Advanced Search
Display options
Filter resources
Text Availability
Article type
Publication date
Species
Language
Sex
Age
Showing 1 to 12 of 21 entries
Sorted by: Best Match Show Resources per page
A Sequential Algorithm for Multiblock Orthogonal Projections to Latent Structures.

Chemometrics and intelligent laboratory systems : an international journal sponsored by the Chemometrics Society

Worley B, Powers R.
PMID: 26640310
Chemometr Intell Lab Syst. 2015 Dec 15;149:33-39. doi: 10.1016/j.chemolab.2015.10.018.

Methods of multiblock bilinear factorizations have increased in popularity in chemistry and biology as recent increases in the availability of information-rich spectroscopic platforms has made collecting multiple spectroscopic observations per sample a practicable possibility. Of the existing multiblock methods,...

Cite
Worley B, Powers R. A Sequential Algorithm for Multiblock Orthogonal Projections to Latent Structures. Chemometr Intell Lab Syst. 2015;149:33-39doi: 10.1016/j.chemolab.2015.10.018.
Worley, B., & Powers, R. (2015). A Sequential Algorithm for Multiblock Orthogonal Projections to Latent Structures. Chemometrics and intelligent laboratory systems : an international journal sponsored by the Chemometrics Society, 14933-39. https://doi.org/10.1016/j.chemolab.2015.10.018
Worley, Bradley, and Powers, Robert. "A Sequential Algorithm for Multiblock Orthogonal Projections to Latent Structures." Chemometrics and intelligent laboratory systems : an international journal sponsored by the Chemometrics Society vol. 149 (2015): 33-39. doi: https://doi.org/10.1016/j.chemolab.2015.10.018
Worley B, Powers R. A Sequential Algorithm for Multiblock Orthogonal Projections to Latent Structures. Chemometr Intell Lab Syst. 2015 Dec 15;149:33-39. doi: 10.1016/j.chemolab.2015.10.018. PMID: 26640310; PMCID: PMC4668594.
Copy Download .nbib Format: NLM
Hiding in Plain Sight: Interplay between Staphylococcal Biofilms and Host Immunity.

Frontiers in immunology

Scherr TD, Heim CE, Morrison JM, Kielian T.
PMID: 24550921
Front Immunol. 2014 Feb 05;5:37. doi: 10.3389/fimmu.2014.00037. eCollection 2014.

Staphylococcus aureus and Staphylococcus epidermidis are notable for their propensity to form biofilms on implanted medical devices. Staphylococcal biofilm infections are typified by their recalcitrance to antibiotics and ability to circumvent host immune-mediated clearance, resulting in the establishment of...

Cite
Scherr TD, Heim CE, Morrison JM, et al. Hiding in Plain Sight: Interplay between Staphylococcal Biofilms and Host Immunity. Front Immunol. 2014;5:37doi: 10.3389/fimmu.2014.00037.
Scherr, T. D., Heim, C. E., Morrison, J. M., & Kielian, T. (2014). Hiding in Plain Sight: Interplay between Staphylococcal Biofilms and Host Immunity. Frontiers in immunology, 537. https://doi.org/10.3389/fimmu.2014.00037
Scherr, Tyler D, et al. "Hiding in Plain Sight: Interplay between Staphylococcal Biofilms and Host Immunity." Frontiers in immunology vol. 5 (2014): 37. doi: https://doi.org/10.3389/fimmu.2014.00037
Scherr TD, Heim CE, Morrison JM, Kielian T. Hiding in Plain Sight: Interplay between Staphylococcal Biofilms and Host Immunity. Front Immunol. 2014 Feb 05;5:37. doi: 10.3389/fimmu.2014.00037. eCollection 2014. PMID: 24550921; PMCID: PMC3913997.
Copy Download .nbib Format: NLM
Staphylococcal ClpXP protease targets the cellular antioxidant system to eliminate fitness-compromised cells in stationary phase.

