Amino-terminal basic residues of Src mediate membrane binding through electrostatic interaction with acidic phospholipids - Test2 - elhamkhani - TriplyDB

Amino-terminal basic residues of Src mediate membrane binding through electrostatic interaction with acidic phospholipids

Amino-terminal basic residues of Src mediate membrane binding through electrostatic interaction with acidic phospholipids

http://www.wikidata.org/entity/Q24564497

about

Palmitoylation by DHHC5/8 targets GRIP1 to dendritic endosomes to regulate AMPA-R trafficking Myristoylation and differential palmitoylation of the HCK protein-tyrosine kinases govern their attachment to membranes and association with caveolae Myristoylated Naked2 escorts transforming growth factor alpha to the basolateral plasma membrane of polarized epithelial cells Electrostatic binding of proteins to membranes. Theoretical predictions and experimental results with charybdotoxin and phospholipid vesicles High-affinity interaction of the N-terminal myristoylation motif of the neuronal calcium sensor protein hippocalcin with phosphatidylinositol 4,5-bisphosphate Alterations in the MA and NC domains modulate phosphoinositide-dependent plasma membrane localization of the Rous sarcoma virus Gag protein Differential membrane binding of the human immunodeficiency virus type 1 matrix protein Regulation of osteoclasts by membrane-derived lipid mediators Interfacial basic cluster in annexin V couples phospholipid binding and trimer formation on membrane surfaces Nonenzymatic Reactions above Phospholipid Surfaces of Biological Membranes: Reactivity of Phospholipids and Their Oxidation Derivatives PIP kinases define PI4,5P₂signaling specificity by association with effectors Posttranslational modifications of the 5'-AMP-activated protein kinase beta1 subunit Targeting of SCG10 to the area of the Golgi complex is mediated by its NH2-terminal region Location and dynamics of basic peptides at the membrane interface: electron paramagnetic resonance spectroscopy of tetramethyl-piperidine-N-oxyl-4-amino-4-carboxylic acid-labeled peptides An SH2-domain-containing kinase negatively regulates the phosphatidylinositol-3 kinase pathway The Molecular Mechanism Underlying Recruitment and Insertion of Lipid-Anchored LC3 Protein into Membranes Specific binding of acidic phospholipids to microtubule-associated protein MAP1B regulates its interaction with tubulin Ras plasma membrane signalling platforms Phospholipase C and D regulation of Src, calcium release and membrane fusion during Xenopus laevis development.Lipid binding by the Unique and SH3 domains of c-Src suggests a new regulatory mechanism.Binding of src-like kinases to the beta-subunit of the interleukin-3 receptor.Fatty acylation of proteins: The long and the short of it.Targeting protein lipidation in disease Src family kinases mediate epidermal growth factor receptor signaling from lipid rafts in breast cancer cells.Basic residues in the matrix domain and multimerization target murine leukemia virus Gag to the virological synapse.c-Src/Lyn kinases activate Helicobacter pylori CagA through tyrosine phosphorylation of the EPIYA motifs.Measurement of membrane binding between recoverin, a calcium-myristoyl switch protein, and lipid bilayers by AFM-based force spectroscopy.Protein myristoylation in health and disease.Conditions for copackaging rous sarcoma virus and murine leukemia virus Gag proteins during retroviral budding.Plasmodium falciparum erythrocyte membrane protein 1 diversity in seven genomes--divide and conquer.Amphitropic proteins: regulation by reversible membrane interactions (review).Repositioning basic residues in the M domain of the Rous sarcoma virus gag protein Posttranslational modifications of the bovine lens beaded filament proteins filensin and CP49.Localization of human immunodeficiency virus type 1 Gag and Env at the plasma membrane by confocal imaging.Chemoattractant-mediated transient activation and membrane localization of Akt/PKB is required for efficient chemotaxis to cAMP in Dictyostelium Conserved domains of the Nullo protein required for cell-surface localization and formation of adherens junctions Binding of small basic peptides to membranes containing acidic lipids: theoretical models and experimental results.Selected glimpses into the activation and function of Src kinase.Myristoylation and membrane binding regulate c-Src stability and kinase activity Requirement of a vasodilator-stimulated phosphoprotein family member for cell adhesion, the formation of filopodia, and chemotaxis in dictyostelium.

