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Wyszukujesz frazę ""Protein Interaction Domains and Motifs"" wg kryterium: Temat


Tytuł :
Calmodulin as Ca -Dependent Interactor of FTO Dioxygenase.
Autorzy :
Marcinkowski M; Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawińskiego 5a, 02-106 Warsaw, Poland.
Pilžys T; Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawińskiego 5a, 02-106 Warsaw, Poland.
Garbicz D; Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawińskiego 5a, 02-106 Warsaw, Poland.
Piwowarski J; Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawińskiego 5a, 02-106 Warsaw, Poland.
Przygońska K; Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawińskiego 5a, 02-106 Warsaw, Poland.
Winiewska-Szajewska M; Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawińskiego 5a, 02-106 Warsaw, Poland.
Ferenc K; Center of Translational Medicine, Warsaw University of Life Sciences, Nowoursynowska 100, 02-797 Warsaw, Poland.
Skorobogatov O; Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawińskiego 5a, 02-106 Warsaw, Poland.
Poznański J; Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawińskiego 5a, 02-106 Warsaw, Poland.
Grzesiuk E; Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawińskiego 5a, 02-106 Warsaw, Poland.
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Źródło :
International journal of molecular sciences [Int J Mol Sci] 2021 Oct 08; Vol. 22 (19). Date of Electronic Publication: 2021 Oct 08.
Typ publikacji :
Journal Article
MeSH Terms :
Calcium Signaling*
Protein Interaction Domains and Motifs*
Alpha-Ketoglutarate-Dependent Dioxygenase FTO/*metabolism
Calcium/*metabolism
Calmodulin/*metabolism
Alpha-Ketoglutarate-Dependent Dioxygenase FTO/chemistry ; Alpha-Ketoglutarate-Dependent Dioxygenase FTO/genetics ; Amino Acid Sequence ; Calmodulin/chemistry ; Calmodulin/genetics ; Humans ; Models, Molecular ; Phosphorylation ; Protein Binding ; Sequence Homology
Czasopismo naukowe
Tytuł :
The Distinct Properties of the Consecutive Disordered Regions Inside or Outside Protein Domains and Their Functional Significance.
Autorzy :
Wang H; State Key Laboratory of Proteomics, Beijing Proteome Research Center, National Center for Protein Sciences (Beijing), Beijing Institute of Lifeomics, Beijing 102206, China.
Zhong H; State Key Laboratory of Proteomics, Beijing Proteome Research Center, National Center for Protein Sciences (Beijing), Beijing Institute of Lifeomics, Beijing 102206, China.
Gao C; State Key Laboratory of Proteomics, Beijing Proteome Research Center, National Center for Protein Sciences (Beijing), Beijing Institute of Lifeomics, Beijing 102206, China.
Zang J; State Key Laboratory of Proteomics, Beijing Proteome Research Center, National Center for Protein Sciences (Beijing), Beijing Institute of Lifeomics, Beijing 102206, China.
Yang D; State Key Laboratory of Proteomics, Beijing Proteome Research Center, National Center for Protein Sciences (Beijing), Beijing Institute of Lifeomics, Beijing 102206, China.
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Źródło :
International journal of molecular sciences [Int J Mol Sci] 2021 Oct 01; Vol. 22 (19). Date of Electronic Publication: 2021 Oct 01.
Typ publikacji :
Journal Article
MeSH Terms :
Protein Domains*
Protein Interaction Domains and Motifs*
Intrinsically Disordered Proteins/*chemistry
Intrinsically Disordered Proteins/*metabolism
Amino Acid Sequence ; Chemical Phenomena ; Gene Expression ; Humans ; Intrinsically Disordered Proteins/genetics ; Protein Binding ; Structure-Activity Relationship
Czasopismo naukowe
Tytuł :
A membrane protein display platform for receptor interactome discovery.
Autorzy :
Cao S; Microchemistry, Proteomics and Lipidomics, Genentech, South San Francisco, CA 94080; .
Peterson SM; Microchemistry, Proteomics and Lipidomics, Genentech, South San Francisco, CA 94080.
Müller S; Oncology Bioinformatics, Genentech, South San Francisco, CA 94080.
Reichelt M; Pathology Labs, Genentech, South San Francisco, CA 94080.
McRoberts Amador C; Biomedical Engineering, Duke University, Durham, NC 27708.
Martinez-Martin N; Microchemistry, Proteomics and Lipidomics, Genentech, South San Francisco, CA 94080; .; Biologics, Almirall, 08022 Barcelona, Spain.
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Źródło :
Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2021 Sep 28; Vol. 118 (39).
