Advanced Search
Display options
Filter resources
Text Availability
Article type
Publication date
Species
Language
Sex
Age
Showing 25 to 36 of 20335 entries
Sorted by: Best Match Show Resources per page
Inflammatory Cyclooxygenase Activity and PGE.

Current immunology reviews

Johansson JU, Woodling NS, Shi J, Andreasson KI.
PMID: 28413375
Curr Immunol Rev. 2015 Aug;11(2):125-131. doi: 10.2174/1573395511666150707181414.

The inflammatory response is a fundamental driving force in the pathogenesis of Alzheimer's disease (AD). In the setting of accumulating immunogenic Aß peptide assemblies, microglia, the innate immune cells of the brain, generate a non-resolving immune response and fail...

Cite
Johansson JU, Woodling NS, Shi J, et al. Inflammatory Cyclooxygenase Activity and PGE. Curr Immunol Rev. 2015;11(2):125-131doi: 10.2174/1573395511666150707181414.
Johansson, J. U., Woodling, N. S., Shi, J., & Andreasson, K. I. (2015). Inflammatory Cyclooxygenase Activity and PGE. Current immunology reviews, 11(2), 125-131. https://doi.org/10.2174/1573395511666150707181414
Johansson, Jenny U, et al. "Inflammatory Cyclooxygenase Activity and PGE." Current immunology reviews vol. 11,2 (2015): 125-131. doi: https://doi.org/10.2174/1573395511666150707181414
Johansson JU, Woodling NS, Shi J, Andreasson KI. Inflammatory Cyclooxygenase Activity and PGE. Curr Immunol Rev. 2015 Aug;11(2):125-131. doi: 10.2174/1573395511666150707181414. PMID: 28413375; PMCID: PMC5384338.
Copy Download .nbib Format: NLM
Targeting LAMP2 in human cerebrospinal fluid with a combination of immunopurification and high resolution parallel reaction monitoring mass spectrometry.

Clinical proteomics

Sjödin S, Öhrfelt A, Brinkmalm G, Zetterberg H, Blennow K, Brinkmalm A.
PMID: 26924951
Clin Proteomics. 2016 Feb 25;13:4. doi: 10.1186/s12014-016-9104-2. eCollection 2016.

BACKGROUND: Alzheimer's disease is the most common form of dementia. An increasing body of evidence suggests that endo-lysosomal dysfunction is a pathogenic mechanism of Alzheimer's disease. Thus there is a potential for proteins involved in the normal function of...

Cite
Sjödin S, Öhrfelt A, Brinkmalm G, et al. Targeting LAMP2 in human cerebrospinal fluid with a combination of immunopurification and high resolution parallel reaction monitoring mass spectrometry. Clin Proteomics. 2016;13:4doi: 10.1186/s12014-016-9104-2.
Sjödin, S., Öhrfelt, A., Brinkmalm, G., Zetterberg, H., Blennow, K., & Brinkmalm, A. (2016). Targeting LAMP2 in human cerebrospinal fluid with a combination of immunopurification and high resolution parallel reaction monitoring mass spectrometry. Clinical proteomics, 134. https://doi.org/10.1186/s12014-016-9104-2
Sjödin, Simon, et al. "Targeting LAMP2 in human cerebrospinal fluid with a combination of immunopurification and high resolution parallel reaction monitoring mass spectrometry." Clinical proteomics vol. 13 (2016): 4. doi: https://doi.org/10.1186/s12014-016-9104-2
Sjödin S, Öhrfelt A, Brinkmalm G, Zetterberg H, Blennow K, Brinkmalm A. Targeting LAMP2 in human cerebrospinal fluid with a combination of immunopurification and high resolution parallel reaction monitoring mass spectrometry. Clin Proteomics. 2016 Feb 25;13:4. doi: 10.1186/s12014-016-9104-2. eCollection 2016. PMID: 26924951; PMCID: PMC4768413.
Copy Download .nbib Format: NLM
DBAASP v.2: an enhanced database of structure and antimicrobial/cytotoxic activity of natural and synthetic peptides.

