Source: European journal of biochemistry [Eur J Biochem] 2002 Jul; Vol. 269 (14), pp. 3596-604.Publisher: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies Country of Publication: England NLM ID: 0107600 Publication Model:

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A multi-protein complex containing cold shock domain (Y-box) and polypyrimidine tract binding proteins forms on the vascular endothelial growth factor mRNA. Potential role in mRNA stabilization.

Authors : Coles LS; Division of Human Immunology, The Hanson Institute, Institute of Medical and Veterinary Science, Adelaide, South Australia, Australia. ; Bartley MA

Subjects: DNA-Binding Proteins* ; Heat-Shock Proteins*; Carrier Proteins/Carrier Proteins/Carrier Proteins/*metabolism

Source: European journal of biochemistry [Eur J Biochem] 2004 Feb; Vol. 271 (3), pp. 648-60.Publisher: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies Country of Publication: England NLM ID: 0107600 Publication Model:

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Isolation and characterization of the major gel proteins in human semen, semenogelin I and semenogelin II

Authors : Malm, Johan; Hellman, Jukka; Magnusson, Helena ...

Subjects: Medical and Health Sciences; Basic Medicine; Medicinal Chemistry

Source: European Journal of Biochemistry. 238(1):48-53

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Effect of fatty acid-binding proteins on intermembrane fatty acid transport studies on different types and mutant proteins.

Authors : Veerkamp JH; Department of Biochemistry, University of Nijmegen, The Netherlands. ; Van Moerkerk And HT

Subjects: Neoplasm Proteins* ; Nerve Tissue Proteins* ; Tumor Suppressor Proteins*

Source: European journal of biochemistry [Eur J Biochem] 2000 Oct; Vol. 267 (19), pp. 5959-66.Publisher: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies Country of Publication: England NLM ID: 0107600 Publication Model:

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Biogenesis of the yeast frataxin homolog Yfh1p. Tim44-dependent transfer to mtHsp70 facilitates folding of newly imported proteins in mitochondria.

Authors : Geissler A; Institut für Biochemie und Molekularbiologie, Universität Freiburg, Germany.; Krimmer T

Subjects: Iron-Binding Proteins* ; Mitochondrial Membrane Transport Proteins* ; Protein Folding*

Source: European journal of biochemistry [Eur J Biochem] 2000 Jun; Vol. 267 (11), pp. 3167-80.Publisher: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies Country of Publication: England NLM ID: 0107600 Publication Model:

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Uncoupling proteins 2 and 3 interact with members of the 14.3.3 family.

Authors : Pierrat B; Novartis Pharma Inc., Basle, Switzerland.; Ito M

Subjects: Membrane Transport Proteins* ; Mitochondrial Proteins* ; Tyrosine 3-Monooxygenase*

Source: European journal of biochemistry [Eur J Biochem] 2000 May; Vol. 267 (9), pp. 2680-7.Publisher: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies Country of Publication: England NLM ID: 0107600 Publication Model:

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Functional and molecular identification of novel members of the ubiquitous membrane fusion proteins alpha- and gamma-SNAP (soluble N-ethylmaleimide-sensitive factor-attachment proteins) families in Dictyostelium discoideum.

Authors : Weidenhaupt M; Laboratoire de Biochimie et Biophysique des Systèmes Intégrés (UMR314 CNRS) and Laboratoire de Chimie des Protéines, Département de Biologie Moléculaire et Structurale, CEA-Grenoble, France.; Bruckert F

Subjects: Vesicular Transport Proteins*; Carrier Proteins/Carrier Proteins/Carrier Proteins/*metabolism ; Dictyostelium/Dictyostelium/Dictyostelium/*metabolism

Source: European journal of biochemistry [Eur J Biochem] 2000 Apr; Vol. 267 (7), pp. 2062-70.Publisher: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies Country of Publication: England NLM ID: 0107600 Publication Model:

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Unique structural determinants in the signal peptides of "spontaneously" inserting thylakoid membrane proteins.

Authors : Tissier C; Department of Biological Sciences, University of Warwick, Coventry CV4 7AL, UK.; Woolhead CA

Subjects: Photosystem II Protein Complex* ; Plant Proteins*; Arabidopsis Proteins/Arabidopsis Proteins/Arabidopsis Proteins/*chemistry

Source: European journal of biochemistry [Eur J Biochem] 2002 Jul; Vol. 269 (13), pp. 3131-41.Publisher: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies Country of Publication: England NLM ID: 0107600 Publication Model:

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Streptokinase activates plasminogen bound to human group C and G streptococci through M-like proteins.

Authors : Ben Nasr, A; Wistedt, A; Ringdahl, Ulrika ...

Subjects: Medical and Health Sciences; Basic Medicine; Immunology in the Medical Area (including Cell and Immunotherapy)

Source: European Journal of Biochemistry. 222(2):267-276

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نتائج البحث

فلترة النتائج

Interactions between M proteins of Streptococcus pyogenes and glycosaminoglycans promote bacterial adhesion to host cells.

Antiproliferative proteins of the BTG/Tob family are degraded by the ubiquitin-proteasome system.

A multi-protein complex containing cold shock domain (Y-box) and polypyrimidine tract binding proteins forms on the vascular endothelial growth factor mRNA. Potential role in mRNA stabilization.

Isolation and characterization of the major gel proteins in human semen, semenogelin I and semenogelin II

Effect of fatty acid-binding proteins on intermembrane fatty acid transport studies on different types and mutant proteins.

Biogenesis of the yeast frataxin homolog Yfh1p. Tim44-dependent transfer to mtHsp70 facilitates folding of newly imported proteins in mitochondria.

Uncoupling proteins 2 and 3 interact with members of the 14.3.3 family.

Functional and molecular identification of novel members of the ubiquitous membrane fusion proteins alpha- and gamma-SNAP (soluble N-ethylmaleimide-sensitive factor-attachment proteins) families in Dictyostelium discoideum.

Unique structural determinants in the signal peptides of "spontaneously" inserting thylakoid membrane proteins.

Streptokinase activates plasminogen bound to human group C and G streptococci through M-like proteins.

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