Typ publikacji :
Journal Article
MeSH Terms :
Protein Interaction Domains and Motifs*
Antigens, CD/*metabolism
Antigens, Neoplasm/*metabolism
B7 Antigens/*metabolism
B7-H1 Antigen/*metabolism
Membrane Proteins/*metabolism
Antigens, CD/genetics ; Antigens, Neoplasm/genetics ; B7 Antigens/genetics ; B7-H1 Antigen/genetics ; HEK293 Cells ; Humans ; Membrane Proteins/genetics
Czasopismo naukowe
Tytuł :
The Central PXXP Motif Is Crucial for PMAP-23 Translocation across the Lipid Bilayer.
Autorzy :
Yang ST; Department of Microbiology, School of Medicine, Chosun University, Gwangju 61452, Korea.
Shin SY; Department of Cellular and Molecular Medicine, School of Medicine, Chosun University, Gwangju 61452, Korea.
Shin SH; Department of Microbiology, School of Medicine, Chosun University, Gwangju 61452, Korea.
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Źródło :
International journal of molecular sciences [Int J Mol Sci] 2021 Sep 09; Vol. 22 (18). Date of Electronic Publication: 2021 Sep 09.
Typ publikacji :
Journal Article
MeSH Terms :
Amino Acid Motifs*
Lipid Bilayers*
Protein Interaction Domains and Motifs*
Antimicrobial Cationic Peptides/*chemistry
Antimicrobial Cationic Peptides/*metabolism
Cell Membrane/*metabolism
Amino Acid Sequence ; Animals ; Bacteria ; Mice ; Models, Biological ; Peptides/chemistry ; Peptides/metabolism ; Protein Structure, Secondary ; Protein Transport ; Surface Plasmon Resonance ; Swine
Czasopismo naukowe
Tytuł :
Insilico study on the effect of SARS-CoV-2 RBD hotspot mutants' interaction with ACE2 to understand the binding affinity and stability.
Autorzy :
Verma J; School of Computational and Integrative Sciences, Jawaharlal Nehru University, New Delhi, 110067, India. Electronic address: .
Subbarao N; School of Computational and Integrative Sciences, Jawaharlal Nehru University, New Delhi, 110067, India. Electronic address: .
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Źródło :
Virology [Virology] 2021 Sep; Vol. 561, pp. 107-116. Date of Electronic Publication: 2021 Jun 28.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Binding Sites*
Mutation*
Protein Interaction Domains and Motifs*
Angiotensin-Converting Enzyme 2/*chemistry
SARS-CoV-2/*genetics
Spike Glycoprotein, Coronavirus/*chemistry
Spike Glycoprotein, Coronavirus/*genetics
Amino Acids ; Angiotensin-Converting Enzyme 2/metabolism ; COVID-19/metabolism ; COVID-19/virology ; Humans ; Hydrogen Bonding ; Molecular Docking Simulation ; Molecular Dynamics Simulation ; Protein Binding ; Protein Conformation ; Structure-Activity Relationship
SCR Organism :
SARS-CoV-2 variants
Czasopismo naukowe
Tytuł :
Molecular Characterization of NDL1-AGB1 Mediated Salt Stress Signaling: Further Exploration of the Role of NDL1 Interacting Partners.
Autorzy :
Gupta N; Department of Botany, University of Delhi, New Delhi 110007, India.
Kanojia A; Department of Botany, University of Delhi, New Delhi 110007, India.
Katiyar A; Department of Botany, University of Delhi, New Delhi 110007, India.
Mudgil Y; Department of Botany, University of Delhi, New Delhi 110007, India.
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Źródło :
Cells [Cells] 2021 Aug 31; Vol. 10 (9). Date of Electronic Publication: 2021 Aug 31.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Gene Expression Regulation, Plant*
Plant Development*
Protein Interaction Domains and Motifs*
Salt Stress*
Arabidopsis/*growth & development
Arabidopsis Proteins/*metabolism
GTP-Binding Protein beta Subunits/*metabolism
Intracellular Signaling Peptides and Proteins/*metabolism
Arabidopsis/genetics ; Arabidopsis/metabolism ; Arabidopsis Proteins/genetics ; Chlorophyll/physiology ; GTP-Binding Protein beta Subunits/genetics ; Germination ; Intracellular Signaling Peptides and Proteins/genetics ; Phenotype ; Signal Transduction
Czasopismo naukowe
Tytuł :
Characteristics of TIMP1, CD63, and β1-Integrin and the Functional Impact of Their Interaction in Cancer.
Autorzy :
Justo BL; Department of Pharmacology, Escola Paulista de Medicina, Universidade Federal de São Paulo (UNIFESP), Rua Pedro de Toledo 669, 5 Floor, São Paulo 04039-032, Brazil.
Jasiulionis MG; Department of Pharmacology, Escola Paulista de Medicina, Universidade Federal de São Paulo (UNIFESP), Rua Pedro de Toledo 669, 5 Floor, São Paulo 04039-032, Brazil.