Nucleic acids research

Pirtskhalava M, Gabrielian A, Cruz P, Griggs HL, Squires RB, Hurt DE, Grigolava M, Chubinidze M, Gogoladze G, Vishnepolsky B, Alekseyev V, Rosenthal A, Tartakovsky M.
PMID: 27060142
Nucleic Acids Res. 2016 Jul 27;44(13):6503. doi: 10.1093/nar/gkw243. Epub 2016 Apr 08.

No abstract available.

Cite
Pirtskhalava M, Gabrielian A, Cruz P, et al. DBAASP v.2: an enhanced database of structure and antimicrobial/cytotoxic activity of natural and synthetic peptides. Nucleic Acids Res. 2016;44(13):6503doi: 10.1093/nar/gkw243.
Pirtskhalava, M., Gabrielian, A., Cruz, P., Griggs, H. L., Squires, R. B., Hurt, D. E., Grigolava, M., Chubinidze, M., Gogoladze, G., Vishnepolsky, B., Alekseyev, V., Rosenthal, A., & Tartakovsky, M. (2016). DBAASP v.2: an enhanced database of structure and antimicrobial/cytotoxic activity of natural and synthetic peptides. Nucleic acids research, 44(13), 6503. https://doi.org/10.1093/nar/gkw243
Pirtskhalava, Malak, et al. "DBAASP v.2: an enhanced database of structure and antimicrobial/cytotoxic activity of natural and synthetic peptides." Nucleic acids research vol. 44,13 (2016): 6503. doi: https://doi.org/10.1093/nar/gkw243
Pirtskhalava M, Gabrielian A, Cruz P, Griggs HL, Squires RB, Hurt DE, Grigolava M, Chubinidze M, Gogoladze G, Vishnepolsky B, Alekseyev V, Rosenthal A, Tartakovsky M. DBAASP v.2: an enhanced database of structure and antimicrobial/cytotoxic activity of natural and synthetic peptides. Nucleic Acids Res. 2016 Jul 27;44(13):6503. doi: 10.1093/nar/gkw243. Epub 2016 Apr 08. PMID: 27060142; PMCID: PMC4994862.
Copy Download .nbib Format: NLM
Classification of self-assembling protein nanoparticle architectures for applications in vaccine design.

Royal Society open science

Indelicato G, Burkhard P, Twarock R.
PMID: 28484626
R Soc Open Sci. 2017 Apr 26;4(4):161092. doi: 10.1098/rsos.161092. eCollection 2017 Apr.

We introduce here a mathematical procedure for the structural classification of a specific class of self-assembling protein nanoparticles (SAPNs) that are used as a platform for repetitive antigen display systems. These SAPNs have distinctive geometries as a consequence of...

Cite
Indelicato G, Burkhard P, Twarock R. Classification of self-assembling protein nanoparticle architectures for applications in vaccine design. R Soc Open Sci. 2017;4(4):161092doi: 10.1098/rsos.161092.
Indelicato, G., Burkhard, P., & Twarock, R. (2017). Classification of self-assembling protein nanoparticle architectures for applications in vaccine design. Royal Society open science, 4(4), 161092. https://doi.org/10.1098/rsos.161092
Indelicato, G, et al. "Classification of self-assembling protein nanoparticle architectures for applications in vaccine design." Royal Society open science vol. 4,4 (2017): 161092. doi: https://doi.org/10.1098/rsos.161092
Indelicato G, Burkhard P, Twarock R. Classification of self-assembling protein nanoparticle architectures for applications in vaccine design. R Soc Open Sci. 2017 Apr 26;4(4):161092. doi: 10.1098/rsos.161092. eCollection 2017 Apr. PMID: 28484626; PMCID: PMC5414263.
Copy Download .nbib Format: NLM
Nematode Peptides with Host-Directed Anti-inflammatory Activity Rescue Caenorhabditis elegans from a Burkholderia pseudomallei Infection.

