Structural and functional characterization of CC chemokine CCL14

Biochemistry

Volumn 46, Issue 35, 2007, Pages 10008-10015

  Blain, Katherine Y ^a,b   Kwiatkowski, Witek ^a   Zhao, Qinghai ^c,d   La Fleur, David ^c,d   Naik, Chethana ^c,d   Chun, Tae Wook ^e   Tsareva, Tatiana ^c,d   Kanakaraj, Palanisamy ^c,d   Laird, Michael W ^c,f   Shah, Rutul ^c,d   George, Lisa ^a   Sanyal, Indra ^c,d   Moore, Paul A ^c,g   Demeler, Borries ^h   Choe, Senyon ^a,b  

^a SALK INSTITUTE FOR BIOLOGICAL STUDIES   (United States)

^b UNIVERSITY OF CALIFORNIA SAN DIEGO   (United States)

^c GLAXOSMITHKLINE   (United States)

^d Drug Development   (United States)

^e NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES   (United States)

^f GENENTECH INC   (United States)

^g Celera Genomics   (United States)

^h UNIVERSITY OF TEXAS HEALTH SCIENCE CENTER AT SAN ANTONIO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CC CHEMOKINE CCL14; INTRACELLULAR CALCIUM FLUX; PHYSIOLOGICALLY RELEVANT CONCENTRATION;

AMINO ACIDS; BINDING SITES; MONOMERS; PROTEINS; PROTEOLYSIS; SURFACE PLASMON RESONANCE; VIRUSES; X RAY CRYSTALLOGRAPHY;

LIGANDS;

BETA CHEMOKINE; CC CHEMOKINE LIGAND 14; CHEMOKINE RECEPTOR CCR5; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; BINDING AFFINITY; CALCIUM TRANSPORT; CELL ACTIVATION; HUMAN; HUMAN CELL; HUMAN IMMUNODEFICIENCY VIRUS 1; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN FUNCTION; PROTEIN PROCESSING; PROTEIN STABILITY; SIGNAL TRANSDUCTION; STRUCTURE ANALYSIS; SURFACE PLASMON RESONANCE; VIRUS DNA CELL DNA INTERACTION; X RAY CRYSTALLOGRAPHY;

BINDING SITES; CALCIUM SIGNALING; CHEMOKINES, CC; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; ENDOPEPTIDASES; HIV-1; HUMANS; INHIBITORY CONCENTRATION 50; PEPTIDE FRAGMENTS; PROTEIN PROCESSING, POST-TRANSLATIONAL; RECEPTORS, CCR5; RECEPTORS, HIV; STRUCTURE-ACTIVITY RELATIONSHIP; SURFACE PLASMON RESONANCE; T-LYMPHOCYTES; ULTRACENTRIFUGATION; VIRUS INTERNALIZATION;

HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 34548472420     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi700936w     Document Type: Article

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