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Źródło :
International journal of molecular sciences [Int J Mol Sci] 2021 Aug 27; Vol. 22 (17). Date of Electronic Publication: 2021 Aug 27.
Typ publikacji :
Journal Article; Review
MeSH Terms :
Protein Interaction Domains and Motifs*
Integrin beta1/*metabolism
Neoplasms/*pathology
Tetraspanin 30/*metabolism
Tissue Inhibitor of Metalloproteinase-1/*metabolism
Humans ; Neoplasms/metabolism ; Signal Transduction
Czasopismo naukowe
Tytuł :
Evaluation of the Binding Kinetics of RHEB with mTORC1 by In-Cell and In Vitro Assays.
Autorzy :
Shams R; Emergent Bioengineering Materials Research Team, RIKEN Center for Emergent Matter Science, RIKEN, Wako 351-0198, Saitama, Japan.; Department of Life Science, Graduate School of Science and Engineering, Saitama University, Saitama City 338-8570, Saitama, Japan.
Ito Y; Emergent Bioengineering Materials Research Team, RIKEN Center for Emergent Matter Science, RIKEN, Wako 351-0198, Saitama, Japan.; Nano Medical Engineering Laboratory, RIKEN Cluster for Pioneering Research, RIKEN, Wako 351-0198, Saitama, Japan.
Miyatake H; Department of Life Science, Graduate School of Science and Engineering, Saitama University, Saitama City 338-8570, Saitama, Japan.; Nano Medical Engineering Laboratory, RIKEN Cluster for Pioneering Research, RIKEN, Wako 351-0198, Saitama, Japan.
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Źródło :
International journal of molecular sciences [Int J Mol Sci] 2021 Aug 16; Vol. 22 (16). Date of Electronic Publication: 2021 Aug 16.
Typ publikacji :
Journal Article
MeSH Terms :
Protein Interaction Domains and Motifs*
Mechanistic Target of Rapamycin Complex 1/*metabolism
Ras Homolog Enriched in Brain Protein/*metabolism
Binding Sites ; HEK293 Cells ; Humans ; In Vitro Techniques ; Kinetics ; Mechanistic Target of Rapamycin Complex 1/genetics ; Phosphorylation ; Ras Homolog Enriched in Brain Protein/genetics
Czasopismo naukowe
Tytuł :
PPIDomainMiner: Inferring domain-domain interactions from multiple sources of protein-protein interactions.
Autorzy :
Alborzi SZ; Université de Lorraine, CNRS, Inria, LORIA, Nancy, France.
Ahmed Nacer A; Université de Lorraine, CNRS, Inria, LORIA, Nancy, France.
Najjar H; Mines Nancy, Nancy, France.
Ritchie DW; Université de Lorraine, CNRS, Inria, LORIA, Nancy, France.
Devignes MD; Université de Lorraine, CNRS, Inria, LORIA, Nancy, France.
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Źródło :
PLoS computational biology [PLoS Comput Biol] 2021 Aug 09; Vol. 17 (8), pp. e1008844. Date of Electronic Publication: 2021 Aug 09 (Print Publication: 2021).
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Protein Interaction Domains and Motifs*
Protein Interaction Maps*
Protein Interaction Mapping/*statistics & numerical data
Algorithms ; Computational Biology ; Data Mining/statistics & numerical data ; Databases, Protein/statistics & numerical data ; Humans ; Software
Czasopismo naukowe
Tytuł :
N-terminal Transmembrane-Helix Epitope Tag for X-ray Crystallography and Electron Microscopy of Small Membrane Proteins.
Autorzy :
McIlwain BC; Department of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, MI 48109, United States.
Erwin AL; Life Sciences Institute, University of Michigan, Ann Arbor, MI 48109, United States; Department of Cell and Developmental Biology, University of Michigan, Ann Arbor, MI 48019, United States.
Davis AR; Department of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, MI 48109, United States.
Ben Koff B; Department of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, MI 48109, United States.
Chang L; Life Sciences Institute, University of Michigan, Ann Arbor, MI 48109, United States.
Bylund T; Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, United States.
Chuang GY; Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, United States.
Kwong PD; Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, United States.
Ohi MD; Life Sciences Institute, University of Michigan, Ann Arbor, MI 48109, United States; Department of Cell and Developmental Biology, University of Michigan, Ann Arbor, MI 48019, United States. Electronic address: .
Lai YT; Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, United States; Moderna Therapeutics, 200 Technology Square, Cambridge, MA 02139, United States. Electronic address: .
Stockbridge RB; Department of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, MI 48109, United States; Program in Biophysics, University of Michigan, Ann Arbor, MI 48109, United States. Electronic address: .