Proceedings of the National Academy of Sciences of the United States of America

Alqarzaee AA, Chaudhari SS, Islam MM, Kumar V, Zimmerman MC, Saha R, Bayles KW, Frees D, Thomas VC.
PMID: 34782466
Proc Natl Acad Sci U S A. 2021 Nov 23;118(47). doi: 10.1073/pnas.2109671118.

The transition from growth to stationary phase is a natural response of bacteria to starvation and stress. When stress is alleviated and more favorable growth conditions return, bacteria resume proliferation without a significant loss in fitness. Although specific adaptations...

Cite
Alqarzaee AA, Chaudhari SS, Islam MM, et al. Staphylococcal ClpXP protease targets the cellular antioxidant system to eliminate fitness-compromised cells in stationary phase. Proc Natl Acad Sci U S A. 2021;118(47)doi: 10.1073/pnas.2109671118.
Alqarzaee, A. A., Chaudhari, S. S., Islam, M. M., Kumar, V., Zimmerman, M. C., Saha, R., Bayles, K. W., Frees, D., & Thomas, V. C. (2021). Staphylococcal ClpXP protease targets the cellular antioxidant system to eliminate fitness-compromised cells in stationary phase. Proceedings of the National Academy of Sciences of the United States of America, 118(47), . https://doi.org/10.1073/pnas.2109671118
Alqarzaee, Abdulelah A, et al. "Staphylococcal ClpXP protease targets the cellular antioxidant system to eliminate fitness-compromised cells in stationary phase." Proceedings of the National Academy of Sciences of the United States of America vol. 118,47 (2021). doi: https://doi.org/10.1073/pnas.2109671118
Alqarzaee AA, Chaudhari SS, Islam MM, Kumar V, Zimmerman MC, Saha R, Bayles KW, Frees D, Thomas VC. Staphylococcal ClpXP protease targets the cellular antioxidant system to eliminate fitness-compromised cells in stationary phase. Proc Natl Acad Sci U S A. 2021 Nov 23;118(47). doi: 10.1073/pnas.2109671118. PMID: 34782466; PMCID: PMC8617462.
Copy Download .nbib Format: NLM
Glycan-Dependent Corneocyte Adherence of Staphylococcus epidermidis Mediated by the Lectin Subdomain of Aap.

mBio

Roy P, Horswill AR, Fey PD.
PMID: 34253065
mBio. 2021 Aug 31;12(4):e0290820. doi: 10.1128/mBio.02908-20. Epub 2021 Jul 13.

Staphylococcus epidermidis and other coagulase-negative staphylococci (CoNS) that colonize skin are known to promote skin immunity and inhibit colonization of pathogens that cause skin and soft tissue infections, including Staphylococcus aureus. However, S. epidermidis adherence to corneocytes, the cells...

Cite
Roy P, Horswill AR, Fey PD. Glycan-Dependent Corneocyte Adherence of Staphylococcus epidermidis Mediated by the Lectin Subdomain of Aap. mBio. 2021;12(4):e0290820doi: 10.1128/mBio.02908-20.
Roy, P., Horswill, A. R., & Fey, P. D. (2021). Glycan-Dependent Corneocyte Adherence of Staphylococcus epidermidis Mediated by the Lectin Subdomain of Aap. mBio, 12(4), e0290820. https://doi.org/10.1128/mBio.02908-20
Roy, Paroma, et al. "Glycan-Dependent Corneocyte Adherence of Staphylococcus epidermidis Mediated by the Lectin Subdomain of Aap." mBio vol. 12,4 (2021): e0290820. doi: https://doi.org/10.1128/mBio.02908-20
Roy P, Horswill AR, Fey PD. Glycan-Dependent Corneocyte Adherence of Staphylococcus epidermidis Mediated by the Lectin Subdomain of Aap. mBio. 2021 Aug 31;12(4):e0290820. doi: 10.1128/mBio.02908-20. Epub 2021 Jul 13. PMID: 34253065; PMCID: PMC8406310.
Copy Download .nbib Format: NLM
Potassium Uptake Modulates Staphylococcus aureus Metabolism.

mSphere

Gries CM, Sadykov MR, Bulock LL, Chaudhari SS, Thomas VC, Bose JL, Bayles KW.
PMID: 27340697
mSphere. 2016 Jun 15;1(3). doi: 10.1128/mSphere.00125-16. eCollection 2016.