Frontiers in microbiology

Lim MP, Firdaus-Raih M, Nathan S.
PMID: 27672387
Front Microbiol. 2016 Sep 12;7:1436. doi: 10.3389/fmicb.2016.01436. eCollection 2016.

Burkholderia pseudomallei, the causative agent of melioidosis, is among a growing number of bacterial pathogens that are increasingly antibiotic resistant. Antimicrobial peptides (AMPs) have been investigated as an alternative approach to treat microbial infections, as generally, there is a...

Cite
Lim MP, Firdaus-Raih M, Nathan S. Nematode Peptides with Host-Directed Anti-inflammatory Activity Rescue Caenorhabditis elegans from a Burkholderia pseudomallei Infection. Front Microbiol. 2016;7:1436doi: 10.3389/fmicb.2016.01436.
Lim, M. P., Firdaus-Raih, M., & Nathan, S. (2016). Nematode Peptides with Host-Directed Anti-inflammatory Activity Rescue Caenorhabditis elegans from a Burkholderia pseudomallei Infection. Frontiers in microbiology, 71436. https://doi.org/10.3389/fmicb.2016.01436
Lim, Mei-Perng, et al. "Nematode Peptides with Host-Directed Anti-inflammatory Activity Rescue Caenorhabditis elegans from a Burkholderia pseudomallei Infection." Frontiers in microbiology vol. 7 (2016): 1436. doi: https://doi.org/10.3389/fmicb.2016.01436
Lim MP, Firdaus-Raih M, Nathan S. Nematode Peptides with Host-Directed Anti-inflammatory Activity Rescue Caenorhabditis elegans from a Burkholderia pseudomallei Infection. Front Microbiol. 2016 Sep 12;7:1436. doi: 10.3389/fmicb.2016.01436. eCollection 2016. PMID: 27672387; PMCID: PMC5019075.
Copy Download .nbib Format: NLM
Pharmacokinetics and pharmacodynamics of subcutaneously administered PYY3-36 and its analogues in vivo.

Lancet (London, England)

Cegla J, Cuenco J, Minnion J, Ghourab S, Hostomska K, Tan T, Bloom S.
PMID: 26312850
Lancet. 2015 Feb 26;385:S28. doi: 10.1016/S0140-6736(15)60343-9.

BACKGROUND: Obesity is an emergent epidemic associated with morbidity, mortality, and psychosocial effects. One of the key gut hormones that controls appetite is peptide tyrosine-tyrosine 3-36 (PYY3-36) whose circulating half-life is only 8 min. A long-acting analogue of PYY3-36...

Cite
Cegla J, Cuenco J, Minnion J, et al. Pharmacokinetics and pharmacodynamics of subcutaneously administered PYY3-36 and its analogues in vivo. Lancet. 2015;385:S28doi: 10.1016/S0140-6736(15)60343-9.
Cegla, J., Cuenco, J., Minnion, J., Ghourab, S., Hostomska, K., Tan, T., & Bloom, S. (2015). Pharmacokinetics and pharmacodynamics of subcutaneously administered PYY3-36 and its analogues in vivo. Lancet (London, England), 385S28. https://doi.org/10.1016/S0140-6736(15)60343-9
Cegla, Jaimini, et al. "Pharmacokinetics and pharmacodynamics of subcutaneously administered PYY3-36 and its analogues in vivo." Lancet (London, England) vol. 385 (2015): S28. doi: https://doi.org/10.1016/S0140-6736(15)60343-9
Cegla J, Cuenco J, Minnion J, Ghourab S, Hostomska K, Tan T, Bloom S. Pharmacokinetics and pharmacodynamics of subcutaneously administered PYY3-36 and its analogues in vivo. Lancet. 2015 Feb 26;385:S28. doi: 10.1016/S0140-6736(15)60343-9. PMID: 26312850.
Copy Download .nbib Format: NLM
Inhibition of complement C3 and fibrinogen interaction: a potential novel therapeutic target to reduce cardiovascular disease in diabetes.