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Źródło :
Journal of molecular biology [J Mol Biol] 2021 Aug 06; Vol. 433 (16), pp. 166909. Date of Electronic Publication: 2021 Mar 05.
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.
MeSH Terms :
Models, Molecular*
Protein Interaction Domains and Motifs*
Epitopes/*chemistry
Membrane Proteins/*chemistry
Crystallography, X-Ray ; Epitopes/immunology ; Humans ; Membrane Proteins/immunology ; Microscopy, Electron ; Protein Conformation ; Structure-Activity Relationship
Czasopismo naukowe
Tytuł :
Evidence for Protein-Protein Interaction between Dopamine Receptors and the G Protein-Coupled Receptor 143.
Autorzy :
Bueschbell B; Center for Neuroscience and Cell Biology, University of Coimbra, 3004-504 Coimbra, Portugal.; PhD Programme in Experimental Biology and Biomedicine, Institute for Interdisciplinary Research (IIIUC), University of Coimbra, Casa Costa Alemão, 3030-789 Coimbra, Portugal.
Manga P; Ronald O. Perelman Department of Dermatology, Grossman School of Medicine, New York University, New York, NY 10016, USA.
Penner E; Department of Pharmaceutical & Medicinal Chemistry, Pharmaceutical Institute, University of Bonn, D-53121 Bonn, Germany.
Schiedel AC; Department of Pharmaceutical & Medicinal Chemistry, Pharmaceutical Institute, University of Bonn, D-53121 Bonn, Germany.
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Źródło :
International journal of molecular sciences [Int J Mol Sci] 2021 Aug 03; Vol. 22 (15). Date of Electronic Publication: 2021 Aug 03.
Typ publikacji :
Journal Article
MeSH Terms :
Protein Interaction Domains and Motifs*
Dopamine/*metabolism
Eye Proteins/*metabolism
Membrane Glycoproteins/*metabolism
Receptors, Dopamine D2/*metabolism
Receptors, Dopamine D3/*metabolism
beta-Arrestins/*metabolism
Eye Proteins/genetics ; Humans ; Membrane Glycoproteins/genetics ; Mutation ; Protein Binding ; Receptors, Dopamine D2/genetics ; Receptors, Dopamine D3/genetics ; Signal Transduction
Czasopismo naukowe
Tytuł :
SARS-CoV-2 Nsp3 unique domain SUD interacts with guanine quadruplexes and G4-ligands inhibit this interaction.
Autorzy :
Lavigne M; Institut Pasteur, Département de Virologie. CNRS UMR 3569, Paris, France.
Helynck O; Institut Pasteur, Unité de Chimie et Biocatalyse. CNRS UMR 3523, Paris, France.
Rigolet P; Institut Curie, Université Paris-Saclay, CNRS UMR 9187, Inserm U1196, Orsay, France.
Boudria-Souilah R; Institut Pasteur, Département de Virologie. CNRS UMR 3569, Paris, France.
Nowakowski M; Institut Pasteur, Plateforme de Production et Purification de Protéines Recombinantes, C2RT, CNRS UMR 3528, Paris, France.
Baron B; Institut Pasteur, Plateforme de Biophysique Moléculaire, C2RT, CNRS UMR 3528, Paris, France.
Brülé S; Institut Pasteur, Plateforme de Biophysique Moléculaire, C2RT, CNRS UMR 3528, Paris, France.
Hoos S; Institut Pasteur, Plateforme de Biophysique Moléculaire, C2RT, CNRS UMR 3528, Paris, France.
Raynal B; Institut Pasteur, Plateforme de Biophysique Moléculaire, C2RT, CNRS UMR 3528, Paris, France.
Guittat L; Université Sorbonne Paris Nord, INSERM U978, Labex Inflamex, F-93017 Bobigny, France.; Laboratoire d'optique et Biosciences, Ecole Polytechnique, Inserm U1182, CNRS UMR7645, Institut Polytechnique de Paris, Palaiseau, France.
Beauvineau C; Institut Curie, Université Paris-Saclay, CNRS UMR 9187, Inserm U1196, Orsay, France.
Petres S; Institut Pasteur, Plateforme de Production et Purification de Protéines Recombinantes, C2RT, CNRS UMR 3528, Paris, France.
Granzhan A; Institut Curie, Université Paris-Saclay, CNRS UMR 9187, Inserm U1196, Orsay, France.
Guillon J; Inserm U1212, CNRS UMR 5320, Laboratoire ARNA, UFR des Sciences Pharmaceutiques, Université de Bordeaux, Bordeaux, France.
Pratviel G; CNRS UPR 8241, Université Paul Sabatier, Laboratoire de Chimie de Coordination, Toulouse, France.
Teulade-Fichou MP; Institut Curie, Université Paris-Saclay, CNRS UMR 9187, Inserm U1196, Orsay, France.
