C25 and C28. ( C ) Effect of stress treatment on SmNAC28 localization. GFP fluorescence, bright-field, and merged images of 35S- SmNAC28 -GFP under Mock, NH 2 OH (hydroxylamine treatment), and Salt (100 mM NaCl) conditions are presented. Arrows indicate the relocalization of SmNAC28 from the membrane to the nucleus following NH 2 OH treatment. (Scale bars = 20 μm).
Alphafold Repository, supplied by Deepmind Technologies Ltd, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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alphafold repository - by Bioz Stars, 2026-07
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Deepmind Technologies Ltd chain protein structures
Subcellular localization and structure of SmNAC28 . ( A ) Subcellular localization of 35S- SmNAC28 -GFP and the double mutant 35S- SmNAC28 C25+28S -GFP. The 35S-GFP construct served as the control. (Scale bars = 20 μm). Using plasma membrane (PM) and nucleus (NC) markers as reference ( B ) <t>AlphaFold-predicted</t> protein structure of SmNAC28 . The overall protein structure is shown in red; the inset highlights a zoomed-in view of the region containing residues C25 and C28. ( C ) Effect of stress treatment on SmNAC28 localization. GFP fluorescence, bright-field, and merged images of 35S- SmNAC28 -GFP under Mock, NH 2 OH (hydroxylamine treatment), and Salt (100 mM NaCl) conditions are presented. Arrows indicate the relocalization of SmNAC28 from the membrane to the nucleus following NH 2 OH treatment. (Scale bars = 20 μm).
Chain Protein Structures, supplied by Deepmind Technologies Ltd, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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chain protein structures - by Bioz Stars, 2026-07
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Mendeley Ltd alphafold predicted lyvac pdzd8 structures
Subcellular localization and structure of SmNAC28 . ( A ) Subcellular localization of 35S- SmNAC28 -GFP and the double mutant 35S- SmNAC28 C25+28S -GFP. The 35S-GFP construct served as the control. (Scale bars = 20 μm). Using plasma membrane (PM) and nucleus (NC) markers as reference ( B ) <t>AlphaFold-predicted</t> protein structure of SmNAC28 . The overall protein structure is shown in red; the inset highlights a zoomed-in view of the region containing residues C25 and C28. ( C ) Effect of stress treatment on SmNAC28 localization. GFP fluorescence, bright-field, and merged images of 35S- SmNAC28 -GFP under Mock, NH 2 OH (hydroxylamine treatment), and Salt (100 mM NaCl) conditions are presented. Arrows indicate the relocalization of SmNAC28 from the membrane to the nucleus following NH 2 OH treatment. (Scale bars = 20 μm).
Alphafold Predicted Lyvac Pdzd8 Structures, supplied by Mendeley Ltd, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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InterPro Inc alphafold
Subcellular localization and structure of SmNAC28 . ( A ) Subcellular localization of 35S- SmNAC28 -GFP and the double mutant 35S- SmNAC28 C25+28S -GFP. The 35S-GFP construct served as the control. (Scale bars = 20 μm). Using plasma membrane (PM) and nucleus (NC) markers as reference ( B ) <t>AlphaFold-predicted</t> protein structure of SmNAC28 . The overall protein structure is shown in red; the inset highlights a zoomed-in view of the region containing residues C25 and C28. ( C ) Effect of stress treatment on SmNAC28 localization. GFP fluorescence, bright-field, and merged images of 35S- SmNAC28 -GFP under Mock, NH 2 OH (hydroxylamine treatment), and Salt (100 mM NaCl) conditions are presented. Arrows indicate the relocalization of SmNAC28 from the membrane to the nucleus following NH 2 OH treatment. (Scale bars = 20 μm).
Alphafold, supplied by InterPro Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Benchling Inc algorithms imagej nih
Subcellular localization and structure of SmNAC28 . ( A ) Subcellular localization of 35S- SmNAC28 -GFP and the double mutant 35S- SmNAC28 C25+28S -GFP. The 35S-GFP construct served as the control. (Scale bars = 20 μm). Using plasma membrane (PM) and nucleus (NC) markers as reference ( B ) <t>AlphaFold-predicted</t> protein structure of SmNAC28 . The overall protein structure is shown in red; the inset highlights a zoomed-in view of the region containing residues C25 and C28. ( C ) Effect of stress treatment on SmNAC28 localization. GFP fluorescence, bright-field, and merged images of 35S- SmNAC28 -GFP under Mock, NH 2 OH (hydroxylamine treatment), and Salt (100 mM NaCl) conditions are presented. Arrows indicate the relocalization of SmNAC28 from the membrane to the nucleus following NH 2 OH treatment. (Scale bars = 20 μm).