Lancet (London, England)

King R, Tiede C, Simmons K, Fishwick C, Tomlinson D, Ajjan R.
PMID: 26312879
Lancet. 2015 Feb 26;385:S57. doi: 10.1016/S0140-6736(15)60372-5.

BACKGROUND: Enhanced complement C3 incorporation into the fibrin network in diabetes is one mechanism for impaired fibrinolysis and increased thrombosis risk in this condition. Our aim was to develop new strategies to modulate fibrinolysis in diabetes by interfering with...

Cite
King R, Tiede C, Simmons K, et al. Inhibition of complement C3 and fibrinogen interaction: a potential novel therapeutic target to reduce cardiovascular disease in diabetes. Lancet. 2015;385:S57doi: 10.1016/S0140-6736(15)60372-5.
King, R., Tiede, C., Simmons, K., Fishwick, C., Tomlinson, D., & Ajjan, R. (2015). Inhibition of complement C3 and fibrinogen interaction: a potential novel therapeutic target to reduce cardiovascular disease in diabetes. Lancet (London, England), 385S57. https://doi.org/10.1016/S0140-6736(15)60372-5
King, Rhodri, et al. "Inhibition of complement C3 and fibrinogen interaction: a potential novel therapeutic target to reduce cardiovascular disease in diabetes." Lancet (London, England) vol. 385 (2015): S57. doi: https://doi.org/10.1016/S0140-6736(15)60372-5
King R, Tiede C, Simmons K, Fishwick C, Tomlinson D, Ajjan R. Inhibition of complement C3 and fibrinogen interaction: a potential novel therapeutic target to reduce cardiovascular disease in diabetes. Lancet. 2015 Feb 26;385:S57. doi: 10.1016/S0140-6736(15)60372-5. PMID: 26312879.
Copy Download .nbib Format: NLM
Hierarchical Analysis of Self-Assembled PEGylated Hexaphenylalanine Photoluminescent Nanostructures.

Chemistry (Weinheim an der Bergstrasse, Germany)

Diaferia C, Sibillano T, Balasco N, Giannini C, Roviello V, Vitagliano L, Morelli G, Accardo A.
PMID: 27706842
Chemistry. 2016 Nov 07;22(46):16586-16597. doi: 10.1002/chem.201604107. Epub 2016 Oct 05.

Despite the growing literature about diphenylalanine-based peptide materials, it still remains a challenge to delineate the theoretical insight into peptide nanostructure formation and the structural features that could permit materials with enhanced properties to be engineered. Herein, we report...

Cite
Diaferia C, Sibillano T, Balasco N, et al. Hierarchical Analysis of Self-Assembled PEGylated Hexaphenylalanine Photoluminescent Nanostructures. Chemistry. 2016;22(46):16586-16597doi: 10.1002/chem.201604107.
Diaferia, C., Sibillano, T., Balasco, N., Giannini, C., Roviello, V., Vitagliano, L., Morelli, G., & Accardo, A. (2016). Hierarchical Analysis of Self-Assembled PEGylated Hexaphenylalanine Photoluminescent Nanostructures. Chemistry (Weinheim an der Bergstrasse, Germany), 22(46), 16586-16597. https://doi.org/10.1002/chem.201604107
Diaferia, Carlo, et al. "Hierarchical Analysis of Self-Assembled PEGylated Hexaphenylalanine Photoluminescent Nanostructures." Chemistry (Weinheim an der Bergstrasse, Germany) vol. 22,46 (2016): 16586-16597. doi: https://doi.org/10.1002/chem.201604107
Diaferia C, Sibillano T, Balasco N, Giannini C, Roviello V, Vitagliano L, Morelli G, Accardo A. Hierarchical Analysis of Self-Assembled PEGylated Hexaphenylalanine Photoluminescent Nanostructures. Chemistry. 2016 Nov 07;22(46):16586-16597. doi: 10.1002/chem.201604107. Epub 2016 Oct 05. PMID: 27706842.
Copy Download .nbib Format: NLM
Design, Synthesis, and Application of an Optimized Monofluorinated Aliphatic Label for Peptide Studies by Solid-State .