England P; Institut Pasteur, Plateforme de Biophysique Moléculaire, C2RT, CNRS UMR 3528, Paris, France.
Mergny JL; Laboratoire d'optique et Biosciences, Ecole Polytechnique, Inserm U1182, CNRS UMR7645, Institut Polytechnique de Paris, Palaiseau, France.
Munier-Lehmann H; Institut Pasteur, Unité de Chimie et Biocatalyse. CNRS UMR 3523, Paris, France.
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Źródło :
Nucleic acids research [Nucleic Acids Res] 2021 Jul 21; Vol. 49 (13), pp. 7695-7712.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
G-Quadruplexes*
Protein Interaction Domains and Motifs*
SARS-CoV-2*
COVID-19/*virology
Coronavirus Papain-Like Proteases/*metabolism
Amino Acid Sequence ; Coronavirus Papain-Like Proteases/chemistry ; Humans ; Ligands ; Models, Molecular ; Protein Binding ; Protein Conformation ; Recombinant Proteins/chemistry ; Recombinant Proteins/metabolism ; Spectrum Analysis ; Structure-Activity Relationship ; Virus Replication
Czasopismo naukowe
Tytuł :
Evolutionary Conservation of Structural and Functional Coupling between the BRM AT-Hook and Bromodomain.
Autorzy :
Lupo BE; University of Iowa, Carver College of Medicine, Department of Biochemistry, Iowa City, IA 52242, United States.
Chu P; University of Iowa, Carver College of Medicine, Department of Biochemistry, Iowa City, IA 52242, United States.
Harms MJ; Institute of Molecular Biology, University of Oregon, Eugene, OR 97403, United States; Department of Chemistry and Biochemistry, University of Oregon, Eugene, OR 97403, United States.
Morrison EA; University of Iowa, Carver College of Medicine, Department of Biochemistry, Iowa City, IA 52242, United States; Medical College of Wisconsin, Department of Biochemistry, Milwaukee, WI 53226, United States. Electronic address: .
Musselman CA; University of Iowa, Carver College of Medicine, Department of Biochemistry, Iowa City, IA 52242, United States; University of Colorado Anschutz Medical Campus, Department of Biochemistry and Molecular Genetics, Aurora, CO 80045, United States. Electronic address: .
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Źródło :
Journal of molecular biology [J Mol Biol] 2021 Jul 09; Vol. 433 (14), pp. 166845. Date of Electronic Publication: 2021 Feb 02.
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.
MeSH Terms :
Conserved Sequence*
Protein Interaction Domains and Motifs*
Transcription Factors/*chemistry
Transcription Factors/*metabolism
Binding Sites ; DNA-Binding Proteins/chemistry ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; Humans ; Models, Molecular ; Mutation ; Protein Binding ; Protein Conformation ; Structure-Activity Relationship ; Transcription Factors/genetics
Czasopismo naukowe
Tytuł :
Simplicity is the Ultimate Sophistication-Crosstalk of Post-translational Modifications on the RNA Polymerase II.
Autorzy :
Venkat Ramani MK; Department of Molecular Biosciences, University of Texas at Austin, Austin, TX 78712, United States.
Yang W; Department of Molecular Biosciences, University of Texas at Austin, Austin, TX 78712, United States.
Irani S; Department of Molecular Biosciences, University of Texas at Austin, Austin, TX 78712, United States.
Zhang Y; Department of Molecular Biosciences, University of Texas at Austin, Austin, TX 78712, United States; The Institute for Cellular and Molecular Biology. University of Texas at Austin, Austin, TX 78712, United States. Electronic address: .
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Źródło :
Journal of molecular biology [J Mol Biol] 2021 Jul 09; Vol. 433 (14), pp. 166912. Date of Electronic Publication: 2021 Mar 05.
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Review
MeSH Terms :
Protein Interaction Domains and Motifs*
Protein Processing, Post-Translational*
RNA Processing, Post-Transcriptional*
RNA Polymerase II/*metabolism
Chromatin/genetics ; Chromatin/metabolism ; Gene Expression Regulation ; Histone Code ; Humans ; Phosphorylation ; Protein Binding ; RNA Polymerase II/chemistry ; Transcription, Genetic
Czasopismo naukowe
Tytuł :
Conserved residues in the extracellular loop 2 regulate Stachel-mediated activation of ADGRG2.
Autorzy :
Gad AA; Department of Surgery, University of Maryland School of Medicine, Baltimore, MD, USA.; Graduate Program in Life Sciences, University of Maryland, Baltimore, MD, USA.
Azimzadeh P; Department of Surgery, University of Maryland School of Medicine, Baltimore, MD, USA.
