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Spin-resolved photoemission of surface states of W(110)-(1 x 1)H.

Physical review letters

Hochstrasser M, Tobin JG, Rotenberg E, Kevan SD.
PMID: 12443440
Phys Rev Lett. 2002 Nov 18;89(21):216802. doi: 10.1103/PhysRevLett.89.216802. Epub 2002 Nov 01.

The surface electronic states of W(110)-(1 x 1)H have been measured using spin- and angle-resolved photoemission. We directly demonstrate that the surface bands are both split and spin-polarized by the spin-orbit interaction in association with the loss of inversion...

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Hochstrasser M, Tobin JG, Rotenberg E, et al. Spin-resolved photoemission of surface states of W(110)-(1 x 1)H. Phys Rev Lett. 2002;89(21):216802doi: 10.1103/PhysRevLett.89.216802.
Hochstrasser, M., Tobin, J. G., Rotenberg, E., & Kevan, S. D. (2002). Spin-resolved photoemission of surface states of W(110)-(1 x 1)H. Physical review letters, 89(21), 216802. https://doi.org/10.1103/PhysRevLett.89.216802
Hochstrasser, M, et al. "Spin-resolved photoemission of surface states of W(110)-(1 x 1)H." Physical review letters vol. 89,21 (2002): 216802. doi: https://doi.org/10.1103/PhysRevLett.89.216802
Hochstrasser M, Tobin JG, Rotenberg E, Kevan SD. Spin-resolved photoemission of surface states of W(110)-(1 x 1)H. Phys Rev Lett. 2002 Nov 18;89(21):216802. doi: 10.1103/PhysRevLett.89.216802. Epub 2002 Nov 01. PMID: 12443440.
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SUMO-1: Ubiquitin gains weight.

Trends in cell biology

Johnson PR, Hochstrasser M.
PMID: 17708991
Trends Cell Biol. 1997 Oct;7(10):408-13. doi: 10.1016/S0962-8924(97)01132-X.

The highly conserved ubiquitin polypeptide functions by covalently modifying other proteins. This modification has a well-established role in facilitating substrate degradation by the proteasome and can regulate some proteins by ways other than targeting them to the proteasome. It...

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Johnson PR, Hochstrasser M. SUMO-1: Ubiquitin gains weight. Trends Cell Biol. 1997;7(10):408-13doi: 10.1016/S0962-8924(97)01132-X.
Johnson, P. R., & Hochstrasser, M. (1997). SUMO-1: Ubiquitin gains weight. Trends in cell biology, 7(10), 408-13. https://doi.org/10.1016/S0962-8924(97)01132-X
Johnson, P R, and Hochstrasser, M. "SUMO-1: Ubiquitin gains weight." Trends in cell biology vol. 7,10 (1997): 408-13. doi: https://doi.org/10.1016/S0962-8924(97)01132-X
Johnson PR, Hochstrasser M. SUMO-1: Ubiquitin gains weight. Trends Cell Biol. 1997 Oct;7(10):408-13. doi: 10.1016/S0962-8924(97)01132-X. PMID: 17708991.
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The Two Dimensional Vibrational Echo of a Nitrile Probe of the Villin HP35 Protein.

The journal of physical chemistry letters

Urbanek DC, Vorobyev DY, Serrano AL, Gai F, Hochstrasser RM.
PMID: 21132120
J Phys Chem Lett. 2010;1:3311-3315. doi: 10.1021/jz101367d.

2D IR spectroscopy was used to probe the hydrophobic core structure of the 35-residue Villin headpiece subdomain, HP35, by monitoring the C≡N vibrational stretching band of a cyano substituted phenylalanine (Phe). The presence of two humps in the vibrational...