Angewandte Chemie (International ed. in English)

Kokhan SO, Tymtsunik AV, Grage SL, Afonin S, Babii O, Berditsch M, Strizhak AV, Bandak D, Platonov MO, Komarov IV, Ulrich AS, Mykhailiuk PK.
PMID: 27706889
Angew Chem Int Ed Engl. 2016 Nov 14;55(47):14788-14792. doi: 10.1002/anie.201608116. Epub 2016 Oct 05.

A conformationally restricted monofluorinated α-amino acid, (3-fluorobicyclo[1.1.1]pentyl)glycine (F-Bpg), was designed as a label for the structural analysis of membrane-bound peptides by solid-state

Cite
Kokhan SO, Tymtsunik AV, Grage SL, et al. Design, Synthesis, and Application of an Optimized Monofluorinated Aliphatic Label for Peptide Studies by Solid-State . Angew Chem Int Ed Engl. 2016;55(47):14788-14792doi: 10.1002/anie.201608116.
Kokhan, S. O., Tymtsunik, A. V., Grage, S. L., Afonin, S., Babii, O., Berditsch, M., Strizhak, A. V., Bandak, D., Platonov, M. O., Komarov, I. V., Ulrich, A. S., & Mykhailiuk, P. K. (2016). Design, Synthesis, and Application of an Optimized Monofluorinated Aliphatic Label for Peptide Studies by Solid-State . Angewandte Chemie (International ed. in English), 55(47), 14788-14792. https://doi.org/10.1002/anie.201608116
Kokhan, Serhii O, et al. "Design, Synthesis, and Application of an Optimized Monofluorinated Aliphatic Label for Peptide Studies by Solid-State ." Angewandte Chemie (International ed. in English) vol. 55,47 (2016): 14788-14792. doi: https://doi.org/10.1002/anie.201608116
Kokhan SO, Tymtsunik AV, Grage SL, Afonin S, Babii O, Berditsch M, Strizhak AV, Bandak D, Platonov MO, Komarov IV, Ulrich AS, Mykhailiuk PK. Design, Synthesis, and Application of an Optimized Monofluorinated Aliphatic Label for Peptide Studies by Solid-State . Angew Chem Int Ed Engl. 2016 Nov 14;55(47):14788-14792. doi: 10.1002/anie.201608116. Epub 2016 Oct 05. PMID: 27706889.
Copy Download .nbib Format: NLM
Towards the development of an enzyme replacement therapy for the metabolic disorder propionic acidemia.

Molecular genetics and metabolism reports

Darvish-Damavandi M, Ho HK, Kang TS.
PMID: 27504265
Mol Genet Metab Rep. 2016 Jul 27;8:51-60. doi: 10.1016/j.ymgmr.2016.06.009. eCollection 2016 Sep.

Propionic acidemia (PA) is a life-threatening disease caused by the deficiency of a mitochondrial biotin-dependent enzyme known as propionyl coenzyme-A carboxylase (PCC). This enzyme is responsible for degrading the metabolic intermediate, propionyl coenzyme-A (PP-CoA), derived from multiple metabolic pathways....

Cite
Darvish-Damavandi M, Ho HK, Kang TS. Towards the development of an enzyme replacement therapy for the metabolic disorder propionic acidemia. Mol Genet Metab Rep. 2016;8:51-60doi: 10.1016/j.ymgmr.2016.06.009.
Darvish-Damavandi, M., Ho, H. K., & Kang, T. S. (2016). Towards the development of an enzyme replacement therapy for the metabolic disorder propionic acidemia. Molecular genetics and metabolism reports, 851-60. https://doi.org/10.1016/j.ymgmr.2016.06.009
Darvish-Damavandi, Mahnaz, et al. "Towards the development of an enzyme replacement therapy for the metabolic disorder propionic acidemia." Molecular genetics and metabolism reports vol. 8 (2016): 51-60. doi: https://doi.org/10.1016/j.ymgmr.2016.06.009
Darvish-Damavandi M, Ho HK, Kang TS. Towards the development of an enzyme replacement therapy for the metabolic disorder propionic acidemia. Mol Genet Metab Rep. 2016 Jul 27;8:51-60. doi: 10.1016/j.ymgmr.2016.06.009. eCollection 2016 Sep. PMID: 27504265; PMCID: PMC4968140.
Copy Download .nbib Format: NLM
Proteinases, Their Extracellular Targets, and Inflammatory Signaling.