Balenga N; Department of Surgery, University of Maryland School of Medicine, Baltimore, MD, USA. .; Department of Pharmacology, University of Maryland School of Medicine, Baltimore, MD, USA. .; Molecular and Structural Biology program at University of Maryland Marlene and Stewart Greenebaum NCI Comprehensive Cancer Center, Baltimore, MD, USA. .; Department of Surgery and Pharmacology, University of Maryland School of Medicine, 655 W. Baltimore Street, Room 10-027, Baltimore, MD, 21201, USA. .
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Źródło :
Scientific reports [Sci Rep] 2021 Jul 07; Vol. 11 (1), pp. 14060. Date of Electronic Publication: 2021 Jul 07.
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural
MeSH Terms :
Amino Acid Sequence*
Conserved Sequence*
Protein Interaction Domains and Motifs*
Receptors, G-Protein-Coupled/*chemistry
Receptors, G-Protein-Coupled/*genetics
Receptors, G-Protein-Coupled/*metabolism
Amino Acid Substitution ; Fluorescent Antibody Technique ; Gene Expression ; HEK293 Cells ; Humans ; Mutagenesis, Site-Directed ; Mutation ; Proteolysis ; Signal Transduction ; Structure-Activity Relationship
Czasopismo naukowe
Tytuł :
Active Rap1-mediated inhibition of choroidal neovascularization requires interactions with IQGAP1 in choroidal endothelial cells.
Autorzy :
Ramshekar A; The John A Moran Eye Center, University of Utah, Salt Lake City, UT, USA.
Wang H; The John A Moran Eye Center, University of Utah, Salt Lake City, UT, USA.
Kunz E; The John A Moran Eye Center, University of Utah, Salt Lake City, UT, USA.
Pappas C; The John A Moran Eye Center, University of Utah, Salt Lake City, UT, USA.; Steele Center for Translational Medicine, John A. Moran Eye Center, University of Utah, Salt Lake City, UT, USA.
Hageman GS; The John A Moran Eye Center, University of Utah, Salt Lake City, UT, USA.; Steele Center for Translational Medicine, John A. Moran Eye Center, University of Utah, Salt Lake City, UT, USA.
Chaqour B; Department of Ophthalmology, Downstate Medical Center, Brooklyn, NY, USA.
Sacks DB; Department of Laboratory Medicine, National Institutes of Health, Bethesda, MD, USA.
Hartnett ME; The John A Moran Eye Center, University of Utah, Salt Lake City, UT, USA.
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Źródło :
FASEB journal : official publication of the Federation of American Societies for Experimental Biology [FASEB J] 2021 Jul; Vol. 35 (7), pp. e21642.
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural; Research Support, N.I.H., Intramural; Research Support, Non-U.S. Gov't
MeSH Terms :
Protein Interaction Domains and Motifs*
Choroid/*metabolism
Choroidal Neovascularization/*prevention & control
Endothelial Cells/*metabolism
rap1 GTP-Binding Proteins/*metabolism
ras GTPase-Activating Proteins/*metabolism
Animals ; Cell Movement ; Choroidal Neovascularization/metabolism ; Choroidal Neovascularization/pathology ; Female ; Male ; Mice ; Mice, Inbred C57BL ; Signal Transduction ; rap1 GTP-Binding Proteins/genetics ; ras GTPase-Activating Proteins/genetics
Czasopismo naukowe
Tytuł :
The armadillo-repeat domain of plakophilin 1 binds the C-terminal sterile alpha motif (SAM) of p73.
Autorzy :
Neira JL; IDIBE, Universidad Miguel Hernández, 03202 Elche, Alicante, Spain; Instituto de Biocomputación y Física de Sistemas Complejos (BIFI), Joint Units IQFR-CSIC-BIFI, GBsC-CSIC-BIFI, Universidad de Zaragoza, 50009 Zaragoza, Spain. Electronic address: .
Rizzuti B; Instituto de Biocomputación y Física de Sistemas Complejos (BIFI), Joint Units IQFR-CSIC-BIFI, GBsC-CSIC-BIFI, Universidad de Zaragoza, 50009 Zaragoza, Spain; CNR-NANOTEC, Licryl-UOS Cosenza and CEMIF.Cal, Department of Physics, University of Calabria, 87036 Rende, Italy. Electronic address: .
Ortega-Alarcón D; Instituto de Biocomputación y Física de Sistemas Complejos (BIFI), Joint Units IQFR-CSIC-BIFI, GBsC-CSIC-BIFI, Universidad de Zaragoza, 50009 Zaragoza, Spain.
Giudici AM; IDIBE, Universidad Miguel Hernández, 03202 Elche, Alicante, Spain.