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Urbanek DC, Vorobyev DY, Serrano AL, et al. The Two Dimensional Vibrational Echo of a Nitrile Probe of the Villin HP35 Protein. J Phys Chem Lett. 2010;1:3311-3315doi: 10.1021/jz101367d.
Urbanek, D. C., Vorobyev, D. Y., Serrano, A. L., Gai, F., & Hochstrasser, R. M. (2010). The Two Dimensional Vibrational Echo of a Nitrile Probe of the Villin HP35 Protein. The journal of physical chemistry letters, 13311-3315. https://doi.org/10.1021/jz101367d
Urbanek, Diana C, et al. "The Two Dimensional Vibrational Echo of a Nitrile Probe of the Villin HP35 Protein." The journal of physical chemistry letters vol. 1 (2010): 3311-3315. doi: https://doi.org/10.1021/jz101367d
Urbanek DC, Vorobyev DY, Serrano AL, Gai F, Hochstrasser RM. The Two Dimensional Vibrational Echo of a Nitrile Probe of the Villin HP35 Protein. J Phys Chem Lett. 2010;1:3311-3315. doi: 10.1021/jz101367d. PMID: 21132120; PMCID: PMC2995499.
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Ubiquitin fusion degradation protein 1 as a blood marker for the early diagnosis of ischemic stroke.

Biomarker insights

Allard L, Turck N, Burkhard PR, Walter N, Rosell A, Gex-Fabry M, Hochstrasser DF, Montaner J, Sanchez JC.
PMID: 19662200
Biomark Insights. 2007 Apr 19;2:155-64.

BACKGROUND: Efficacy of thrombolysis in acute ischemic stroke is strongly related to physician's ability to make an accurate diagnosis and to intervene within 3-6 h after event onset. In this context, the discovery and validation of very early blood...

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Allard L, Turck N, Burkhard PR, et al. Ubiquitin fusion degradation protein 1 as a blood marker for the early diagnosis of ischemic stroke. Biomark Insights. 2007;2:155-64
Allard, L., Turck, N., Burkhard, P. R., Walter, N., Rosell, A., Gex-Fabry, M., Hochstrasser, D. F., Montaner, J., & Sanchez, J. C. (2007). Ubiquitin fusion degradation protein 1 as a blood marker for the early diagnosis of ischemic stroke. Biomarker insights, 2155-64.
Allard, Laure, et al. "Ubiquitin fusion degradation protein 1 as a blood marker for the early diagnosis of ischemic stroke." Biomarker insights vol. 2 (2007): 155-64.
Allard L, Turck N, Burkhard PR, Walter N, Rosell A, Gex-Fabry M, Hochstrasser DF, Montaner J, Sanchez JC. Ubiquitin fusion degradation protein 1 as a blood marker for the early diagnosis of ischemic stroke. Biomark Insights. 2007 Apr 19;2:155-64. PMID: 19662200; PMCID: PMC2717829.
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Impact of preanalytical variables on the analysis of biological fluids in proteomic studies.

Proteomics. Clinical applications

Ferguson RE, Hochstrasser DF, Banks RE.
PMID: 21136730
Proteomics Clin Appl. 2007 Aug;1(8):739-46. doi: 10.1002/prca.200700380. Epub 2007 Jul 10.

Although proteomic technologies have been enthusiastically embraced in the field of biomarker discovery and particularly with biological fluids, it is increasingly being recognized that pre-analytical effects, i.e. those occurring prior to the point of actual sample analysis and including...

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Ferguson RE, Hochstrasser DF, Banks RE. Impact of preanalytical variables on the analysis of biological fluids in proteomic studies. Proteomics Clin Appl. 2007;1(8):739-46doi: 10.1002/prca.200700380.
Ferguson, R. E., Hochstrasser, D. F., & Banks, R. E. (2007). Impact of preanalytical variables on the analysis of biological fluids in proteomic studies. Proteomics. Clinical applications, 1(8), 739-46. https://doi.org/10.1002/prca.200700380
Ferguson, Roisean E, et al. "Impact of preanalytical variables on the analysis of biological fluids in proteomic studies." Proteomics. Clinical applications vol. 1,8 (2007): 739-46. doi: https://doi.org/10.1002/prca.200700380
Ferguson RE, Hochstrasser DF, Banks RE. Impact of preanalytical variables on the analysis of biological fluids in proteomic studies. Proteomics Clin Appl. 2007 Aug;1(8):739-46. doi: 10.1002/prca.200700380. Epub 2007 Jul 10. PMID: 21136730.
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Proteomic analysis of a podocyte vesicle-enriched fraction from human normal and pathological urine samples.