P2860

Q24305056-B5E23DD1-E3CB-49D0-AFD3-DC6B108C8401 Q24323219-1E412E95-EF13-4D13-8EDE-697958C01273 Q24324074-7581A1CA-04CD-4A0A-B1C5-70B0F42B59E7 Q24532908-149D5759-AF53-4FE5-821D-FB61C2F0FE2D Q24537124-875DF7E4-7ADA-4ABA-BF1D-652ED49315E5 Q24609231-5A50F333-6DB4-4F89-87A4-728745E2FAC5 Q24679629-C0D05F08-3BD5-4662-849A-AB8E23DB28AF Q26996000-EC4FFEC8-E07A-4A11-9CA0-C2E30226C440 Q27639873-F51CDA4B-EC40-41B9-BD5A-71C79EFBC63B Q28080632-3E35B5F4-7BD3-41DD-BDC0-DE89EA23352C Q28083975-C90786A1-FFF0-4B4C-A454-7B3C31FADA5F Q28249598-A0C4D7AE-BA39-4A19-9F0E-BBDB1220A72A Q28303504-A489E53E-5292-407C-A698-49F72EC52C44 Q28359658-5D6AB58D-DAEC-4C06-84B3-B6707893E466 Q28361516-AC33CFE1-D201-4E1D-8DB0-FC6D60F9AF07 Q28394509-49B509CE-F04D-4CE6-A565-37BA4A47FA90 Q28581442-C5CCC7B5-CCAE-42A8-A06C-8217BF0CDE2A Q28769530-5E659349-D320-48B6-9C49-2D8128F2BC94 Q30009210-787E5213-BAE9-474B-A28B-7898CCFB5017 Q30009924-46CCA872-BA58-400E-B56D-7EF17EAE149F Q30176500-23EE2CBD-327A-46E1-87A7-3D3635399B4F Q30388573-3E338CEE-5013-4390-99A4-FA93E2867ACA Q30413212-E632A922-0E1B-4E69-A332-1EC0E06E778B Q30424531-ED8D7D61-C6AC-4707-9D97-E7E62B6D7883 Q30540433-590C4FC7-1F4D-4A38-9AE1-516A5C98644A Q30829845-185D9E11-3146-4D57-9367-65036A18CE1D Q31060484-11343295-7BC6-474A-9EF2-9675F9059CCF Q33631172-42C77A60-DEE9-4B47-8764-38E476A41C28 Q33653116-72029A3A-7CAD-4246-978A-E4E3FDF2E923 Q33700519-5B763774-5F49-479C-B77E-D3AA3D593078 Q33741843-16E42E17-80F8-4C14-9BFC-21A93E00D04B Q33827168-F24043CF-1115-4410-9FE7-2E5D27A8C536 Q33845202-CFFEE00E-031A-4624-82F5-B942AE33DAC2 Q33874415-3EFA47BF-DEF2-42AB-B4C2-0E9BBDE7C5ED Q33890748-ADFC3AC9-E81E-49F6-8D84-7471B3CEB52C Q33953344-35202786-808D-4A24-B586-F3BEDE15E570 Q34040242-E8F8B644-27E6-447B-8C07-A518F9D1C168 Q34103644-73E19D77-0B11-4BA3-A6E9-1D06A0B38952 Q34119774-41EAC4FC-2D1B-499D-A3E3-834DAE98AC0F Q34155214-FE0E6CF1-3EFC-479F-A0CF-68503932609A

P2860

Amino-terminal basic residues of Src mediate membrane binding through electrostatic interaction with acidic phospholipids

