Advanced Search
Display options
Filter resources
Text Availability
Article type
Publication date
Species
Language
Sex
Age
Showing 1 to 12 of 223 entries
Sorted by: Best Match Show Resources per page
Anti-infectious and anti-inflammatory effects of peptide fragments sequentially derived from the antimicrobial peptide centrocin 1 isolated from the green sea urchin, Strongylocentrotus droebachiensis.

AMB Express

Björn C, Håkansson J, Myhrman E, Sjöstrand V, Haug T, Lindgren K, Blencke HM, Stensvåg K, Mahlapuu M.
PMID: 23237525
AMB Express. 2012 Dec 13;2(1):67. doi: 10.1186/2191-0855-2-67.

Bacterial resistance against antibiotic treatment has become a major threat to public health. Antimicrobial peptides (AMPs) have emerged as promising alternative agents for treatment of infectious diseases. This study characterizes novel synthetic peptides sequentially derived from the AMP centrocin...

Cite
Björn C, Håkansson J, Myhrman E, et al. Anti-infectious and anti-inflammatory effects of peptide fragments sequentially derived from the antimicrobial peptide centrocin 1 isolated from the green sea urchin, Strongylocentrotus droebachiensis. AMB Express. 2012;2(1):67doi: 10.1186/2191-0855-2-67.
Björn, C., Håkansson, J., Myhrman, E., Sjöstrand, V., Haug, T., Lindgren, K., Blencke, H. M., Stensvåg, K., & Mahlapuu, M. (2012). Anti-infectious and anti-inflammatory effects of peptide fragments sequentially derived from the antimicrobial peptide centrocin 1 isolated from the green sea urchin, Strongylocentrotus droebachiensis. AMB Express, 2(1), 67. https://doi.org/10.1186/2191-0855-2-67
Björn, Camilla, et al. "Anti-infectious and anti-inflammatory effects of peptide fragments sequentially derived from the antimicrobial peptide centrocin 1 isolated from the green sea urchin, Strongylocentrotus droebachiensis." AMB Express vol. 2,1 (2012): 67. doi: https://doi.org/10.1186/2191-0855-2-67
Björn C, Håkansson J, Myhrman E, Sjöstrand V, Haug T, Lindgren K, Blencke HM, Stensvåg K, Mahlapuu M. Anti-infectious and anti-inflammatory effects of peptide fragments sequentially derived from the antimicrobial peptide centrocin 1 isolated from the green sea urchin, Strongylocentrotus droebachiensis. AMB Express. 2012 Dec 13;2(1):67. doi: 10.1186/2191-0855-2-67. PMID: 23237525; PMCID: PMC3561256.
Copy Download .nbib Format: NLM
Biliverdin reductase: more than a namesake - the reductase, its Peptide fragments, and biliverdin regulate activity of the three classes of protein kinase C.

Frontiers in pharmacology

Gibbs PE, Tudor C, Maines MD.
PMID: 22419908
Front Pharmacol. 2012 Mar 13;3:31. doi: 10.3389/fphar.2012.00031. eCollection 2012.

The expanse of human biliverdin reductase (hBVR) functions in the cells is arguably unmatched by any single protein. hBVR is a Ser/Thr/Tyr-kinase, a scaffold protein, a transcription factor, and an intracellular transporter of gene regulators. hBVR is an upstream...