Proteomics. Clinical applications

Lescuyer P, Pernin A, Hainard A, Bigeire C, Burgess JA, Zimmermann-Ivol C, Sanchez JC, Schifferli JA, Hochstrasser DF, Moll S.
PMID: 21136901
Proteomics Clin Appl. 2008 Jul;2(7):1008-18. doi: 10.1002/prca.200800033. Epub 2008 Jul 10.

Podocytes (glomerular visceral epithelial cells) release vesicles into urine. Podocyte vesicle-enriched fractions from normal and pathological human urine samples were prepared for proteomic analysis. An immunoadsorption method was applied and enrichment of podocyte vesicles was assessed. We identified 76...

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Lescuyer P, Pernin A, Hainard A, et al. Proteomic analysis of a podocyte vesicle-enriched fraction from human normal and pathological urine samples. Proteomics Clin Appl. 2008;2(7):1008-18doi: 10.1002/prca.200800033.
Lescuyer, P., Pernin, A., Hainard, A., Bigeire, C., Burgess, J. A., Zimmermann-Ivol, C., Sanchez, J. C., Schifferli, J. A., Hochstrasser, D. F., & Moll, S. (2008). Proteomic analysis of a podocyte vesicle-enriched fraction from human normal and pathological urine samples. Proteomics. Clinical applications, 2(7), 1008-18. https://doi.org/10.1002/prca.200800033
Lescuyer, Pierre, et al. "Proteomic analysis of a podocyte vesicle-enriched fraction from human normal and pathological urine samples." Proteomics. Clinical applications vol. 2,7 (2008): 1008-18. doi: https://doi.org/10.1002/prca.200800033
Lescuyer P, Pernin A, Hainard A, Bigeire C, Burgess JA, Zimmermann-Ivol C, Sanchez JC, Schifferli JA, Hochstrasser DF, Moll S. Proteomic analysis of a podocyte vesicle-enriched fraction from human normal and pathological urine samples. Proteomics Clin Appl. 2008 Jul;2(7):1008-18. doi: 10.1002/prca.200800033. Epub 2008 Jul 10. PMID: 21136901.
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Regenerative amplification of 30-fs pulses in Ti:sapphire at 5 kHz.

Optics letters

Wynne K, Reid GD, Hochstrasser RM.
PMID: 19844480
Opt Lett. 1994 Jun 15;19(12):895-7. doi: 10.1364/ol.19.000895.

18-fs pulses from a self-mode-locked Ti:sapphire laser are amplified to 60 microJ of energy at 4.9 kHz with chirped-pulse amplification in a Ti:sapphire regenerative amplifier. After recompression, 30-35-fs, near-transform-limited pulses are obtained.

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Wynne K, Reid GD, Hochstrasser RM. Regenerative amplification of 30-fs pulses in Ti:sapphire at 5 kHz. Opt Lett. 1994;19(12):895-7doi: 10.1364/ol.19.000895.
Wynne, K., Reid, G. D., & Hochstrasser, R. M. (1994). Regenerative amplification of 30-fs pulses in Ti:sapphire at 5 kHz. Optics letters, 19(12), 895-7. https://doi.org/10.1364/ol.19.000895
Wynne, K, et al. "Regenerative amplification of 30-fs pulses in Ti:sapphire at 5 kHz." Optics letters vol. 19,12 (1994): 895-7. doi: https://doi.org/10.1364/ol.19.000895
Wynne K, Reid GD, Hochstrasser RM. Regenerative amplification of 30-fs pulses in Ti:sapphire at 5 kHz. Opt Lett. 1994 Jun 15;19(12):895-7. doi: 10.1364/ol.19.000895. PMID: 19844480.
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High-repetition-rate infrared-pump, infrared-probe spectrometer.

