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Academic Journal

Mutual annotation-based prediction of protein domain functions with Domain2GO.

  • Authors : Ulusoy E; Biological Data Science Lab, Department of Computer Engineering, Hacettepe University, Ankara, Turkey.; Department of Bioinformatics, Graduate School of Health Sciences, Hacettepe University, Ankara, Turkey.

Subjects: Protein Domains* ; Proteins*/Proteins*/Proteins*/chemistry ; Proteins*/Proteins*/Proteins*/metabolism

  • Source: Protein science : a publication of the Protein Society [Protein Sci] 2024 Jun; Vol. 33 (6), Publisher: Cold Spring Harbor Laboratory Press Country of Publication: United States NLM ID: 9211750 Publication Model: Print Cited Medium: Internet

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Academic Journal

The role of the STAS domain in SLC26A9 for chloride ion transporter function.

  • Authors : Omori S; Graduate School of Information Sciences, Tohoku University, Sendai, Miyagi, Japan; Department of Bioscience, Nagahama Institute of Bio-Science and Technology, Nagahama, Shiga, Japan.

Subjects: Sulfate Transporters*/Sulfate Transporters*/Sulfate Transporters*/metabolism ; Sulfate Transporters*/Sulfate Transporters*/Sulfate Transporters*/chemistry ; Sulfate Transporters*/Sulfate Transporters*/Sulfate Transporters*/genetics

  • Source: Biophysical journal [Biophys J] 2024 Jun 18; Vol. 123 (12), pp. 1751-1762. Date of Electronic Publication: 2024 May 21.Publisher: Cell Press Country of Publication: United States NLM ID: 0370626 Publication Model: Print-Electronic Cited Medium: Internet ISSN:

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Academic Journal

Structural homology-based identification of BEN domain proteins in Poxviruses.

  • Authors : Jia F; State Key Laboratory of Common Mechanism Research for Major Diseases, Department of Molecular Biology and Biochemistry, Institute of Basic Medical Sciences, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing, 100005, China.; Shi Y

Subjects: Poxviridae*/Poxviridae*/Poxviridae*/genetics ; Poxviridae*/Poxviridae*/Poxviridae*/chemistry ; Viral Proteins*/Viral Proteins*/Viral Proteins*/chemistry

  • Source: Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2024 Jun 18; Vol. 712-713, pp. 149933. Date of Electronic Publication: 2024 Apr 16.Publisher: Elsevier Country of Publication: United States NLM ID: 0372516 Publication Model: Print-Electronic Cited Medium: Internet ISSN:

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Academic Journal

Influence of an Intrinsically Disordered Region on Protein Domains Revealed by NMR-Based Electrostatic Potential Measurements.

  • Authors : Yu B; Department of Biochemistry and Molecular Biology, Sealy Center for Structural Biology and Molecular Biophysics, University of Texas Medical Branch, Galveston, Texas 77555-1068, United States.; Wang X

Subjects: Static Electricity* ; Nuclear Magnetic Resonance, Biomolecular* ; HMGB1 Protein*/HMGB1 Protein*/HMGB1 Protein*/chemistry

  • Source: Journal of the American Chemical Society [J Am Chem Soc] 2024 Jun 05; Vol. 146 (22), pp. 14922-14926. Date of Electronic Publication: 2024 May 21.Publisher: American Chemical Society Country of Publication: United States NLM ID: 7503056 Publication Model: Print-Electronic Cited Medium: Internet

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Academic Journal

Structure and interactions of prion-like domains in transcription factor Efg1 phase separation.

  • Authors : Wang SH; Department of Molecular Biology, Cell Biology, and Biochemistry, Brown University, Providence, Rhode Island.; Zheng T

Subjects: Protein Domains* ; Fungal Proteins*/Fungal Proteins*/Fungal Proteins*/metabolism ; Fungal Proteins*/Fungal Proteins*/Fungal Proteins*/chemistry

  • Source: Biophysical journal [Biophys J] 2024 Jun 04; Vol. 123 (11), pp. 1481-1493. Date of Electronic Publication: 2024 Feb 01.Publisher: Cell Press Country of Publication: United States NLM ID: 0370626 Publication Model: Print-Electronic Cited Medium: Internet ISSN:

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Academic Journal

Short disordered termini and proline-rich domain are major regulators of UBQLN1/2/4 phase separation.