http://www.wikidata.org/entity/Q24564497

description

1994 nî lūn-bûn

@nan

1994 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

1994 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

1994年の論文

@ja

1994年学术文章

@wuu

1994年学术文章

@zh-cn

1994年学术文章

@zh-hans

1994年学术文章

@zh-my

1994年学术文章

@zh-sg

1994年學術文章

@yue

name

Amino-terminal basic residues ...... tion with acidic phospholipids

@ast

Amino-terminal basic residues ...... tion with acidic phospholipids

@en

Amino-terminal basic residues ...... tion with acidic phospholipids

@nl

type

label

Amino-terminal basic residues ...... tion with acidic phospholipids

@ast

Amino-terminal basic residues ...... tion with acidic phospholipids

@en

Amino-terminal basic residues ...... tion with acidic phospholipids

@nl

prefLabel

Amino-terminal basic residues ...... tion with acidic phospholipids

@ast

Amino-terminal basic residues ...... tion with acidic phospholipids

@en

Amino-terminal basic residues ...... tion with acidic phospholipids

@nl

P1433

Q24564497-616A01A2-A6B9-49EC-855E-60841FF65E90

P1476

Q24564497-4FA6D59E-741C-48D0-9FDC-FC28C2DBED00

P2093

Q24564497-45118F7D-65F3-419F-BD08-507C625244E5

Q24564497-5311E4FE-7246-4C41-B4F4-208A0051546B

Q24564497-5A2A20DA-E4F9-454E-9890-ABD8F3DA7152

Q24564497-DB03700C-4D46-4AF8-BCA0-A9926A523FF2

Q24564497-DD4CF7DF-F5AB-4E35-A615-1F0311BE9F1B

P2860

Q24564497-0914B94F-DE4F-40DA-99E4-33BA40F660A4

Q24564497-0E247E8E-7DD3-4EC0-8FA5-03BE495B90D6

Q24564497-14AA4B5E-D9F5-4DE4-B130-D8F7F6E3C2A1

Q24564497-15AAD8B6-E26E-4652-B725-BD1BBCC606FB

Q24564497-1758157F-4FC1-483D-B98D-CDD3D3C60C8B

Q24564497-19CE15F5-7261-47B2-8A45-376FD6A3C65E

Q24564497-33F6E9C3-A25D-4BD3-BE36-B52B62C78255

Q24564497-4FC0A988-0E2C-48FE-AC65-0D1F0B5B0936

Q24564497-59766795-99C6-4ED1-9374-45925FEB5C67

Q24564497-7318B385-1BA6-465C-A95C-D93BD937FE5A

P304

Q24564497-9AAE55FF-055F-4225-A7E0-AD8B92DA6997

P31

Q24564497-5DBF836B-C5E9-4ECA-A0CA-774FAD3FC51D

P3181

Q24564497-8068A583-7C62-47BC-A8D5-351E9B770D72

P356

Q24564497-B3314F4C-9D48-40C1-B1CA-42881993279E

P407

Q24564497-3C54213A-CC6E-4336-B1DB-74EF0295392D

P433

Q24564497-1AE34008-07E6-4744-AFD9-DB795F0DC204

P478

Q24564497-4B610C8E-D681-4B57-9384-B7934B8DE76A

P577

Q24564497-EA465ADC-612C-439D-AB4C-81589F458344

P5875

Q24564497-5DF1A1DA-BB8A-42C5-A004-74D80DC82454

P698

Q24564497-3C5FFFDC-1DCB-48E9-B84F-273929829CF5

P932

Q24564497-EC7F8C53-AD4C-49DF-A8A2-0D2CAB5646D9

P3181

P356

PNAS.91.25.12253

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Amino-terminal basic residues ...... tion with acidic phospholipids

@en

P2093

C A Buser

http://www.w3.org/2001/XMLSchema#string

C T Sigal

http://www.w3.org/2001/XMLSchema#string

M D Resh

http://www.w3.org/2001/XMLSchema#string

S McLaughlin

http://www.w3.org/2001/XMLSchema#string

W Zhou

http://www.w3.org/2001/XMLSchema#string

P2860

Binding of peptides with basic residues to membranes containing acidic phospholipids

Identification of a membrane-binding domain within the amino-terminal region of human immunodeficiency virus type 1 Gag protein which interacts with acidic phospholipids

Amino terminal myristylation of the protein kinase p60src, a retroviral transforming protein

Binding of transforming protein, P47gag-crk, to a broad range of phosphotyrosine-containing proteins.

Phosphorylation reverses the membrane association of peptides that correspond to the basic domains of MARCKS and neuromodulin.

Activation and suppression of pp60c-src transforming ability by mutation of its primary sites of tyrosine phosphorylation.

The src protein contains multiple domains for specific attachment to membranes.

Adhesion plaques of Rous sarcoma virus-transformed cells contain the src gene product.

Lysine residues form an integral component of a novel NH2-terminal membrane targeting motif for myristylated pp60v-src.

Association of p60c-src with endosomal membranes in mammalian fibroblasts

P304

12253-7

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P3181

1811475

http://www.w3.org/2001/XMLSchema#string

P356

10.1073/PNAS.91.25.12253

http://www.w3.org/2001/XMLSchema#string

P407

P433

25

http://www.w3.org/2001/XMLSchema#string

P478

91

http://www.w3.org/2001/XMLSchema#string

P577

1994-12-06T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

15670668

http://www.w3.org/2001/XMLSchema#string

P698

7527558

http://www.w3.org/2001/XMLSchema#string

P932

45415

http://www.w3.org/2001/XMLSchema#string