Erdjan Salih

ORCID: 0000-0003-3322-2323
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About
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Research Areas
  • Bone and Dental Protein Studies
  • Oral microbiology and periodontitis research
  • Advanced Proteomics Techniques and Applications
  • dental development and anomalies
  • Bone Metabolism and Diseases
  • Periodontal Regeneration and Treatments
  • Peptidase Inhibition and Analysis
  • Cholinesterase and Neurodegenerative Diseases
  • Salivary Gland Disorders and Functions
  • Bone Tissue Engineering Materials
  • Enzyme Production and Characterization
  • Endodontics and Root Canal Treatments
  • Bone health and treatments
  • Papaya Research and Applications
  • Chemical Reaction Mechanisms
  • Mass Spectrometry Techniques and Applications
  • Phytase and its Applications
  • Protein Hydrolysis and Bioactive Peptides
  • Enzyme function and inhibition
  • Metal complexes synthesis and properties
  • Bone fractures and treatments
  • Cassava research and cyanide
  • Protease and Inhibitor Mechanisms
  • Biochemical and Structural Characterization
  • Plant biochemistry and biosynthesis

Boston University
2008-2020

Boston Medical Center
2010-2019

University Medical Center
2011-2019

Harvard University
2003-2014

Boston Children's Hospital
1998-2011

Kanagawa Dental University
2010

Harvard University Press
2003

Mater Misericordiae University Hospital
1998

University College Dublin
1998

Brandeis University
1989-1994

Dentin matrix protein-1 (DMP1) is a mineralized tissue protein synthesized by osteoblasts, hypertrophic chondrocytes, and ameloblasts as well odontoblasts. DMP1 believed to have multiple in vivo functions, acting both signaling molecule regulator of biomineralization. Using cell-free system vitro, we evaluated the action regulation hydroxylapatite (HA) formation crystal growth. The non-phosphorylated recombinant acted an HA nucleator, increasing amount mineral formed gelatin gel growth...

10.1074/jbc.m314114200 article EN cc-by Journal of Biological Chemistry 2004-04-01

Recent research efforts in oral biology have resulted elucidation of the proteomes major human salivary secretions and whole saliva. One might hypothesize that proteome minor gland may show significantly different characteristics when compared with parotid or submandibular/sublingual secretions. To test this hypothesis, we conducted first exploration into secretion. Minor secretion was obtained from healthy volunteers, its components were subjected to...

10.1177/154405910808700508 article EN Journal of Dental Research 2008-05-01

Application of quantitative stable isotope-labelling chemistries and mass spectrometry (MS) to determine alterations in gingival crevicular fluid (GCF) proteome periodontal disease.Quantitative GCF from 40 healthy individuals versus patients with disease was established using 320 samples reagents, ICAT mTRAQ, MS technology validated by enzyme-linked immunosorbent methods.We have identified 238 distinct proteins which 180 were quantified both additional 26 32 that found only or patients. In...

10.1111/jcpe.12262 article EN Journal Of Clinical Periodontology 2014-04-16

To evaluate the effects of bioactive molecules in pulpal wound healing, we carried out experiments using rat upper molars as an vivo model. Cavities were prepared on mesial aspect, and pulp perforation was accomplished by application pressure with tip a steel probe. After pulp-capping procedure, cavities filled glass-ionomer cement. Comparison made between among: (1) sham-operated controls dentin predentin fragments implanted during after 8, 14, 28 days; (2) carrier without substance; (3)...

10.1177/08959374010150012401 article EN Advances in Dental Research 2001-08-01

The nonsterile environment of the oral cavity facilitates substantial proteolytic processing, not only resident salivary proteins but also dietary proteins. To gain insight into whole saliva enzymatic processes, in vivo generated peptides this fluid were subjected to nano-flow liquid chromatography electrospray ionization tandem mass spectrometry. 182 identified predominantly derived from acidic and basic proline-rich proteins, statherin, histatins. cleavages occurred preferentially after a...