Applied optics

Lannone M, Cowen BR, Diller R, Maiti S, Hochstrasser RM.
PMID: 20717353
Appl Opt. 1991 Dec 20;30(36):5247-9. doi: 10.1364/AO.30.005247.

A method for generating two independently tunable 25-ps infrared pulses at 500 Hz was demonstrated. The apparatus is based on two dye lasers, a regenerative amplifier, and two lithium iodate optical-parametric amplifiers. Using the pump-probe technique, we measured the...

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Lannone M, Cowen BR, Diller R, et al. High-repetition-rate infrared-pump, infrared-probe spectrometer. Appl Opt. 1991;30(36):5247-9doi: 10.1364/AO.30.005247.
Lannone, M., Cowen, B. R., Diller, R., Maiti, S., & Hochstrasser, R. M. (1991). High-repetition-rate infrared-pump, infrared-probe spectrometer. Applied optics, 30(36), 5247-9. https://doi.org/10.1364/AO.30.005247
Lannone, M, et al. "High-repetition-rate infrared-pump, infrared-probe spectrometer." Applied optics vol. 30,36 (1991): 5247-9. doi: https://doi.org/10.1364/AO.30.005247
Lannone M, Cowen BR, Diller R, Maiti S, Hochstrasser RM. High-repetition-rate infrared-pump, infrared-probe spectrometer. Appl Opt. 1991 Dec 20;30(36):5247-9. doi: 10.1364/AO.30.005247. PMID: 20717353.
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Is a gene-centric human proteome project the best way for proteomics to serve biology?.

Proteomics

Rabilloud T, Hochstrasser D, Simpson RJ.
PMID: 20648483
Proteomics. 2010 Sep;10(17):3067-72. doi: 10.1002/pmic.201000220.

With the recent developments in proteomic technologies, a complete human proteome project (HPP) appears feasible for the first time. However, there is still debate as to how it should be designed and what it should encompass. In "proteomics speak",...

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Rabilloud T, Hochstrasser D, Simpson RJ. Is a gene-centric human proteome project the best way for proteomics to serve biology?. Proteomics. 2010;10(17):3067-72doi: 10.1002/pmic.201000220.
Rabilloud, T., Hochstrasser, D., & Simpson, R. J. (2010). Is a gene-centric human proteome project the best way for proteomics to serve biology?. Proteomics, 10(17), 3067-72. https://doi.org/10.1002/pmic.201000220
Rabilloud, Thierry, et al. "Is a gene-centric human proteome project the best way for proteomics to serve biology?." Proteomics vol. 10,17 (2010): 3067-72. doi: https://doi.org/10.1002/pmic.201000220
Rabilloud T, Hochstrasser D, Simpson RJ. Is a gene-centric human proteome project the best way for proteomics to serve biology?. Proteomics. 2010 Sep;10(17):3067-72. doi: 10.1002/pmic.201000220. PMID: 20648483.
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Analysis of proteomes using the molecular scanner.

CSH protocols

Déon C, Bienvenut W, Sanchez JC, Hochstrasser DF, Müller M, Gras R, Appel RD.
PMID: 21357015
CSH Protoc. 2007 Feb 01;2007:pdb.prot4592. doi: 10.1101/pdb.prot4592.

INTRODUCTIONThe molecular scanner offers a flexible and powerful visualization tool that can create a fully annotated 2D gel electrophoresis map. Proteins separated by 2D gel electrophoresis are simultaneously digested while undergoing electrotransfer from the gel to a membrane. The...