  • Authors : Dao TP; Departments of Biology and Chemistry, Syracuse University, Syracuse, New York.; Rajendran A

Subjects: Autophagy-Related Proteins*/Autophagy-Related Proteins*/Autophagy-Related Proteins*/metabolism ; Autophagy-Related Proteins*/Autophagy-Related Proteins*/Autophagy-Related Proteins*/chemistry ; Autophagy-Related Proteins*/Autophagy-Related Proteins*/Autophagy-Related Proteins*/genetics

  • Source: Biophysical journal [Biophys J] 2024 Jun 04; Vol. 123 (11), pp. 1449-1457. Date of Electronic Publication: 2023 Nov 30.Publisher: Cell Press Country of Publication: United States NLM ID: 0370626 Publication Model: Print-Electronic Cited Medium: Internet ISSN:

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Academic Journal

Kainate receptor channel opening and gating mechanism.

  • Authors : Gangwar SP; Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY, USA.; Yelshanskaya MV

Subjects: Cryoelectron Microscopy* ; Receptors, Kainic Acid*/Receptors, Kainic Acid*/Receptors, Kainic Acid*/chemistry ; Receptors, Kainic Acid*/Receptors, Kainic Acid*/Receptors, Kainic Acid*/metabolism

  • Source: Nature [Nature] 2024 Jun; Vol. 630 (8017), pp. 762-768. Date of Electronic Publication: 2024 May 22.Publisher: Nature Publishing Group Country of Publication: England NLM ID: 0410462 Publication Model: Print-Electronic Cited Medium: Internet ISSN:

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Academic Journal

Revealing the role of the X25 domains through the characterization of truncated variants of amylopullulanase enzyme from Thermoanaerobacter brockii brockii.

  • Authors : Kayrav A; Istanbul Technical University, Faculty of Science and Letters, Department of Molecular Biology and Genetics, 34469 Istanbul, Türkiye; Istanbul Technical University, Dr. Orhan Öcalgiray Molecular Biology-Biotechnology and Genetics Research Center, Istanbul, Türkiye.

Subjects: Thermoanaerobacter*/Thermoanaerobacter*/Thermoanaerobacter*/enzymology ; Thermoanaerobacter*/Thermoanaerobacter*/Thermoanaerobacter*/genetics ; Glycoside Hydrolases*/Glycoside Hydrolases*/Glycoside Hydrolases*/genetics

  • Source: International journal of biological macromolecules [Int J Biol Macromol] 2024 Jun; Vol. 270 (Pt 2), pp. 132404. Date of Electronic Publication: 2024 May 14.Publisher: Elsevier Country of Publication: Netherlands NLM ID: 7909578 Publication Model: Print-Electronic Cited Medium: Internet ISSN:

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Academic Journal

1 H, 15 N and 13 C resonance backbone and side-chain assignments and secondary structure determination of the BRCT domain of Mtb LigA.

  • Authors : Vaishnav J; Sophisticated Analytical Instrumentation Facility & Research (SAIF-R), CSIR-Central Drug Research Institute, Lucknow, Uttar Pradesh, 226031, India.; Jawaharlal Nehru University, New Delhi, 110067, India.

Subjects: Mycobacterium tuberculosis* ; Protein Domains* ; Nuclear Magnetic Resonance, Biomolecular*

  • Source: Biomolecular NMR assignments [Biomol NMR Assign] 2024 Jun; Vol. 18 (1), pp. 105-109. Date of Electronic Publication: 2024 Apr 30.Publisher: Springer Country of Publication: Netherlands NLM ID: 101472371 Publication Model: Print-Electronic Cited Medium: Internet ISSN:

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Academic Journal

Chemical shift assignments of the ACID domain of MED25, a subunit of the mediator complex in Arabidopsis thaliana.

  • Authors : Xiong Y; State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, Key Laboratory of Magnetic Resonance in Biological Systems, National Center for Magnetic Resonance in Wuhan, Wuhan Institute of Physics and Mathematics, Innovation Academy for Precision Measurement Science and Technology, Chinese Academy of Sciences - Wuhan National Laboratory for Optoelectronics, Wuhan, 430071, China.; University of Chinese Academy of Sciences, Beijing, 100049, China.

Subjects: Arabidopsis Proteins*/Arabidopsis Proteins*/Arabidopsis Proteins*/chemistry ; Arabidopsis Proteins*/Arabidopsis Proteins*/Arabidopsis Proteins*/metabolism ; Arabidopsis*/Arabidopsis*/Arabidopsis*/chemistry

  • Source: Biomolecular NMR assignments [Biomol NMR Assign] 2024 Jun; Vol. 18 (1), pp. 27-31. Date of Electronic Publication: 2024 Feb 09.Publisher: Springer Country of Publication: Netherlands NLM ID: 101472371 Publication Model: Print-Electronic Cited Medium: Internet ISSN:

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