Abián O; Instituto de Biocomputación y Física de Sistemas Complejos (BIFI), Joint Units IQFR-CSIC-BIFI, GBsC-CSIC-BIFI, Universidad de Zaragoza, 50009 Zaragoza, Spain; Instituto de Investigación Sanitaria Aragón (IIS Aragón), 50009 Zaragoza, Spain; Instituto Aragonés de Ciencias de la Salud (IACS), 50009 Zaragoza, Spain; Centro de Investigación Biomédica en Red en el Área Temática de Enfermedades Hepáticas y Digestivas (CIBERehd), Madrid, Spain; Departamento de Bioquímica y Biología Molecular y Celular, Universidad de Zaragoza, 50009 Zaragoza, Spain.
Fárez-Vidal ME; Departamento de Bioquímica y Biología Molecular III e Inmunología, Facultad de Medicina, Universidad de Granada, 18016 Granada, Spain; Instituto de Investigación Biomédica IBS, Complejo Hospitalario Universitario de Granada, Universidad de Granada, 18071 Granada, Spain.
Velázquez-Campoy A; Instituto de Biocomputación y Física de Sistemas Complejos (BIFI), Joint Units IQFR-CSIC-BIFI, GBsC-CSIC-BIFI, Universidad de Zaragoza, 50009 Zaragoza, Spain; Instituto de Investigación Sanitaria Aragón (IIS Aragón), 50009 Zaragoza, Spain; Fundacion ARAID, Government of Aragon, 50009 Zaragoza, Spain; Centro de Investigación Biomédica en Red en el Área Temática de Enfermedades Hepáticas y Digestivas (CIBERehd), Madrid, Spain; Departamento de Bioquímica y Biología Molecular y Celular, Universidad de Zaragoza, 50009 Zaragoza, Spain.
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Źródło :
Biochimica et biophysica acta. General subjects [Biochim Biophys Acta Gen Subj] 2021 Jul; Vol. 1865 (7), pp. 129914. Date of Electronic Publication: 2021 Apr 17.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Protein Interaction Domains and Motifs*
Sterile Alpha Motif*
Armadillo Domain Proteins/*metabolism
Plakophilins/*metabolism
Tumor Protein p73/*metabolism
Armadillo Domain Proteins/chemistry ; Humans ; Models, Molecular ; Molecular Docking Simulation ; Plakophilins/chemistry ; Protein Binding ; Protein Conformation ; Protein Domains ; Tumor Protein p73/chemistry
Czasopismo naukowe
Tytuł :
Post Zygotic, Somatic, Deletion in KERATIN 1 V1 Domain Generates Structural Alteration of the K1/K10 Dimer, Producing a Monolateral Palmar Epidermolytic Nevus.
Autorzy :
Caporali S; Department of Industrial Engineering, University of Rome Tor Vergata, 00133 Rome, Italy.
Didona B; Fondazione Luigi Maria Monti, IDI-IRCCS, 00167 Rome, Italy.
Paradisi M; Department of Experimental Medicine, University of Tor Vergata, 00133 Rome, Italy.
Mauriello A; Department of Experimental Medicine, University of Tor Vergata, 00133 Rome, Italy.
Campione E; Department of Systems Medicine, University of Tor Vergata, 00133 Rome, Italy.
Falconi M; Department of Biology, University of Rome Tor Vergata, Via della Ricerca Scientifica, 00133 Rome, Italy.
Iacovelli F; Department of Biology, University of Rome Tor Vergata, Via della Ricerca Scientifica, 00133 Rome, Italy.
Minieri M; Department of Experimental Medicine, University of Tor Vergata, 00133 Rome, Italy.
Pieri M; Department of Experimental Medicine, University of Tor Vergata, 00133 Rome, Italy.
Bernardini S; Department of Experimental Medicine, University of Tor Vergata, 00133 Rome, Italy.
Terrinoni A; Department of Experimental Medicine, University of Tor Vergata, 00133 Rome, Italy.
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Źródło :
International journal of molecular sciences [Int J Mol Sci] 2021 Jun 27; Vol. 22 (13). Date of Electronic Publication: 2021 Jun 27.
Typ publikacji :
Journal Article
MeSH Terms :
Protein Interaction Domains and Motifs*
Sequence Deletion*
Keratin-1/*chemistry
Keratin-1/*genetics
Keratin-10/*chemistry
Nevus/*etiology
Skin Neoplasms/*etiology
Amino Acid Sequence ; Base Sequence ; Biopsy ; DNA Mutational Analysis ; Fluorescent Antibody Technique ; Humans ; Immunohistochemistry ; Keratin-1/metabolism ; Keratin-10/metabolism ; Models, Molecular ; Nevus/metabolism ; Nevus/pathology ; Protein Conformation ; Protein Multimerization ; Skin Neoplasms/metabolism ; Skin Neoplasms/pathology ; Structure-Activity Relationship
Czasopismo naukowe
Tytuł :
A comprehensive analysis of novel disulfide bond introduction site into the constant domain of human Fab.