Cite
Gibbs PE, Tudor C, Maines MD. Biliverdin reductase: more than a namesake - the reductase, its Peptide fragments, and biliverdin regulate activity of the three classes of protein kinase C. Front Pharmacol. 2012;3:31doi: 10.3389/fphar.2012.00031.
Gibbs, P. E., Tudor, C., & Maines, M. D. (2012). Biliverdin reductase: more than a namesake - the reductase, its Peptide fragments, and biliverdin regulate activity of the three classes of protein kinase C. Frontiers in pharmacology, 331. https://doi.org/10.3389/fphar.2012.00031
Gibbs, Peter E M, et al. "Biliverdin reductase: more than a namesake - the reductase, its Peptide fragments, and biliverdin regulate activity of the three classes of protein kinase C." Frontiers in pharmacology vol. 3 (2012): 31. doi: https://doi.org/10.3389/fphar.2012.00031
Gibbs PE, Tudor C, Maines MD. Biliverdin reductase: more than a namesake - the reductase, its Peptide fragments, and biliverdin regulate activity of the three classes of protein kinase C. Front Pharmacol. 2012 Mar 13;3:31. doi: 10.3389/fphar.2012.00031. eCollection 2012. PMID: 22419908; PMCID: PMC3299957.
Copy Download .nbib Format: NLM
Proteolytic degradation patterns of the receptor for advanced glycation end products peptide fragments correlate with their neuroprotective activity in Alzheimer's disease models.

Drug development research

Volpina OM, Koroev DO, Serebryakova MV, Volkova TD, Kamynina AV, Bobkova NV.
PMID: 34060112
Drug Dev Res. 2021 Dec;82(8):1217-1226. doi: 10.1002/ddr.21836. Epub 2021 May 31.

The receptor for advanced glycation end products (RAGE) plays an essential role in Alzheimer's disease (AD). We previously demonstrated that a fragment (60-76) of RAGE improved the memory of olfactory bulbectomized (OBX) and Tg 5 × FAD mice -...

Cite
Volpina OM, Koroev DO, Serebryakova MV, et al. Proteolytic degradation patterns of the receptor for advanced glycation end products peptide fragments correlate with their neuroprotective activity in Alzheimer's disease models. Drug Dev Res. 2021;82(8):1217-1226doi: 10.1002/ddr.21836.
Volpina, O. M., Koroev, D. O., Serebryakova, M. V., Volkova, T. D., Kamynina, A. V., & Bobkova, N. V. (2021). Proteolytic degradation patterns of the receptor for advanced glycation end products peptide fragments correlate with their neuroprotective activity in Alzheimer's disease models. Drug development research, 82(8), 1217-1226. https://doi.org/10.1002/ddr.21836
Volpina, Olga M, et al. "Proteolytic degradation patterns of the receptor for advanced glycation end products peptide fragments correlate with their neuroprotective activity in Alzheimer's disease models." Drug development research vol. 82,8 (2021): 1217-1226. doi: https://doi.org/10.1002/ddr.21836
Volpina OM, Koroev DO, Serebryakova MV, Volkova TD, Kamynina AV, Bobkova NV. Proteolytic degradation patterns of the receptor for advanced glycation end products peptide fragments correlate with their neuroprotective activity in Alzheimer's disease models. Drug Dev Res. 2021 Dec;82(8):1217-1226. doi: 10.1002/ddr.21836. Epub 2021 May 31. PMID: 34060112.
Copy Download .nbib Format: NLM
Native CGRP Neuropeptide and Its Stable Analogue SAX, But Not CGRP Peptide Fragments, Inhibit Mucosal HIV-1 Transmission.

Frontiers in immunology

Mariotton J, Sams A, Cohen E, Sennepin A, Siracusano G, Sanvito F, Edvinsson L, Delongchamps NB, Zerbib M, Lopalco L, Bomsel M, Ganor Y.
PMID: 34956215
Front Immunol. 2021 Dec 08;12:785072. doi: 10.3389/fimmu.2021.785072. eCollection 2021.

BACKGROUND: The vasodilator neuropeptide calcitonin gene-related peptide (CGRP) plays both detrimental and protective roles in different pathologies. CGRP is also an essential component of the neuro-immune dialogue between nociceptors and mucosal immune cells. We previously discovered that CGRP is...