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Déon C, Bienvenut W, Sanchez JC, et al. Analysis of proteomes using the molecular scanner. CSH Protoc. 2007;2007:pdb.prot4592doi: 10.1101/pdb.prot4592.
Déon, C., Bienvenut, W., Sanchez, J. C., Hochstrasser, D. F., Müller, M., Gras, R., & Appel, R. D. (2007). Analysis of proteomes using the molecular scanner. CSH protocols, 2007pdb.prot4592. https://doi.org/10.1101/pdb.prot4592
Déon, Catherine, et al. "Analysis of proteomes using the molecular scanner." CSH protocols vol. 2007 (2007): pdb.prot4592. doi: https://doi.org/10.1101/pdb.prot4592
Déon C, Bienvenut W, Sanchez JC, Hochstrasser DF, Müller M, Gras R, Appel RD. Analysis of proteomes using the molecular scanner. CSH Protoc. 2007 Feb 01;2007:pdb.prot4592. doi: 10.1101/pdb.prot4592. PMID: 21357015.
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Accessing Reliable Health Information on the Web: A Review of the HON Approach.

Studies in health technology and informatics

Boyer C, Gaudinat A, Hanbury A, Appel RD, Ball MJ, Carpentier M, van Bemmel JH, Bergmans JP, Hochstrasser D, Lindberg D, Miller R, Peterschmitt JC, Safran C, Thonnet M, Geissbühler A.
PMID: 29295252
Stud Health Technol Inform. 2017;245:1004-1008.

Accessing online health content of high quality and reliability presents challenges. Laypersons cannot easily differentiate trustworthy content from misinformed or manipulated content. This article describes complementary approaches for members of the general public and health professionals to find trustworthy...

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Boyer C, Gaudinat A, Hanbury A, et al. Accessing Reliable Health Information on the Web: A Review of the HON Approach. Stud Health Technol Inform. 2017;245:1004-1008
Boyer, C., Gaudinat, A., Hanbury, A., Appel, R. D., Ball, M. J., Carpentier, M., van Bemmel, J. H., Bergmans, J. P., Hochstrasser, D., Lindberg, D., Miller, R., Peterschmitt, J. C., Safran, C., Thonnet, M., & Geissbühler, A. (2017). Accessing Reliable Health Information on the Web: A Review of the HON Approach. Studies in health technology and informatics, 2451004-1008.
Boyer, Célia, et al. "Accessing Reliable Health Information on the Web: A Review of the HON Approach." Studies in health technology and informatics vol. 245 (2017): 1004-1008.
Boyer C, Gaudinat A, Hanbury A, Appel RD, Ball MJ, Carpentier M, van Bemmel JH, Bergmans JP, Hochstrasser D, Lindberg D, Miller R, Peterschmitt JC, Safran C, Thonnet M, Geissbühler A. Accessing Reliable Health Information on the Web: A Review of the HON Approach. Stud Health Technol Inform. 2017;245:1004-1008. PMID: 29295252.
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CRISPR meets caspase.

Nature microbiology

Hochstrasser ML, Nuñez JK.
PMID: 34799728
Nat Microbiol. 2021 Dec;6(12):1481-1482. doi: 10.1038/s41564-021-01001-y.

No abstract available.

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Hochstrasser ML, Nuñez JK. CRISPR meets caspase. Nat Microbiol. 2021;6(12):1481-1482doi: 10.1038/s41564-021-01001-y.
Hochstrasser, M. L., & Nuñez, J. K. (2021). CRISPR meets caspase. Nature microbiology, 6(12), 1481-1482. https://doi.org/10.1038/s41564-021-01001-y
Hochstrasser, Megan L, and Nuñez, James K. "CRISPR meets caspase." Nature microbiology vol. 6,12 (2021): 1481-1482. doi: https://doi.org/10.1038/s41564-021-01001-y
Hochstrasser ML, Nuñez JK. CRISPR meets caspase. Nat Microbiol. 2021 Dec;6(12):1481-1482. doi: 10.1038/s41564-021-01001-y. PMID: 34799728.
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Showing 1 to 12 of 76 entries