Pharmacological reviews

Ramachandran R, Altier C, Oikonomopoulou K, Hollenberg MD.
PMID: 27677721
Pharmacol Rev. 2016 Oct;68(4):1110-1142. doi: 10.1124/pr.115.010991.

Given that over 2% of the human genome codes for proteolytic enzymes and their inhibitors, it is not surprising that proteinases serve many physiologic-pathophysiological roles. In this context, we provide an overview of proteolytic mechanisms regulating inflammation, with a...

Cite
Ramachandran R, Altier C, Oikonomopoulou K, et al. Proteinases, Their Extracellular Targets, and Inflammatory Signaling. Pharmacol Rev. 2016;68(4):1110-1142doi: 10.1124/pr.115.010991.
Ramachandran, R., Altier, C., Oikonomopoulou, K., & Hollenberg, M. D. (2016). Proteinases, Their Extracellular Targets, and Inflammatory Signaling. Pharmacological reviews, 68(4), 1110-1142. https://doi.org/10.1124/pr.115.010991
Ramachandran, Rithwik, et al. "Proteinases, Their Extracellular Targets, and Inflammatory Signaling." Pharmacological reviews vol. 68,4 (2016): 1110-1142. doi: https://doi.org/10.1124/pr.115.010991
Ramachandran R, Altier C, Oikonomopoulou K, Hollenberg MD. Proteinases, Their Extracellular Targets, and Inflammatory Signaling. Pharmacol Rev. 2016 Oct;68(4):1110-1142. doi: 10.1124/pr.115.010991. PMID: 27677721.
Copy Download .nbib Format: NLM
Preparation of phenyl-functionalized magnetic mesoporous silica microspheres for the fast separation and selective enrichment of phenyl-containing peptides.

Journal of separation science

Li S, Wang L, Zhao S, Lin J, Zheng J, Lin Z.
PMID: 26377040
J Sep Sci. 2015 Nov;38(22):3954-3960. doi: 10.1002/jssc.201500876. Epub 2015 Oct 14.

Peptide enrichment before mass spectrometry analysis is essential for large-scale peptidomic studies, but challenges still remain. Herein, magnetic mesoporous silica microspheres with phenyl group modified interior pore walls were prepared by a facile sol-gel coating strategy, and were successfully...

Cite
Li S, Wang L, Zhao S, et al. Preparation of phenyl-functionalized magnetic mesoporous silica microspheres for the fast separation and selective enrichment of phenyl-containing peptides. J Sep Sci. 2015;38(22):3954-3960doi: 10.1002/jssc.201500876.
Li, S., Wang, L., Zhao, S., Lin, J., Zheng, J., & Lin, Z. (2015). Preparation of phenyl-functionalized magnetic mesoporous silica microspheres for the fast separation and selective enrichment of phenyl-containing peptides. Journal of separation science, 38(22), 3954-3960. https://doi.org/10.1002/jssc.201500876
Li, Shihua, et al. "Preparation of phenyl-functionalized magnetic mesoporous silica microspheres for the fast separation and selective enrichment of phenyl-containing peptides." Journal of separation science vol. 38,22 (2015): 3954-3960. doi: https://doi.org/10.1002/jssc.201500876
Li S, Wang L, Zhao S, Lin J, Zheng J, Lin Z. Preparation of phenyl-functionalized magnetic mesoporous silica microspheres for the fast separation and selective enrichment of phenyl-containing peptides. J Sep Sci. 2015 Nov;38(22):3954-3960. doi: 10.1002/jssc.201500876. Epub 2015 Oct 14. PMID: 26377040.
Copy Download .nbib Format: NLM
Showing 25 to 36 of 20335 entries