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While the revolution will not be crystallized, biochemistry reigns supreme.

Protein science : a publication of the Protein Society

Takizawa Y, Binshtein E, Erwin AL, Pyburn TM, Mittendorf KF, Ohi MD.
PMID: 27673321
Protein Sci. 2017 Jan;26(1):69-81. doi: 10.1002/pro.3054. Epub 2016 Oct 06.

Single-particle cryo-electron microscopy (EM) is currently gaining attention for the ability to calculate structures that reach sub-5 Å resolutions; however, the technique is more than just an alternative approach to X-ray crystallography. Molecular machines work via dynamic conformational changes,...

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Takizawa Y, Binshtein E, Erwin AL, et al. While the revolution will not be crystallized, biochemistry reigns supreme. Protein Sci. 2016;26(1):69-81doi: 10.1002/pro.3054.
Takizawa, Y., Binshtein, E., Erwin, A. L., Pyburn, T. M., Mittendorf, K. F., & Ohi, M. D. (2017). While the revolution will not be crystallized, biochemistry reigns supreme. Protein science : a publication of the Protein Society, 26(1), 69-81. https://doi.org/10.1002/pro.3054
Takizawa, Yoshimasa, et al. "While the revolution will not be crystallized, biochemistry reigns supreme." Protein science : a publication of the Protein Society vol. 26,1 (2017): 69-81. doi: https://doi.org/10.1002/pro.3054
Takizawa Y, Binshtein E, Erwin AL, Pyburn TM, Mittendorf KF, Ohi MD. While the revolution will not be crystallized, biochemistry reigns supreme. Protein Sci. 2017 Jan;26(1):69-81. doi: 10.1002/pro.3054. Epub 2016 Oct 06. PMID: 27673321; PMCID: PMC5192976.
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Estimate your dose: RADDOSE-3D.

Protein science : a publication of the Protein Society

Bury CS, Brooks-Bartlett JC, Walsh SP, Garman EF.
PMID: 28921782
Protein Sci. 2018 Jan;27(1):217-228. doi: 10.1002/pro.3302. Epub 2017 Nov 06.

We present the current status of RADDOSE-3D, a software tool allowing the estimation of the dose absorbed in a macromolecular crystallography diffraction experiment. The code allows a temporal and spatial dose contour map to be calculated for a crystal...

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Bury CS, Brooks-Bartlett JC, Walsh SP, et al. Estimate your dose: RADDOSE-3D. Protein Sci. 2017;27(1):217-228doi: 10.1002/pro.3302.
Bury, C. S., Brooks-Bartlett, J. C., Walsh, S. P., & Garman, E. F. (2018). Estimate your dose: RADDOSE-3D. Protein science : a publication of the Protein Society, 27(1), 217-228. https://doi.org/10.1002/pro.3302
Bury, Charles S, et al. "Estimate your dose: RADDOSE-3D." Protein science : a publication of the Protein Society vol. 27,1 (2018): 217-228. doi: https://doi.org/10.1002/pro.3302
Bury CS, Brooks-Bartlett JC, Walsh SP, Garman EF. Estimate your dose: RADDOSE-3D. Protein Sci. 2018 Jan;27(1):217-228. doi: 10.1002/pro.3302. Epub 2017 Nov 06. PMID: 28921782; PMCID: PMC5734275.
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Etiologic Framework for the Study of Neurodegenerative Disorders as Well as Vascular and Metabolic Comorbidities on the Grounds of Shared Epidemiologic and Biologic Features.

Frontiers in aging neuroscience

de Pedro-Cuesta J, Martínez-Martín P, Rábano A, Ruiz-Tovar M, Alcalde-Cabero E, Calero M.
PMID: 27378910
Front Aging Neurosci. 2016 Jun 13;8:138. doi: 10.3389/fnagi.2016.00138. eCollection 2016.

BACKGROUND: During the last two decades, protein aggregation at all organismal levels, from viruses to humans, has emerged from a neglected area of protein science to become a central issue in biology and biomedicine. This article constitutes a risk-based...

