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Publication : proceedings of the national academy of sciences of the united states of america
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Academic Journal

An AAGAB-to-CCDC32 handover mechanism controls the assembly of the AP2 adaptor complex.

  • Authors : Wan C; Department of Molecular, Cellular and Developmental Biology, University of Colorado, Boulder, CO 80309.; Puscher H

Subjects: Adaptor Protein Complex 2*/Adaptor Protein Complex 2*/Adaptor Protein Complex 2*/metabolism ; Adaptor Protein Complex 2*/Adaptor Protein Complex 2*/Adaptor Protein Complex 2*/genetics ; Molecular Chaperones*/Molecular Chaperones*/Molecular Chaperones*/metabolism

  • Source: Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2024 Aug 20; Vol. 121 (34), pp. e2409341121. Publisher: National Academy of Sciences Country of Publication: United States NLM ID: 7505876 Publication Model: Print-Electronic Cited Medium: Internet

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Academic Journal

Engineered polymer nanoparticles as artificial chaperones facilitating the selective refolding of denatured enzymes.

  • Authors : Li Y; State Key Laboratory of Organic-Inorganic Composites, National Energy Research and Development Center for Biorefinery, International Joint Bioenergy Laboratory of Ministry of Education, Beijing Key Laboratory of Bioprocess, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing 100029, China.; Metabolic and Biomolecular Engineering National Research Laboratory and Systems Metabolic Engineering and Systems Healthcare Cross-Generation Collaborative Laboratory, Department of Chemical and Biomolecular Engineering (BK21 four), Korea Advanced Institute of Science and Technology, Daejeon 34141, Republic of Korea.

Subjects: Nanoparticles*/Nanoparticles*/Nanoparticles*/chemistry ; Molecular Chaperones*/Molecular Chaperones*/Molecular Chaperones*/chemistry ; Molecular Chaperones*/Molecular Chaperones*/Molecular Chaperones*/metabolism

  • Source: Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2024 May 07; Vol. 121 (19), pp. e2403049121. Publisher: National Academy of Sciences Country of Publication: United States NLM ID: 7505876 Publication Model: Print-Electronic Cited Medium: Internet

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Academic Journal

Data-driven large-scale genomic analysis reveals an intricate phylogenetic and functional landscape in J-domain proteins.

  • Authors : Malinverni D; Department of Structural Biology and Center for Data Driven Discovery, St. Jude Children's Research Hospital, Memphis, TN 38105.; Zamuner S

Subjects: HSP70 Heat-Shock Proteins*/HSP70 Heat-Shock Proteins*/HSP70 Heat-Shock Proteins*/metabolism ; Molecular Chaperones*/Molecular Chaperones*/Molecular Chaperones*/metabolism; Humans

  • Source: Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2023 Aug 08; Vol. 120 (32), pp. e2218217120. Publisher: National Academy of Sciences Country of Publication: United States NLM ID: 7505876 Publication Model: Print-Electronic Cited Medium: Internet

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Academic Journal

Germline C1GALT1C1 mutation causes a multisystem chaperonopathy.

  • Authors : Erger F; Institute of Human Genetics, University Hospital Cologne, Faculty of Medicine, University of Cologne, 50931 Cologne, Germany.; Center for Molecular Medicine Cologne, University of Cologne, 50931 Cologne, Germany.

Subjects: Molecular Chaperones*/Molecular Chaperones*/Molecular Chaperones*/metabolism ; Acute Kidney Injury*; Male

  • Source: Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2023 May 30; Vol. 120 (22), pp. e2211087120. Publisher: National Academy of Sciences Country of Publication: United States NLM ID: 7505876 Publication Model: Print-Electronic Cited Medium: Internet

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Academic Journal

Structure of metallochaperone in complex with the cobalamin-binding domain of its target mutase provides insight into cofactor delivery.

  • Authors : Vaccaro FA; Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 01239.; Born DA

Subjects: Metallochaperones* ; Molecular Chaperones*/Molecular Chaperones*/Molecular Chaperones*/metabolism; Humans Methylmalonic acidemia

  • Source: Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2023 Feb 21; Vol. 120 (8), pp. e2214085120. Publisher: National Academy of Sciences Country of Publication: United States NLM ID: 7505876 Publication Model: Print-Electronic Cited Medium: Internet

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Academic Journal

Memo1 binds reduced copper ions, interacts with copper chaperone Atox1, and protects against copper-mediated redox activity in vitro.