10.1074/jbc.m708282200 article EN cc-by Journal of Biological Chemistry 2008-05-08

Carneiro LG, Venuleo C, Oppenheim FG, Salih E. Proteome data set of human gingival crevicular fluid from healthy periodontium sites by multidimensional protein separation and mass spectrometry. J Periodont Res 2012; 47: 248–262. © 2011 John Wiley & Sons A/S Background Objective: Gingival has been major interest for many decades as a valuable body that may serve source biomarkers both periodontal systemic diseases. Owing to its very small sample size, submicroliter volumes, identification...

10.1111/j.1600-0765.2011.01429.x article EN Journal of Periodontal Research 2011-10-26

The present study was undertaken to investigate the rate and mode of degradation individual histatin proteins in whole saliva establish impact on its functional domains. Pure synthetic histatins 1, 3, 5 were incubated with supernatant as enzyme source, peptides resultant digests separated by reverse-phase-HPLC structurally characterized electrospray ionization-tandem mass spectrometry. overall V(max)/K(m) ratios, a measure proteolytic efficiency, order histatin-5 > histatin-3 histatin-1....

10.1096/fj.09-131045 article EN The FASEB Journal 2009-04-01

Lysyl oxidase enzyme activity is critical for the biosynthesis of mature and functional collagens elastin. In addition, lysyl has tumor suppressor that been shown to depend on propeptide region (LOX-PP) derived from pro-lysyl (Pro-LOX) not activity. Pro-LOX secreted as a 50 kDa proenzyme then undergoes biosynthetic proteolytic processing active ∼30 LOX LOX-PP. The present study reports efficient recombinant expression purification rat Moreover, using enzymatic deglycosylation DTT...

10.1021/bi902218p article EN Biochemistry 2010-03-01

Osteopontin (OPN) is one of the major secretory phosphoproteins in both calcifying and non-calcifying tissues. Evidence has accumulated for biological importance and, particular, phosphate groups bone formation, resorption, calcification. The precise locations OPN molecule were determined by metabolically labeling with32P cultured chicken osteoblasts, followed purification to homogeneity. N-terminal sequencing showed a single sequence WPVSKRQHAISA, consistent with that deduced from cDNA,...

10.1074/jbc.272.21.13966 article EN cc-by Journal of Biological Chemistry 1997-05-01

1. A model of the three-dimensional structure papaya proteinase omega, most basic cysteine component latex (Carica papaya), was built from its amino acid sequence and two currently known high-resolution crystal structures homologous enzymes papain (EC 3.4.22.2) actinidin 3.4.22.14). The method used a knowledge-based approach incorporated in COMPOSER suite programs refinement by using interactive graphics program FRODO on an Evans Sutherland PS 390 energy minimization GROMOS library. 2....

10.1042/bj2800079 article EN Biochemical Journal 1991-11-15

Human salivary statherin inhibits both primary and secondary calcium phosphate precipitation and, upon binding to hydroxyapatite, associates with a variety of oral bacteria. These functions, crucial in the maintenance tooth enamel integrity, are located defined regions within molecule. Proteases associated saliva, however, cleave effectively, it is importance determine how functional domains affected by these events. Statherin was isolated from human parotid secretion zinc purified...

10.1021/pr100653r article EN Journal of Proteome Research 2010-08-23

Proteases present in oral fluid effectively modulate the structure and function of some salivary proteins have been implicated tissue destruction disease. To identify proteases operating environment, pooled whole saliva supernatant were separated by anion-exchange chromatography individual fractions analyzed for proteolytic activity zymography using histatins as enzyme substrates. Protein bands displaying particularly prominent 50-75 kDa region. Individual excised, in-gel trypsinized...

10.1002/prca.200800242 article EN PROTEOMICS - CLINICAL APPLICATIONS 2009-07-01
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