نتایج جستجو برای: proline rich protein

تعداد نتایج: 1372205  

Journal: :کشاورزی (منتشر نمی شود) 0
منیژه سبکدست مربی گروه زراعت و اصلاح نباتات، پردیس کشاورزی و منابع طبیعی کرج، دانشگاه تهران فرنگیس خیال پرست مربی گروه زراعت و اصلاح نباتات، پردیس کشاورزی و منابع طبیعی کرج، دانشگاه تهران

in a pot experiment the effect of water stress on the proteins and proline amino acid content of jam, kurosh, pirooz chickpea cultivars (cicer arientinum) were evaluated using a complete block design with factorial treatments inducing cultivars and watering periods, three, six and nine day intervals in three replications. soluble protein and free proline content of the leaf and the root were me...

Journal: :Plant physiology 1967
R Cleland

Free hydroxyproline inhibits the formation of protein-bound hydroxyproline from proline to a considerably greater extent than it does the incorporation of proline into protein of auxin-treated Avena coleoptiles. This inhibition is greater in the wall than in the cytoplasmic fraction. In the absence of auxin, free hydroxyproline exerts little or no inhibition of hydroxyproline formation. Further...

2013
Kenrick A. Vassall Kyrylo Bessonov Miguel De Avila Eugenia Polverini George Harauz

The classic isoforms of myelin basic protein (MBP) are essential for the formation and maintenance of myelin in the central nervous system of higher vertebrates. The protein is involved in all facets of the development, compaction, and stabilization of the multilamellar myelin sheath, and also interacts with cytoskeletal and signaling proteins. The predominant 18.5-kDa isoform of MBP is an intr...

2013
Aarthi Ravichandran Boon Chuan Low

BPGAP1 is a Rho GTPase-activating protein (RhoGAP) that regulates cell morphogenesis, cell migration, and ERK signaling by the concerted action of its proline-rich region (PRR), RhoGAP domain, and the BNIP-2 and Cdc42GAP homology (BCH) domain. Although multiple cellular targets for the PRR and RhoGAP have been identified, and their functions delineated, the mechanism by which the BCH domain reg...

Journal: :Journal of virology 2011
Qianting Zhai Michael B Landesman Hyo-Young Chung Adam Dierkers Cy M Jeffries Jill Trewhella Christopher P Hill Wesley I Sundquist

The cellular ALIX protein functions within the ESCRT pathway to facilitate intralumenal endosomal vesicle formation, the abscission stage of cytokinesis, and enveloped virus budding. Here, we report that the C-terminal proline-rich region (PRR) of ALIX folds back against the upstream domains and auto-inhibits V domain binding to viral late domains. Mutations designed to destabilize the closed c...

Journal: :The Journal of biological chemistry 1996
X Zhu N S Lamango I Lindberg

The neuroendocrine protein 7B2 is known to be involved in the biosynthesis and activity of prohormone convertase 2 (PC2). Previous studies have demonstrated that while the carboxyl-terminal portion of 7B2 (residues 155-186) regulates the enzymatic activity of PC2, the amino terminus of the molecule (residues 1-151) is required for maturation of proPC2. In this study we employed four different e...

Journal: :Frontiers in bioscience 2012
Zaidoun Salah Akram Alian Rami I Aqeilan

WW domains are protein modules that mediate protein-protein interactions through recognition of proline-rich peptide motifs (PRM) and phosphorylated serine/threonine-proline sites. WW domains are found in many different structural and signaling proteins that are involved in a variety of cellular processes, including RNA transcription and processing, protein trafficking and stability, receptor s...

Journal: :Hypertension 2012
Gustavo R Ares Mohammed Z Haque Eric Delpire Pablo A Ortiz

Salt-sensitive hypertension involves a renal defect preventing the kidney from eliminating excess NaCl. The thick ascending limb of Henle loop reabsorbs ≈ 30% of filtered NaCl via the apical Na-K-2Cl cotransporter (NKCC2). Higher NKCC2 activity and Cl reabsorption have been reported in the thick ascending limbs from Dahl salt-sensitive rats (DSS) fed normal salt. NKCC2 activity is primarily reg...

2011
Ayse Elif Erson Elizabeth M Petty

Hugo: TRIM37 Other names: MUL; KIAA0898; POB1; TEF3 Location: 17q23.2 Local order: Genes flanking TRIM37 oriented from centromere to telomere on 17q23 are: RAD51C, 17q22-q23, D51 homolog C (S. Cerevisiae) PPM1E, 17q23.2, protein phosphatase 1E (PP2C domain containing) TRIM37, 17q22-q23, tripartite motif-containing 37 FAM33A 17q23.2, family with sequence similarity 33, member A PRR11(FLJ11029) 1...

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