Cite
Mariotton J, Sams A, Cohen E, et al. Native CGRP Neuropeptide and Its Stable Analogue SAX, But Not CGRP Peptide Fragments, Inhibit Mucosal HIV-1 Transmission. Front Immunol. 2021;12:785072doi: 10.3389/fimmu.2021.785072.
Mariotton, J., Sams, A., Cohen, E., Sennepin, A., Siracusano, G., Sanvito, F., Edvinsson, L., Delongchamps, N. B., Zerbib, M., Lopalco, L., Bomsel, M., & Ganor, Y. (2021). Native CGRP Neuropeptide and Its Stable Analogue SAX, But Not CGRP Peptide Fragments, Inhibit Mucosal HIV-1 Transmission. Frontiers in immunology, 12785072. https://doi.org/10.3389/fimmu.2021.785072
Mariotton, Jammy, et al. "Native CGRP Neuropeptide and Its Stable Analogue SAX, But Not CGRP Peptide Fragments, Inhibit Mucosal HIV-1 Transmission." Frontiers in immunology vol. 12 (2021): 785072. doi: https://doi.org/10.3389/fimmu.2021.785072
Mariotton J, Sams A, Cohen E, Sennepin A, Siracusano G, Sanvito F, Edvinsson L, Delongchamps NB, Zerbib M, Lopalco L, Bomsel M, Ganor Y. Native CGRP Neuropeptide and Its Stable Analogue SAX, But Not CGRP Peptide Fragments, Inhibit Mucosal HIV-1 Transmission. Front Immunol. 2021 Dec 08;12:785072. doi: 10.3389/fimmu.2021.785072. eCollection 2021. PMID: 34956215; PMCID: PMC8692891.
Copy Download .nbib Format: NLM
Enzymatic condensation of cholecystokinin CCK-8 (4-6) and CCK-8 (7-8) peptide fragments in organic media.

Biotechnology and bioengineering

Capellas M, Caminal G, Gonzalez G, López-Santín J, Clapés P.
PMID: 18642248
Biotechnol Bioeng. 1997 Nov 20;56(4):456-63. doi: 10.1002/(SICI)1097-0290(19971120)56:4<456::AID-BIT11>3.0.CO;2-A.

The kinetically controlled condensation reaction of Z-Gly-Trp-Met-OR(1) (R(1): Et, Al, Cam) and H-Asp-(OR(2))-Phe-NH(2) (R(2): H, Bu(t)) catalyzed by alpha-chymotrypsin deposited onto polyamide in organic media was studied. The effect of the drying process of the enzyme-support preparation, substrate concentrations,...

Cite
Capellas M, Caminal G, Gonzalez G, et al. Enzymatic condensation of cholecystokinin CCK-8 (4-6) and CCK-8 (7-8) peptide fragments in organic media. Biotechnol Bioeng. 1997;56(4):456-63doi: 10.1002/(SICI)1097-0290(19971120)56:4<456::AID-BIT11>3.0.CO;2-A.
Capellas, M., Caminal, G., Gonzalez, G., López-Santín, J., & Clapés, P. (1997). Enzymatic condensation of cholecystokinin CCK-8 (4-6) and CCK-8 (7-8) peptide fragments in organic media. Biotechnology and bioengineering, 56(4), 456-63. https://doi.org/10.1002/(SICI)1097-0290(19971120)56:4<456::AID-BIT11>3.0.CO;2-A
Capellas, M, et al. "Enzymatic condensation of cholecystokinin CCK-8 (4-6) and CCK-8 (7-8) peptide fragments in organic media." Biotechnology and bioengineering vol. 56,4 (1997): 456-63. doi: https://doi.org/10.1002/(SICI)1097-0290(19971120)56:4<456::AID-BIT11>3.0.CO;2-A
Capellas M, Caminal G, Gonzalez G, López-Santín J, Clapés P. Enzymatic condensation of cholecystokinin CCK-8 (4-6) and CCK-8 (7-8) peptide fragments in organic media. Biotechnol Bioeng. 1997 Nov 20;56(4):456-63. doi: 10.1002/(SICI)1097-0290(19971120)56:4<456::AID-BIT11>3.0.CO;2-A. PMID: 18642248.
Copy Download .nbib Format: NLM
Responses of Cultured Astrocytes, C6 Glioma and 1321NI Astrocytoma Cells to Amyloid beta-Peptide Fragments.

Nonlinearity in biology, toxicology, medicine

Pentreath VW, Mead C.
PMID: 19330108
Nonlinearity Biol Toxicol Med. 2004 Jan;2(1):45-63. doi: 10.1080/15401420490426990.