As a leading cause of community-associated and nosocomial infections, Staphylococcus aureus requires sophisticated mechanisms that function to maintain cellular homeostasis in response to its exposure to changing environmental conditions. The adaptation to stress and maintenance of homeostasis depend largely...

Cite
Gries CM, Sadykov MR, Bulock LL, et al. Potassium Uptake Modulates Staphylococcus aureus Metabolism. mSphere. 2016;1(3)doi: 10.1128/mSphere.00125-16.
Gries, C. M., Sadykov, M. R., Bulock, L. L., Chaudhari, S. S., Thomas, V. C., Bose, J. L., & Bayles, K. W. (2016). Potassium Uptake Modulates Staphylococcus aureus Metabolism. mSphere, 1(3), . https://doi.org/10.1128/mSphere.00125-16
Gries, Casey M, et al. "Potassium Uptake Modulates Staphylococcus aureus Metabolism." mSphere vol. 1,3 (2016). doi: https://doi.org/10.1128/mSphere.00125-16
Gries CM, Sadykov MR, Bulock LL, Chaudhari SS, Thomas VC, Bose JL, Bayles KW. Potassium Uptake Modulates Staphylococcus aureus Metabolism. mSphere. 2016 Jun 15;1(3). doi: 10.1128/mSphere.00125-16. eCollection 2016. PMID: 27340697; PMCID: PMC4911797.
Copy Download .nbib Format: NLM
Whole-Genome Sequences of Staphylococcus aureus Isolates from Positive Blood Cultures.

Microbiology resource announcements

Reslane I, Sladek M, Fey PD, Abdalhamid B.
PMID: 34709047
Microbiol Resour Announc. 2021 Oct 28;10(43):e0089821. doi: 10.1128/MRA.00898-21. Epub 2021 Oct 28.

Staphylococcus aureus is a major cause of skin and soft tissue infections as well as bloodstream infections worldwide. Here, we report the draft genome sequences of 18 deidentified S. aureus clinical strains collected from positive blood cultures.

Cite
Reslane I, Sladek M, Fey PD, et al. Whole-Genome Sequences of Staphylococcus aureus Isolates from Positive Blood Cultures. Microbiol Resour Announc. 2021;10(43):e0089821doi: 10.1128/MRA.00898-21.
Reslane, I., Sladek, M., Fey, P. D., & Abdalhamid, B. (2021). Whole-Genome Sequences of Staphylococcus aureus Isolates from Positive Blood Cultures. Microbiology resource announcements, 10(43), e0089821. https://doi.org/10.1128/MRA.00898-21
Reslane, Itidal, et al. "Whole-Genome Sequences of Staphylococcus aureus Isolates from Positive Blood Cultures." Microbiology resource announcements vol. 10,43 (2021): e0089821. doi: https://doi.org/10.1128/MRA.00898-21
Reslane I, Sladek M, Fey PD, Abdalhamid B. Whole-Genome Sequences of Staphylococcus aureus Isolates from Positive Blood Cultures. Microbiol Resour Announc. 2021 Oct 28;10(43):e0089821. doi: 10.1128/MRA.00898-21. Epub 2021 Oct 28. PMID: 34709047; PMCID: PMC8552733.
Copy Download .nbib Format: NLM
Mucin 5AC Serves as the Nexus for β-Catenin/c-Myc Interplay to Promote Glutamine Dependency During Pancreatic Cancer Chemoresistance.