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de Pedro-Cuesta J, Martínez-Martín P, Rábano A, et al. Etiologic Framework for the Study of Neurodegenerative Disorders as Well as Vascular and Metabolic Comorbidities on the Grounds of Shared Epidemiologic and Biologic Features. Front Aging Neurosci. 2016;8:138doi: 10.3389/fnagi.2016.00138.
de Pedro-Cuesta, J., Martínez-Martín, P., Rábano, A., Ruiz-Tovar, M., Alcalde-Cabero, E., & Calero, M. (2016). Etiologic Framework for the Study of Neurodegenerative Disorders as Well as Vascular and Metabolic Comorbidities on the Grounds of Shared Epidemiologic and Biologic Features. Frontiers in aging neuroscience, 8138. https://doi.org/10.3389/fnagi.2016.00138
de Pedro-Cuesta, Jesús, et al. "Etiologic Framework for the Study of Neurodegenerative Disorders as Well as Vascular and Metabolic Comorbidities on the Grounds of Shared Epidemiologic and Biologic Features." Frontiers in aging neuroscience vol. 8 (2016): 138. doi: https://doi.org/10.3389/fnagi.2016.00138
de Pedro-Cuesta J, Martínez-Martín P, Rábano A, Ruiz-Tovar M, Alcalde-Cabero E, Calero M. Etiologic Framework for the Study of Neurodegenerative Disorders as Well as Vascular and Metabolic Comorbidities on the Grounds of Shared Epidemiologic and Biologic Features. Front Aging Neurosci. 2016 Jun 13;8:138. doi: 10.3389/fnagi.2016.00138. eCollection 2016. PMID: 27378910; PMCID: PMC4904010.
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Erratum.

Protein science : a publication of the Protein Society

[No authors listed]
PMID: 26735112
Protein Sci. 2016 Jan;25(1):302-3. doi: 10.1002/pro.2846.

No abstract available.

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Erratum. Protein Sci. 2016;25(1):302-3doi: 10.1002/pro.2846.
(2016). Erratum. Protein science : a publication of the Protein Society, 25(1), 302-3. https://doi.org/10.1002/pro.2846
"Erratum." Protein science : a publication of the Protein Society vol. 25,1 (2016): 302-3. doi: https://doi.org/10.1002/pro.2846
Erratum. Protein Sci. 2016 Jan;25(1):302-3. doi: 10.1002/pro.2846. PMID: 26735112; PMCID: PMC4815296.
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Standard laboratory equipment.

Current protocols in protein science

[No authors listed]
PMID: 18429067
Curr Protoc Protein Sci. 2001 May;Appendix 2D. doi: 10.1002/0471140864.psa02ds01.

This appendix lists standard pieces of equipment in the modern biochemistry laboratory, i.e., items used extensively in this manual and thus not included in the individual materials lists.

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Standard laboratory equipment. Curr Protoc Protein Sci. 2001;Appendix 2Ddoi: 10.1002/0471140864.psa02ds01.
(2001). Standard laboratory equipment. Current protocols in protein science, Appendix 2D. https://doi.org/10.1002/0471140864.psa02ds01
"Standard laboratory equipment." Current protocols in protein science vol. (2001): Appendix 2D. doi: https://doi.org/10.1002/0471140864.psa02ds01
Standard laboratory equipment. Curr Protoc Protein Sci. 2001 May;Appendix 2D. doi: 10.1002/0471140864.psa02ds01. PMID: 18429067.
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Prediction of the disulfide-bonding state of cysteines in proteins at 88% accuracy.

Protein science : a publication of the Protein Society

Martelli PL, Fariselli P, Malaguti L, Casadio R.
PMID: 15452953
Protein Sci. 2003 Jul;12(7):1578. doi: 10.1110/ps.0219602.

No abstract available.

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Martelli PL, Fariselli P, Malaguti L, et al. Prediction of the disulfide-bonding state of cysteines in proteins at 88% accuracy. Protein Sci. 2003;12(7):1578doi: 10.1110/ps.0219602.
Martelli, P. L., Fariselli, P., Malaguti, L., & Casadio, R. (2003). Prediction of the disulfide-bonding state of cysteines in proteins at 88% accuracy. Protein science : a publication of the Protein Society, 12(7), 1578. https://doi.org/10.1110/ps.0219602
Martelli, Pier Luigi, et al. "Prediction of the disulfide-bonding state of cysteines in proteins at 88% accuracy." Protein science : a publication of the Protein Society vol. 12,7 (2003): 1578. doi: https://doi.org/10.1110/ps.0219602
Martelli PL, Fariselli P, Malaguti L, Casadio R. Prediction of the disulfide-bonding state of cysteines in proteins at 88% accuracy. Protein Sci. 2003 Jul;12(7):1578. doi: 10.1110/ps.0219602. PMID: 15452953; PMCID: PMC2323920.
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Miniaturizing sample spots for matrix-assisted laser desorption/ionization mass spectrometry.