The effect of amyloid beta-peptide (betaAP), which can have both neurotrophic or neurotoxic effects on neurons and has been implicated in the pathogenesis of Alzheimer's disease (AD), was studied on astrocytes using primary cultures and astrocyte cell lines (rat...

Cite
Pentreath VW, Mead C. Responses of Cultured Astrocytes, C6 Glioma and 1321NI Astrocytoma Cells to Amyloid beta-Peptide Fragments. Nonlinearity Biol Toxicol Med. 2004;2(1):45-63doi: 10.1080/15401420490426990.
Pentreath, V. W., & Mead, C. (2004). Responses of Cultured Astrocytes, C6 Glioma and 1321NI Astrocytoma Cells to Amyloid beta-Peptide Fragments. Nonlinearity in biology, toxicology, medicine, 2(1), 45-63. https://doi.org/10.1080/15401420490426990
Pentreath, V W, and Mead, C. "Responses of Cultured Astrocytes, C6 Glioma and 1321NI Astrocytoma Cells to Amyloid beta-Peptide Fragments." Nonlinearity in biology, toxicology, medicine vol. 2,1 (2004): 45-63. doi: https://doi.org/10.1080/15401420490426990
Pentreath VW, Mead C. Responses of Cultured Astrocytes, C6 Glioma and 1321NI Astrocytoma Cells to Amyloid beta-Peptide Fragments. Nonlinearity Biol Toxicol Med. 2004 Jan;2(1):45-63. doi: 10.1080/15401420490426990. PMID: 19330108; PMCID: PMC2647817.
Copy Download .nbib Format: NLM
Phytochrome structure: Peptide fragments from the amino-terminal domain involved in protein-chromophore interactions.

Planta

Jones AM, Quail PH.
PMID: 24212743
Planta. 1989 May;178(2):147-56. doi: 10.1007/BF00393189.

We have undertaken a study of the structure of the amino-terminal domain of the phytochrome polypeptide purified from Avena sativa L. Amino-acid sequencing was used to indentify arginine 52 as the precise location of a conformation-specific cleavage of phytochrome...

Cite
Jones AM, Quail PH. Phytochrome structure: Peptide fragments from the amino-terminal domain involved in protein-chromophore interactions. Planta. 1989;178(2):147-56doi: 10.1007/BF00393189.
Jones, A. M., & Quail, P. H. (1989). Phytochrome structure: Peptide fragments from the amino-terminal domain involved in protein-chromophore interactions. Planta, 178(2), 147-56. https://doi.org/10.1007/BF00393189
Jones, A M, and Quail, P H. "Phytochrome structure: Peptide fragments from the amino-terminal domain involved in protein-chromophore interactions." Planta vol. 178,2 (1989): 147-56. doi: https://doi.org/10.1007/BF00393189
Jones AM, Quail PH. Phytochrome structure: Peptide fragments from the amino-terminal domain involved in protein-chromophore interactions. Planta. 1989 May;178(2):147-56. doi: 10.1007/BF00393189. PMID: 24212743.
Copy Download .nbib Format: NLM
Antimicrobial Peptide Designing and Optimization Employing Large-Scale Flexibility Analysis of Protein-Peptide Fragments.

ACS omega

Kumar N, Sood D, Tomar R, Chandra R.
PMID: 31867532
ACS Omega. 2019 Dec 03;4(25):21370-21380. doi: 10.1021/acsomega.9b03035. eCollection 2019 Dec 17.

The mankind relies on the use of antibiotics for a healthy life. The epidemic-like emergence of drug-resistant bacterial strains is increasingly becoming one of the leading causes of morbidity and mortality, which gives rise to design a potential antimicrobial...