Gastroenterology

Ganguly K, Bhatia R, Rauth S, Kisling A, Atri P, Thompson C, Vengoji R, Ram Krishn S, Shinde D, Thomas V, Kaur S, Mallya K, Cox JL, Kumar S, Batra SK.
PMID: 34534538
Gastroenterology. 2022 Jan;162(1):253-268.e13. doi: 10.1053/j.gastro.2021.09.017. Epub 2021 Sep 14.

BACKGROUND & AIMS: A major clinical challenge for patients with pancreatic cancer (PC) is metabolic adaptation. Neoplastic cells harboring molecular perturbations suffice for their increased anabolic demand and nucleotide biosynthesis to acquire chemoresistance. The mucin 5AC expressed de novo...

Cite
Ganguly K, Bhatia R, Rauth S, et al. Mucin 5AC Serves as the Nexus for β-Catenin/c-Myc Interplay to Promote Glutamine Dependency During Pancreatic Cancer Chemoresistance. Gastroenterology. 2021;162(1):253-268.e13doi: 10.1053/j.gastro.2021.09.017.
Ganguly, K., Bhatia, R., Rauth, S., Kisling, A., Atri, P., Thompson, C., Vengoji, R., Ram Krishn, S., Shinde, D., Thomas, V., Kaur, S., Mallya, K., Cox, J. L., Kumar, S., & Batra, S. K. (2022). Mucin 5AC Serves as the Nexus for β-Catenin/c-Myc Interplay to Promote Glutamine Dependency During Pancreatic Cancer Chemoresistance. Gastroenterology, 162(1), 253-268.e13. https://doi.org/10.1053/j.gastro.2021.09.017
Ganguly, Koelina, et al. "Mucin 5AC Serves as the Nexus for β-Catenin/c-Myc Interplay to Promote Glutamine Dependency During Pancreatic Cancer Chemoresistance." Gastroenterology vol. 162,1 (2022): 253-268.e13. doi: https://doi.org/10.1053/j.gastro.2021.09.017
Ganguly K, Bhatia R, Rauth S, Kisling A, Atri P, Thompson C, Vengoji R, Ram Krishn S, Shinde D, Thomas V, Kaur S, Mallya K, Cox JL, Kumar S, Batra SK. Mucin 5AC Serves as the Nexus for β-Catenin/c-Myc Interplay to Promote Glutamine Dependency During Pancreatic Cancer Chemoresistance. Gastroenterology. 2022 Jan;162(1):253-268.e13. doi: 10.1053/j.gastro.2021.09.017. Epub 2021 Sep 14. PMID: 34534538; PMCID: PMC8678212.
Copy Download .nbib Format: NLM
Fluorescent Sensor Arrays Can Predict and Quantify the Composition of Multicomponent Bacterial Samples.

Frontiers in chemistry

Svechkarev D, Sadykov MR, Houser LJ, Bayles KW, Mohs AM.
PMID: 32010667
Front Chem. 2020 Jan 15;7:916. doi: 10.3389/fchem.2019.00916. eCollection 2019.

Fast and reliable identification of infectious disease agents is among the most important challenges for the healthcare system. The discrimination of individual components of mixed infections represents a particularly difficult task. In the current study we further expand the...