  • Authors : Zhang X; Department of Biology and Biological Engineering, Chalmers University of Technology, 412 96 Gothenburg, Sweden.; Walke GR

Subjects: Copper*/Copper*/Copper*/metabolism ; Copper Transport Proteins*/Copper Transport Proteins*/Copper Transport Proteins*/genetics ; Copper Transport Proteins*/Copper Transport Proteins*/Copper Transport Proteins*/metabolism

  • Source: Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2022 Sep 13; Vol. 119 (37), pp. e2206905119. Publisher: National Academy of Sciences Country of Publication: United States NLM ID: 7505876 Publication Model: Print-Electronic Cited Medium: Internet

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Academic Journal

Structure of IMPORTIN-4 bound to the H3-H4-ASF1 histone-histone chaperone complex.

  • Authors : Bernardes NE; Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, TX 75390.; Fung HYJ

Subjects: Histone Chaperones*/Histone Chaperones*/Histone Chaperones*/chemistry ; Histones*/Histones*/Histones*/chemistry ; Karyopherins*/Karyopherins*/Karyopherins*/chemistry

  • Source: Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2022 Sep 20; Vol. 119 (38), pp. e2207177119. Publisher: National Academy of Sciences Country of Publication: United States NLM ID: 7505876 Publication Model: Print-Electronic Cited Medium: Internet

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Academic Journal

Phosphorylation of Arl4A/D promotes their binding by the HYPK chaperone for their stable recruitment to the plasma membrane.

  • Authors : Lin MC; Institute of Molecular Medicine, National Taiwan University, Taipei, Taiwan 10002.; Center of Precision Medicine, National Taiwan University, Taipei, Taiwan 10002.

Subjects: ADP-Ribosylation Factors*/ADP-Ribosylation Factors*/ADP-Ribosylation Factors*/metabolism ; Carrier Proteins*/Carrier Proteins*/Carrier Proteins*/metabolism ; Cell Membrane*/Cell Membrane*/Cell Membrane*/metabolism

  • Source: Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2022 Jul 26; Vol. 119 (30), pp. e2207414119. Publisher: National Academy of Sciences Country of Publication: United States NLM ID: 7505876 Publication Model: Print-Electronic Cited Medium: Internet

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Academic Journal

The sacrificial adaptor protein Skp functions to remove stalled substrates from the β-barrel assembly machine.

  • Authors : Combs AN; Department of Molecular Biology, Princeton University, Princeton, NJ 08544.; Silhavy TJ

Subjects: DNA-Binding Proteins/DNA-Binding Proteins/DNA-Binding Proteins/*physiology ; Escherichia coli Proteins/Escherichia coli Proteins/Escherichia coli Proteins/*physiology ; Molecular Chaperones/Molecular Chaperones/Molecular Chaperones/*physiology

  • Source: Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2022 Jan 04; Vol. 119 (1).Publisher: National Academy of Sciences Country of Publication: United States NLM ID: 7505876 Publication Model: Print Cited Medium: Internet ISSN:

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Academic Journal

Chaperones Skp and SurA dynamically expand unfolded OmpX and synergistically disassemble oligomeric aggregates.

  • Authors : Chamachi N; B CUBE - Center for Molecular Bioengineering, Technische Universität Dresden, 01307 Dresden, Germany.; Hartmann A

Subjects: Bacterial Outer Membrane Proteins/Bacterial Outer Membrane Proteins/Bacterial Outer Membrane Proteins/*metabolism ; Biopolymers/Biopolymers/Biopolymers/*metabolism ; Molecular Chaperones/Molecular Chaperones/Molecular Chaperones/*metabolism

  • Source: Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2022 Mar 01; Vol. 119 (9).Publisher: National Academy of Sciences Country of Publication: United States NLM ID: 7505876 Publication Model: Print Cited Medium: Internet ISSN:

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  • 1-10 of  1,882 results for ""Molecular Chaperones""