Autorzy :
Nakamura H; Faculty of Pharmaceutical Sciences, Sojo University, 4-22-1 Ikeda, Nishi-ku, Kumamoto, 860-0082, Japan.
Yoshikawa M; Faculty of Pharmaceutical Sciences, Sojo University, 4-22-1 Ikeda, Nishi-ku, Kumamoto, 860-0082, Japan.
Oda-Ueda N; Faculty of Pharmaceutical Sciences, Sojo University, 4-22-1 Ikeda, Nishi-ku, Kumamoto, 860-0082, Japan.
Ueda T; Graduate School of Pharmaceutical Sciences, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka, 812-8582, Japan.
Ohkuri T; Faculty of Pharmaceutical Sciences, Sojo University, 4-22-1 Ikeda, Nishi-ku, Kumamoto, 860-0082, Japan. .
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Źródło :
Scientific reports [Sci Rep] 2021 Jun 21; Vol. 11 (1), pp. 12937. Date of Electronic Publication: 2021 Jun 21.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Models, Molecular*
Protein Conformation*
Protein Interaction Domains and Motifs*/genetics
Disulfides/*chemistry
Immunoglobulin Fab Fragments/*chemistry
Antigens/chemistry ; Humans ; Immunoglobulin Fab Fragments/genetics ; Mutation ; Protein Binding ; Protein Stability ; Thermodynamics
Czasopismo naukowe
Tytuł :
Kinetics of the multitasking high-affinity Win binding site of WDR5 in restricted and unrestricted conditions.
Autorzy :
Imran A; Department of Physics, Syracuse University, 201 Physics Building, Syracuse, New York 13244-1130, U.S.A.
Moyer BS; Ichor Therapeutics, Inc., 2521 US Route 11, LaFayette, New York 13084, U.S.A.
Canning AJ; Department of Biochemistry and Molecular Biology, State University of New York, Upstate Medical University, 4249 Weiskotten Hall, 766 Irving Avenue, Syracuse, New York 13210, U.S.A.
Kalina D; Ichor Therapeutics, Inc., 2521 US Route 11, LaFayette, New York 13084, U.S.A.; Department of Chemistry, State University of New York, College of Environmental Science and Forestry, 1 Forestry Dr., Syracuse, New York 13210, U.S.A.
Duncan TM; Department of Biochemistry and Molecular Biology, State University of New York, Upstate Medical University, 4249 Weiskotten Hall, 766 Irving Avenue, Syracuse, New York 13210, U.S.A.
Moody KJ; Department of Physics, Syracuse University, 201 Physics Building, Syracuse, New York 13244-1130, U.S.A.; Ichor Therapeutics, Inc., 2521 US Route 11, LaFayette, New York 13084, U.S.A.; Department of Chemistry, State University of New York, College of Environmental Science and Forestry, 1 Forestry Dr., Syracuse, New York 13210, U.S.A.
Wolfe AJ; Department of Physics, Syracuse University, 201 Physics Building, Syracuse, New York 13244-1130, U.S.A.; Ichor Therapeutics, Inc., 2521 US Route 11, LaFayette, New York 13084, U.S.A.; Department of Chemistry, State University of New York, College of Environmental Science and Forestry, 1 Forestry Dr., Syracuse, New York 13210, U.S.A.
Cosgrove MS; Department of Biochemistry and Molecular Biology, State University of New York, Upstate Medical University, 4249 Weiskotten Hall, 766 Irving Avenue, Syracuse, New York 13210, U.S.A.
Movileanu L; Department of Physics, Syracuse University, 201 Physics Building, Syracuse, New York 13244-1130, U.S.A.; The BioInspired Institute, Syracuse University, Syracuse, New York 13244, U.S.A.; Department of Biomedical and Chemical Engineering, Syracuse University, 329 Link Hall, Syracuse, New York 13244, U.S.A.
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Źródło :
The Biochemical journal [Biochem J] 2021 Jun 11; Vol. 478 (11), pp. 2145-2161.
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural
MeSH Terms :
Protein Interaction Domains and Motifs*
Histone-Lysine N-Methyltransferase/*metabolism
Intracellular Signaling Peptides and Proteins/*metabolism
Peptide Fragments/*metabolism
Amino Acid Motifs ; Binding Sites ; Histone-Lysine N-Methyltransferase/chemistry ; Histone-Lysine N-Methyltransferase/genetics ; Humans ; Intracellular Signaling Peptides and Proteins/chemistry ; Intracellular Signaling Peptides and Proteins/genetics ; Kinetics ; Peptide Fragments/chemistry ; Peptide Fragments/genetics ; Protein Binding ; Protein Conformation
Czasopismo naukowe

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