Cite
Svechkarev D, Sadykov MR, Houser LJ, et al. Fluorescent Sensor Arrays Can Predict and Quantify the Composition of Multicomponent Bacterial Samples. Front Chem. 2020;7:916doi: 10.3389/fchem.2019.00916.
Svechkarev, D., Sadykov, M. R., Houser, L. J., Bayles, K. W., & Mohs, A. M. (2019). Fluorescent Sensor Arrays Can Predict and Quantify the Composition of Multicomponent Bacterial Samples. Frontiers in chemistry, 7916. https://doi.org/10.3389/fchem.2019.00916
Svechkarev, Denis, et al. "Fluorescent Sensor Arrays Can Predict and Quantify the Composition of Multicomponent Bacterial Samples." Frontiers in chemistry vol. 7 (2019): 916. doi: https://doi.org/10.3389/fchem.2019.00916
Svechkarev D, Sadykov MR, Houser LJ, Bayles KW, Mohs AM. Fluorescent Sensor Arrays Can Predict and Quantify the Composition of Multicomponent Bacterial Samples. Front Chem. 2020 Jan 15;7:916. doi: 10.3389/fchem.2019.00916. eCollection 2019. PMID: 32010667; PMCID: PMC6974461.
Copy Download .nbib Format: NLM
The Spl Serine Proteases Modulate .

mSphere

Paharik AE, Salgado-Pabon W, Meyerholz DK, White MJ, Schlievert PM, Horswill AR.
PMID: 27747296
mSphere. 2016 Oct 12;1(5). doi: 10.1128/mSphere.00208-16. eCollection 2016.

The Spl proteases are a group of six serine proteases that are encoded on the νSaβ pathogenicity island and are unique to

Cite
Paharik AE, Salgado-Pabon W, Meyerholz DK, et al. The Spl Serine Proteases Modulate . mSphere. 2016;1(5)doi: 10.1128/mSphere.00208-16.
Paharik, A. E., Salgado-Pabon, W., Meyerholz, D. K., White, M. J., Schlievert, P. M., & Horswill, A. R. (2016). The Spl Serine Proteases Modulate . mSphere, 1(5), . https://doi.org/10.1128/mSphere.00208-16
Paharik, Alexandra E, et al. "The Spl Serine Proteases Modulate ." mSphere vol. 1,5 (2016). doi: https://doi.org/10.1128/mSphere.00208-16
Paharik AE, Salgado-Pabon W, Meyerholz DK, White MJ, Schlievert PM, Horswill AR. The Spl Serine Proteases Modulate . mSphere. 2016 Oct 12;1(5). doi: 10.1128/mSphere.00208-16. eCollection 2016. PMID: 27747296; PMCID: PMC5061998.
Copy Download .nbib Format: NLM
Glycan-Dependent Corneocyte Adherence of Staphylococcus epidermidis Mediated by the Lectin Subdomain of Aap.

mBio

Roy P, Horswill AR, Fey PD.
PMID: 34253065
mBio. 2021 Aug 31;12(4):e0290820. doi: 10.1128/mBio.02908-20. Epub 2021 Jul 13.

Staphylococcus epidermidis and other coagulase-negative staphylococci (CoNS) that colonize skin are known to promote skin immunity and inhibit colonization of pathogens that cause skin and soft tissue infections, including Staphylococcus aureus. However, S. epidermidis adherence to corneocytes, the cells...

Cite
Roy P, Horswill AR, Fey PD. Glycan-Dependent Corneocyte Adherence of Staphylococcus epidermidis Mediated by the Lectin Subdomain of Aap. mBio. 2021;12(4):e0290820doi: 10.1128/mBio.02908-20.
Roy, P., Horswill, A. R., & Fey, P. D. (2021). Glycan-Dependent Corneocyte Adherence of Staphylococcus epidermidis Mediated by the Lectin Subdomain of Aap. mBio, 12(4), e0290820. https://doi.org/10.1128/mBio.02908-20
Roy, Paroma, et al. "Glycan-Dependent Corneocyte Adherence of Staphylococcus epidermidis Mediated by the Lectin Subdomain of Aap." mBio vol. 12,4 (2021): e0290820. doi: https://doi.org/10.1128/mBio.02908-20
Roy P, Horswill AR, Fey PD. Glycan-Dependent Corneocyte Adherence of Staphylococcus epidermidis Mediated by the Lectin Subdomain of Aap. mBio. 2021 Aug 31;12(4):e0290820. doi: 10.1128/mBio.02908-20. Epub 2021 Jul 13. PMID: 34253065; PMCID: PMC8406310.
Copy Download .nbib Format: NLM
Human monoclonal antibodies against .