Algorithms Imagej Nih, supplied by Benchling Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Deepmind Technologies Ltd alphafolddb
Subcellular localization and structure of SmNAC28 . ( A ) Subcellular localization of 35S- SmNAC28 -GFP and the double mutant 35S- SmNAC28 C25+28S -GFP. The 35S-GFP construct served as the control. (Scale bars = 20 μm). Using plasma membrane (PM) and nucleus (NC) markers as reference ( B ) <t>AlphaFold-predicted</t> protein structure of SmNAC28 . The overall protein structure is shown in red; the inset highlights a zoomed-in view of the region containing residues C25 and C28. ( C ) Effect of stress treatment on SmNAC28 localization. GFP fluorescence, bright-field, and merged images of 35S- SmNAC28 -GFP under Mock, NH 2 OH (hydroxylamine treatment), and Salt (100 mM NaCl) conditions are presented. Arrows indicate the relocalization of SmNAC28 from the membrane to the nucleus following NH 2 OH treatment. (Scale bars = 20 μm).
Alphafolddb, supplied by Deepmind Technologies Ltd, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Benchling Inc alphafold2
Subcellular localization and structure of SmNAC28 . ( A ) Subcellular localization of 35S- SmNAC28 -GFP and the double mutant 35S- SmNAC28 C25+28S -GFP. The 35S-GFP construct served as the control. (Scale bars = 20 μm). Using plasma membrane (PM) and nucleus (NC) markers as reference ( B ) <t>AlphaFold-predicted</t> protein structure of SmNAC28 . The overall protein structure is shown in red; the inset highlights a zoomed-in view of the region containing residues C25 and C28. ( C ) Effect of stress treatment on SmNAC28 localization. GFP fluorescence, bright-field, and merged images of 35S- SmNAC28 -GFP under Mock, NH 2 OH (hydroxylamine treatment), and Salt (100 mM NaCl) conditions are presented. Arrows indicate the relocalization of SmNAC28 from the membrane to the nucleus following NH 2 OH treatment. (Scale bars = 20 μm).
Alphafold2, supplied by Benchling Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Molecular Dynamics Inc alphafold3 predicted structures
Subcellular localization and structure of SmNAC28 . ( A ) Subcellular localization of 35S- SmNAC28 -GFP and the double mutant 35S- SmNAC28 C25+28S -GFP. The 35S-GFP construct served as the control. (Scale bars = 20 μm). Using plasma membrane (PM) and nucleus (NC) markers as reference ( B ) <t>AlphaFold-predicted</t> protein structure of SmNAC28 . The overall protein structure is shown in red; the inset highlights a zoomed-in view of the region containing residues C25 and C28. ( C ) Effect of stress treatment on SmNAC28 localization. GFP fluorescence, bright-field, and merged images of 35S- SmNAC28 -GFP under Mock, NH 2 OH (hydroxylamine treatment), and Salt (100 mM NaCl) conditions are presented. Arrows indicate the relocalization of SmNAC28 from the membrane to the nucleus following NH 2 OH treatment. (Scale bars = 20 μm).
Alphafold3 Predicted Structures, supplied by Molecular Dynamics Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Schrodinger LLC alphafold3 structural prediction
(A) The mutations encoded by each mob1 allele are listed. (B) The indicated strains were grown in liquid YE media at 25°C until they reached mid-log phase and then adjusted to the same cell concentrations measured by optical density (Moreno et al., 1991). Next, 10-fold serial dilutions were made and 2.5 µL of each was spotted on YE agar plates and incubated at the indicated temperatures for 2-3 days prior to imaging. The spot assays were done twice and a representative is shown. (C) The indicated strains were grown in liquid YE media at 25˚C. Samples were collected before and again after growing the cells for an additional 3.5 hours at 36˚C. The cells were then fixed and stained with DAPI and methylene blue. Representative images are shown. The experiment was performed in duplicate. Scale bar, 5 µm. (D) The number of nuclei per cell (top), and the percentage of septated cells (middle) and lysed cells (bottom) were quantified at 36°C from the same experiments as in C. N≥200 cells of each genotype. (E) Ribbon diagram of a structural model of S. pombe Mob1 using <t>AlphaFold3</t> (Abramson et al., 2024). The positions of the N- and C-termini and the positions of the mutated residues in the mob1 alleles are indicated. (F) Schematic of sid2 gene product (drawn to scale). Numbers indicate amino acid position (top). Ribbon diagram of a structural model of S. pombe Mob1 bound to the Sid2 regulatory region and kinase domain using AF3. Mob1 is in magenta, the Sid2 regulatory region is in green, and the Sid2 kinase domain is in cyan (bottom).
Alphafold3 Structural Prediction, supplied by Schrodinger LLC, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