Cite
Kumar N, Sood D, Tomar R, et al. Antimicrobial Peptide Designing and Optimization Employing Large-Scale Flexibility Analysis of Protein-Peptide Fragments. ACS Omega. 2019;4(25):21370-21380doi: 10.1021/acsomega.9b03035.
Kumar, N., Sood, D., Tomar, R., & Chandra, R. (2019). Antimicrobial Peptide Designing and Optimization Employing Large-Scale Flexibility Analysis of Protein-Peptide Fragments. ACS omega, 4(25), 21370-21380. https://doi.org/10.1021/acsomega.9b03035
Kumar, Neeraj, et al. "Antimicrobial Peptide Designing and Optimization Employing Large-Scale Flexibility Analysis of Protein-Peptide Fragments." ACS omega vol. 4,25 (2019): 21370-21380. doi: https://doi.org/10.1021/acsomega.9b03035
Kumar N, Sood D, Tomar R, Chandra R. Antimicrobial Peptide Designing and Optimization Employing Large-Scale Flexibility Analysis of Protein-Peptide Fragments. ACS Omega. 2019 Dec 03;4(25):21370-21380. doi: 10.1021/acsomega.9b03035. eCollection 2019 Dec 17. PMID: 31867532; PMCID: PMC6921640.
Copy Download .nbib Format: NLM
Peptide fragments released from the collagen molecule by pronase.

FEBS letters

Deyl Z, Rosmus J, Adam M.
PMID: 11945570
FEBS Lett. 1971 Jan 12;12(3):176-178. doi: 10.1016/0014-5793(71)80062-5.

No abstract available.

Cite
Deyl Z, Rosmus J, Adam M. Peptide fragments released from the collagen molecule by pronase. FEBS Lett. 1971;12(3):176-178doi: 10.1016/0014-5793(71)80062-5.
Deyl, Z., Rosmus, J., & Adam, M. (1971). Peptide fragments released from the collagen molecule by pronase. FEBS letters, 12(3), 176-178. https://doi.org/10.1016/0014-5793(71)80062-5
Deyl, Z, et al. "Peptide fragments released from the collagen molecule by pronase." FEBS letters vol. 12,3 (1971): 176-178. doi: https://doi.org/10.1016/0014-5793(71)80062-5
Deyl Z, Rosmus J, Adam M. Peptide fragments released from the collagen molecule by pronase. FEBS Lett. 1971 Jan 12;12(3):176-178. doi: 10.1016/0014-5793(71)80062-5. PMID: 11945570.
Copy Download .nbib Format: NLM
Exploring amyloid oligomers with peptide model systems.

Current opinion in chemical biology

Samdin TD, Kreutzer AG, Nowick JS.
PMID: 34229162
Curr Opin Chem Biol. 2021 Oct;64:106-115. doi: 10.1016/j.cbpa.2021.05.004. Epub 2021 Jul 03.

The assembly of amyloidogenic peptides and proteins, such as the β-amyloid peptide, α-synuclein, huntingtin, tau, and islet amyloid polypeptide, into amyloid fibrils and oligomers is directly linked to amyloid diseases, such as Alzheimer's, Parkinson's, and Huntington's diseases, frontotemporal dementias,...

Cite
Samdin TD, Kreutzer AG, Nowick JS. Exploring amyloid oligomers with peptide model systems. Curr Opin Chem Biol. 2021;64:106-115doi: 10.1016/j.cbpa.2021.05.004.
Samdin, T. D., Kreutzer, A. G., & Nowick, J. S. (2021). Exploring amyloid oligomers with peptide model systems. Current opinion in chemical biology, 64106-115. https://doi.org/10.1016/j.cbpa.2021.05.004
Samdin, Tuan D, et al. "Exploring amyloid oligomers with peptide model systems." Current opinion in chemical biology vol. 64 (2021): 106-115. doi: https://doi.org/10.1016/j.cbpa.2021.05.004
Samdin TD, Kreutzer AG, Nowick JS. Exploring amyloid oligomers with peptide model systems. Curr Opin Chem Biol. 2021 Oct;64:106-115. doi: 10.1016/j.cbpa.2021.05.004. Epub 2021 Jul 03. PMID: 34229162.
Copy Download .nbib Format: NLM
Peptide Extracts from Seven Medicinal Plants Discovered to Inhibit Oomycete .