eLife

de Vor L, van Dijk B, van Kessel K, Kavanaugh JS, de Haas C, Aerts PC, Viveen MC, Boel EC, Fluit AC, Kwiecinski JM, Krijger GC, Ramakers RM, Beekman FJ, Dadachova E, Lam MG, Vogely HC, van der Wal BC, van Strijp JA, Horswill AR, Weinans H, Rooijakkers SH.
PMID: 34989676
Elife. 2022 Jan 06;11. doi: 10.7554/eLife.67301.

Implant-associated

Cite
de Vor L, van Dijk B, van Kessel K, et al. Human monoclonal antibodies against . Elife. 2022;11doi: 10.7554/eLife.67301.
de Vor, L., van Dijk, B., van Kessel, K., Kavanaugh, J. S., de Haas, C., Aerts, P. C., Viveen, M. C., Boel, E. C., Fluit, A. C., Kwiecinski, J. M., Krijger, G. C., Ramakers, R. M., Beekman, F. J., Dadachova, E., Lam, M. G., Vogely, H. C., van der Wal, B. C., van Strijp, J. A., Horswill, A. R., Weinans, H., & Rooijakkers, S. H. (2022). Human monoclonal antibodies against . eLife, 11. https://doi.org/10.7554/eLife.67301
de Vor, Lisanne, et al. "Human monoclonal antibodies against ." eLife vol. 11 (2022). doi: https://doi.org/10.7554/eLife.67301
de Vor L, van Dijk B, van Kessel K, Kavanaugh JS, de Haas C, Aerts PC, Viveen MC, Boel EC, Fluit AC, Kwiecinski JM, Krijger GC, Ramakers RM, Beekman FJ, Dadachova E, Lam MG, Vogely HC, van der Wal BC, van Strijp JA, Horswill AR, Weinans H, Rooijakkers SH. Human monoclonal antibodies against . Elife. 2022 Jan 06;11. doi: 10.7554/eLife.67301. PMID: 34989676; PMCID: PMC8751199.
Copy Download .nbib Format: NLM
Electron Paramagnetic Resonance (EPR) Spectroscopy to Detect Reactive Oxygen Species in .

Bio-protocol

Thomas VC, Chaudhari SS, Jones J, Zimmerman MC, Bayles KW.
PMID: 27182534
Bio Protoc. 2015 Sep 05;5(17). doi: 10.21769/bioprotoc.1586.

Under aerobic conditions,

Cite
Thomas VC, Chaudhari SS, Jones J, et al. Electron Paramagnetic Resonance (EPR) Spectroscopy to Detect Reactive Oxygen Species in . Bio Protoc. 2015;5(17)doi: 10.21769/bioprotoc.1586.
Thomas, V. C., Chaudhari, S. S., Jones, J., Zimmerman, M. C., & Bayles, K. W. (2015). Electron Paramagnetic Resonance (EPR) Spectroscopy to Detect Reactive Oxygen Species in . Bio-protocol, 5(17), . https://doi.org/10.21769/bioprotoc.1586
Thomas, Vinai Chittezham, et al. "Electron Paramagnetic Resonance (EPR) Spectroscopy to Detect Reactive Oxygen Species in ." Bio-protocol vol. 5,17 (2015). doi: https://doi.org/10.21769/bioprotoc.1586
Thomas VC, Chaudhari SS, Jones J, Zimmerman MC, Bayles KW. Electron Paramagnetic Resonance (EPR) Spectroscopy to Detect Reactive Oxygen Species in . Bio Protoc. 2015 Sep 05;5(17). doi: 10.21769/bioprotoc.1586. PMID: 27182534; PMCID: PMC4863951.
Copy Download .nbib Format: NLM
Showing 1 to 12 of 21 entries