Trends in analytical chemistry : TRAC

Tu T, Gross ML.
PMID: 20161086
Trends Analyt Chem. 2009 Aug 01;28(7):833-841. doi: 10.1016/j.trac.2009.03.013.

The trend of miniaturization in bioanalytical chemistry is shifting from technical development to practical application. In matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS), progress in miniaturizing sample spots has been driven by the needs to increase sensitivity and speed, to...

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Tu T, Gross ML. Miniaturizing sample spots for matrix-assisted laser desorption/ionization mass spectrometry. Trends Analyt Chem. 2009;28(7):833-841doi: 10.1016/j.trac.2009.03.013.
Tu, T., & Gross, M. L. (2009). Miniaturizing sample spots for matrix-assisted laser desorption/ionization mass spectrometry. Trends in analytical chemistry : TRAC, 28(7), 833-841. https://doi.org/10.1016/j.trac.2009.03.013
Tu, Tingting, and Gross, Michael L. "Miniaturizing sample spots for matrix-assisted laser desorption/ionization mass spectrometry." Trends in analytical chemistry : TRAC vol. 28,7 (2009): 833-841. doi: https://doi.org/10.1016/j.trac.2009.03.013
Tu T, Gross ML. Miniaturizing sample spots for matrix-assisted laser desorption/ionization mass spectrometry. Trends Analyt Chem. 2009 Aug 01;28(7):833-841. doi: 10.1016/j.trac.2009.03.013. PMID: 20161086; PMCID: PMC2744082.
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Solution structure of a small protein containing a fluorinated side chain in the core.

Protein science : a publication of the Protein Society

Cornilescu G, Hadley EB, Woll MG, Markley JL, Gellman SH, Cornilescu CC.
PMID: 17915350
Protein Sci. 2007 Sep;16(9):2089. doi: 10.1110/ps.062557707.

No abstract available.

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Cornilescu G, Hadley EB, Woll MG, et al. Solution structure of a small protein containing a fluorinated side chain in the core. Protein Sci. 2007;16(9):2089doi: 10.1110/ps.062557707.
Cornilescu, G., Hadley, E. B., Woll, M. G., Markley, J. L., Gellman, S. H., & Cornilescu, C. C. (2007). Solution structure of a small protein containing a fluorinated side chain in the core. Protein science : a publication of the Protein Society, 16(9), 2089. https://doi.org/10.1110/ps.062557707
Cornilescu, Gabriel, et al. "Solution structure of a small protein containing a fluorinated side chain in the core." Protein science : a publication of the Protein Society vol. 16,9 (2007): 2089. doi: https://doi.org/10.1110/ps.062557707
Cornilescu G, Hadley EB, Woll MG, Markley JL, Gellman SH, Cornilescu CC. Solution structure of a small protein containing a fluorinated side chain in the core. Protein Sci. 2007 Sep;16(9):2089. doi: 10.1110/ps.062557707. PMID: 17915350; PMCID: PMC2206987.
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Concepts in MDM2 Signaling: Allosteric Regulation and Feedback Loops.

Genes & cancer

Ponnuswamy A, Hupp T, Fåhraeus R.
PMID: 23150762
Genes Cancer. 2012 Mar;3(3):291-7. doi: 10.1177/1947601912454140.

The function and regulation of MDM2 as a component of a p53-dependent negative feedback loop has formed a core paradigm in the p53 field. This concept, now 20 years old, has been solidified by fields of protein science, transgenic...

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Ponnuswamy A, Hupp T, Fåhraeus R. Concepts in MDM2 Signaling: Allosteric Regulation and Feedback Loops. Genes Cancer. 2012;3(3):291-7doi: 10.1177/1947601912454140.
Ponnuswamy, A., Hupp, T., & Fåhraeus, R. (2012). Concepts in MDM2 Signaling: Allosteric Regulation and Feedback Loops. Genes & cancer, 3(3), 291-7. https://doi.org/10.1177/1947601912454140
Ponnuswamy, Anand, et al. "Concepts in MDM2 Signaling: Allosteric Regulation and Feedback Loops." Genes & cancer vol. 3,3 (2012): 291-7. doi: https://doi.org/10.1177/1947601912454140
Ponnuswamy A, Hupp T, Fåhraeus R. Concepts in MDM2 Signaling: Allosteric Regulation and Feedback Loops. Genes Cancer. 2012 Mar;3(3):291-7. doi: 10.1177/1947601912454140. PMID: 23150762; PMCID: PMC3494372.
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The 29(th) Annual Symposium of the Protein Society, Barcelona, Spain, July 22-25, 2015.