Plants (Basel, Switzerland)

Rogozhin EA, Vasilchenko AS, Barashkova AS, Smirnov AN, Zavriev SK, Demushkin VP.
PMID: 33007947
Plants (Basel). 2020 Sep 30;9(10). doi: 10.3390/plants9101294.

We report the inhibitory effect of peptide extracts obtained from seven medicinal plants against a causative agent of late blight disease

Cite
Rogozhin EA, Vasilchenko AS, Barashkova AS, et al. Peptide Extracts from Seven Medicinal Plants Discovered to Inhibit Oomycete . Plants (Basel). 2020;9(10)doi: 10.3390/plants9101294.
Rogozhin, E. A., Vasilchenko, A. S., Barashkova, A. S., Smirnov, A. N., Zavriev, S. K., & Demushkin, V. P. (2020). Peptide Extracts from Seven Medicinal Plants Discovered to Inhibit Oomycete . Plants (Basel, Switzerland), 9(10), . https://doi.org/10.3390/plants9101294
Rogozhin, Eugene A, et al. "Peptide Extracts from Seven Medicinal Plants Discovered to Inhibit Oomycete ." Plants (Basel, Switzerland) vol. 9,10 (2020). doi: https://doi.org/10.3390/plants9101294
Rogozhin EA, Vasilchenko AS, Barashkova AS, Smirnov AN, Zavriev SK, Demushkin VP. Peptide Extracts from Seven Medicinal Plants Discovered to Inhibit Oomycete . Plants (Basel). 2020 Sep 30;9(10). doi: 10.3390/plants9101294. PMID: 33007947; PMCID: PMC7599828.
Copy Download .nbib Format: NLM
From Synthetic Fragments of Endogenous Three-Finger Proteins to Potential Drugs.

Frontiers in pharmacology

Kryukova EV, Egorova NS, Kudryavtsev DS, Lebedev DS, Spirova EN, Zhmak MN, Garifulina AI, Kasheverov IE, Utkin YN, Tsetlin VI.
PMID: 31333465
Front Pharmacol. 2019 Jul 03;10:748. doi: 10.3389/fphar.2019.00748. eCollection 2019.

The proteins of the Ly6 family have a three-finger folding as snake venom α-neurotoxins, targeting nicotinic acetylcholine receptors (nAChRs), and some of them, like mammalian secreted Ly6/uPAR protein (SLURP1) and membrane-attached Ly-6/neurotoxin (Lynx1), also interact with distinct nAChR subtypes....

Cite
Kryukova EV, Egorova NS, Kudryavtsev DS, et al. From Synthetic Fragments of Endogenous Three-Finger Proteins to Potential Drugs. Front Pharmacol. 2019;10:748doi: 10.3389/fphar.2019.00748.
Kryukova, E. V., Egorova, N. S., Kudryavtsev, D. S., Lebedev, D. S., Spirova, E. N., Zhmak, M. N., Garifulina, A. I., Kasheverov, I. E., Utkin, Y. N., & Tsetlin, V. I. (2019). From Synthetic Fragments of Endogenous Three-Finger Proteins to Potential Drugs. Frontiers in pharmacology, 10748. https://doi.org/10.3389/fphar.2019.00748
Kryukova, Elena V, et al. "From Synthetic Fragments of Endogenous Three-Finger Proteins to Potential Drugs." Frontiers in pharmacology vol. 10 (2019): 748. doi: https://doi.org/10.3389/fphar.2019.00748
Kryukova EV, Egorova NS, Kudryavtsev DS, Lebedev DS, Spirova EN, Zhmak MN, Garifulina AI, Kasheverov IE, Utkin YN, Tsetlin VI. From Synthetic Fragments of Endogenous Three-Finger Proteins to Potential Drugs. Front Pharmacol. 2019 Jul 03;10:748. doi: 10.3389/fphar.2019.00748. eCollection 2019. PMID: 31333465; PMCID: PMC6616073.
Copy Download .nbib Format: NLM
Showing 1 to 12 of 223 entries