Subcellular localization and structure of SmNAC28 . ( A ) Subcellular localization of 35S- SmNAC28 -GFP and the double mutant 35S- SmNAC28 C25+28S -GFP. The 35S-GFP construct served as the control. (Scale bars = 20 μm). Using plasma membrane (PM) and nucleus (NC) markers as reference ( B ) AlphaFold-predicted protein structure of SmNAC28 . The overall protein structure is shown in red; the inset highlights a zoomed-in view of the region containing residues C25 and C28. ( C ) Effect of stress treatment on SmNAC28 localization. GFP fluorescence, bright-field, and merged images of 35S- SmNAC28 -GFP under Mock, NH 2 OH (hydroxylamine treatment), and Salt (100 mM NaCl) conditions are presented. Arrows indicate the relocalization of SmNAC28 from the membrane to the nucleus following NH 2 OH treatment. (Scale bars = 20 μm).

Journal: Current Issues in Molecular Biology

Article Title: Identification of SmNAC28 Transcription Factor and Its Mechanism of Regulating Salt Tolerance in Eggplant via S-Palmitoylation

doi: 10.3390/cimb48040398

Figure Lengend Snippet: Subcellular localization and structure of SmNAC28 . ( A ) Subcellular localization of 35S- SmNAC28 -GFP and the double mutant 35S- SmNAC28 C25+28S -GFP. The 35S-GFP construct served as the control. (Scale bars = 20 μm). Using plasma membrane (PM) and nucleus (NC) markers as reference ( B ) AlphaFold-predicted protein structure of SmNAC28 . The overall protein structure is shown in red; the inset highlights a zoomed-in view of the region containing residues C25 and C28. ( C ) Effect of stress treatment on SmNAC28 localization. GFP fluorescence, bright-field, and merged images of 35S- SmNAC28 -GFP under Mock, NH 2 OH (hydroxylamine treatment), and Salt (100 mM NaCl) conditions are presented. Arrows indicate the relocalization of SmNAC28 from the membrane to the nucleus following NH 2 OH treatment. (Scale bars = 20 μm).

Article Snippet: The tertiary structures of eggplant NAC proteins were predicted using the AlphaFold Protein Structure Database (DeepMind, Islington, London, UK) ( https://alphafold.com/ , accessed on 25 December 2025).

Techniques: Mutagenesis, Construct, Control, Clinical Proteomics, Membrane, Fluorescence

(A) The mutations encoded by each mob1 allele are listed. (B) The indicated strains were grown in liquid YE media at 25°C until they reached mid-log phase and then adjusted to the same cell concentrations measured by optical density (Moreno et al., 1991). Next, 10-fold serial dilutions were made and 2.5 µL of each was spotted on YE agar plates and incubated at the indicated temperatures for 2-3 days prior to imaging. The spot assays were done twice and a representative is shown. (C) The indicated strains were grown in liquid YE media at 25˚C. Samples were collected before and again after growing the cells for an additional 3.5 hours at 36˚C. The cells were then fixed and stained with DAPI and methylene blue. Representative images are shown. The experiment was performed in duplicate. Scale bar, 5 µm. (D) The number of nuclei per cell (top), and the percentage of septated cells (middle) and lysed cells (bottom) were quantified at 36°C from the same experiments as in C. N≥200 cells of each genotype. (E) Ribbon diagram of a structural model of S. pombe Mob1 using AlphaFold3 (Abramson et al., 2024). The positions of the N- and C-termini and the positions of the mutated residues in the mob1 alleles are indicated. (F) Schematic of sid2 gene product (drawn to scale). Numbers indicate amino acid position (top). Ribbon diagram of a structural model of S. pombe Mob1 bound to the Sid2 regulatory region and kinase domain using AF3. Mob1 is in magenta, the Sid2 regulatory region is in green, and the Sid2 kinase domain is in cyan (bottom).

Journal: microPublication Biology

Article Title: Characterization of temperature-sensitive alleles of the septation initiation network protein Mob1 in Schizosaccharomyces pombe

doi: 10.17912/micropub.biology.001595

Figure Lengend Snippet: (A) The mutations encoded by each mob1 allele are listed. (B) The indicated strains were grown in liquid YE media at 25°C until they reached mid-log phase and then adjusted to the same cell concentrations measured by optical density (Moreno et al., 1991). Next, 10-fold serial dilutions were made and 2.5 µL of each was spotted on YE agar plates and incubated at the indicated temperatures for 2-3 days prior to imaging. The spot assays were done twice and a representative is shown. (C) The indicated strains were grown in liquid YE media at 25˚C. Samples were collected before and again after growing the cells for an additional 3.5 hours at 36˚C. The cells were then fixed and stained with DAPI and methylene blue. Representative images are shown. The experiment was performed in duplicate. Scale bar, 5 µm. (D) The number of nuclei per cell (top), and the percentage of septated cells (middle) and lysed cells (bottom) were quantified at 36°C from the same experiments as in C. N≥200 cells of each genotype. (E) Ribbon diagram of a structural model of S. pombe Mob1 using AlphaFold3 (Abramson et al., 2024). The positions of the N- and C-termini and the positions of the mutated residues in the mob1 alleles are indicated. (F) Schematic of sid2 gene product (drawn to scale). Numbers indicate amino acid position (top). Ribbon diagram of a structural model of S. pombe Mob1 bound to the Sid2 regulatory region and kinase domain using AF3. Mob1 is in magenta, the Sid2 regulatory region is in green, and the Sid2 kinase domain is in cyan (bottom).

Article Snippet: AlphaFold3 structural prediction Protein structure predictions were generated with the AlphaFold3 server (Abramson et al., 2024) and visualized using the PyMOL molecular graphics system (version 3.0, Schrodinger, LLC).

Techniques: Comparison, Incubation, Imaging, Staining