Protein science : a publication of the Protein Society

[No authors listed]
PMID: 26452528
Protein Sci. 2015 Oct;24:1-313. doi: 10.1002/pro.2823.

No abstract available.

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The 29(th) Annual Symposium of the Protein Society, Barcelona, Spain, July 22-25, 2015. Protein Sci. 2015;24:1-313doi: 10.1002/pro.2823.
(2015). The 29(th) Annual Symposium of the Protein Society, Barcelona, Spain, July 22-25, 2015. Protein science : a publication of the Protein Society, 241-313. https://doi.org/10.1002/pro.2823
"The 29(th) Annual Symposium of the Protein Society, Barcelona, Spain, July 22-25, 2015." Protein science : a publication of the Protein Society vol. 24 (2015): 1-313. doi: https://doi.org/10.1002/pro.2823
The 29(th) Annual Symposium of the Protein Society, Barcelona, Spain, July 22-25, 2015. Protein Sci. 2015 Oct;24:1-313. doi: 10.1002/pro.2823. PMID: 26452528; PMCID: PMC4632850.
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Quantifying and understanding the fitness effects of protein mutations: Laboratory versus nature.

Protein science : a publication of the Protein Society

Boucher JI, Bolon DNA, Tawfik DS.
PMID: 30747470
Protein Sci. 2019 Mar;28(3):671. doi: 10.1002/pro.3476.

No abstract available.

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Boucher JI, Bolon DNA, Tawfik DS. Quantifying and understanding the fitness effects of protein mutations: Laboratory versus nature. Protein Sci. 2019;28(3):671doi: 10.1002/pro.3476.
Boucher, J. I., Bolon, D. N. A., & Tawfik, D. S. (2019). Quantifying and understanding the fitness effects of protein mutations: Laboratory versus nature. Protein science : a publication of the Protein Society, 28(3), 671. https://doi.org/10.1002/pro.3476
Boucher, Jeffrey I, et al. "Quantifying and understanding the fitness effects of protein mutations: Laboratory versus nature." Protein science : a publication of the Protein Society vol. 28,3 (2019): 671. doi: https://doi.org/10.1002/pro.3476
Boucher JI, Bolon DNA, Tawfik DS. Quantifying and understanding the fitness effects of protein mutations: Laboratory versus nature. Protein Sci. 2019 Mar;28(3):671. doi: 10.1002/pro.3476. PMID: 30747470; PMCID: PMC6371626.
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Award Winners and Abstracts of the 33rd Annual Symposium of The Protein Society; Seattle, Washington, June 30-July 3, 2019.

Protein science : a publication of the Protein Society

[No authors listed]
PMID: 31566831
Protein Sci. 2019 Sep;28:12-211. doi: 10.1002/pro.3710.

No abstract available.

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Award Winners and Abstracts of the 33rd Annual Symposium of The Protein Society; Seattle, Washington, June 30-July 3, 2019. Protein Sci. 2019;28:12-211doi: 10.1002/pro.3710.
(2019). Award Winners and Abstracts of the 33rd Annual Symposium of The Protein Society; Seattle, Washington, June 30-July 3, 2019. Protein science : a publication of the Protein Society, 2812-211. https://doi.org/10.1002/pro.3710
"Award Winners and Abstracts of the 33rd Annual Symposium of The Protein Society; Seattle, Washington, June 30-July 3, 2019." Protein science : a publication of the Protein Society vol. 28 (2019): 12-211. doi: https://doi.org/10.1002/pro.3710
Award Winners and Abstracts of the 33rd Annual Symposium of The Protein Society; Seattle, Washington, June 30-July 3, 2019. Protein Sci. 2019 Sep;28:12-211. doi: 10.1002/pro.3710. PMID: 31566831; PMCID: PMC6767941.
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Showing 1 to 12 of 434 entries