Scientific
Papers:
Citations
NB: This page lists my scientific papers ranked by citations.* Only papers with at least 12 citations* are listed here. For a full list of publications click here.
Apologies for any broken links to scientific journals -- these seem to be always on the move !
Groß M & Jaenicke R (1994)
European Journal of Biochemistry 221, 617-630
Proteins under pressure: the influence of high hydrostatic pressure on structure, function and assembly of proteins and protein complexes
451 (411;396;379;363;345;328;313;284;263;238;211;174;147)Robinson CV, Groß M, Eyles SJ, Ewbank JJ, Mayhew M, Hartl FU, Dobson CM & Radford SE (1994)
Nature 372, 646-651
Conformation of GroEL-bound alpha-lactalbumin probed by mass spectrometry
187 (181;169;169;169;164;164;156;150;144;133;127;126;119)Jaikaran ETAS, Higham CE, Serpell LC, Zurdo J, Gross M, Clark A & Fraser PE (2001)
Journal of Molecular Biology 308, 515-525
Identification of a novel human islet amyloid polypeptide beta-sheet domain and factors influencing fibrillogenesis
132 (113;99;87;76;59;50;42;37;29;19;12;1;--)Plaxco KW & Groß M (1997)
Nature 386, 657-659
Cell biology: The importance of being unfolded (News and Views)
91 (81;78;73;72;70;67;65;61;55;50;41;31;18)Chung EW, Nettleton EJ, Morgan CJ, Groß M, Miranker A, Radford SE, Dobson CM & Robinson CV (1997)
Protein Science 6, 1316-1324
Hydrogen exchange properties of proteins in native and denatured states monitored by mass spectrometry and NMR
89 (88;85;84;80;77;77;71;61;59;54;47;42;30)Higham CE, Jaikaran ETAS, Fraser PE, Groß M & Clark A (2000)
FEBS Letters 470, 55-60
Preparation of synthetic human islet amyloid polypeptide (IAPP) in a stable conformation to enable study of conversion to amyloid-like fibrils FULL TEXT
78 (66;60;53;46;38;32;29;26;20;10;8;2;--)Plaxco KW & Gross M (2001)
Nature Structural Biology 8, 659-660
Unfolded, yes - but random? Never! (News and Views)
72 (69;66;65;63;61;55;51;46;36;23;15;0;--)Groß M, Robinson CV, Mayhew M, Hartl FU, Radford, SE (1996)
Protein Science 5, 2506-2513
Significant hydrogen exchange protection in GroEL-bound DHFR is maintained during iterative rounds of substrate cycling
56 (56;54;54;54;54;53;49;46;43;36;33;31;28)Groß M, Wilkins DK, Pitkeathly MC, Chung EW, Higham C, Clark A & Dobson CM (1999)
Protein Science 8, 1350-1357
Formation of amyloid fibrils by peptides derived from the bacterial cold-shock protein CspB
53 (52;51;51;47;45;40;38;36;33;27;22;12;9)Groß M, Lehle K, Jaenicke R & Nierhaus KH (1993)
European Journal of Biochemistry 218, 463-468
Pressure-induced dissociation of ribosomes and elongation cycle intermediates. Stabilizing conditions and identification of the most sensitive functional state
50 (41;39;34;32;28;25;24;23;21;18;18;15;12)Groß M & Jaenicke R (1991)
FEBS Letters 284, 87-90
Growth inhibition of lysozyme crystals at high hydrostatic pressure
48 (47;46;41;41;41;37;37;36;34;30;24;21;19)Groß M, Auerbach G & Jaenicke R (1993)
FEBS Letters 321, 256-260
The activities of monomeric enzymes show complex pressure-dependence
47 (46;45;45;44;42;39;38;38;35;33;33;31;28)Coyle JE, Jaeger J, Groß M, Robinson CV & Radford SE (1997)
Folding & Design 2, R93-R104
Structural and mechanistic consequences of polypeptide binding by GroEL
31 (31;31;31;31;30;29;29;28;27;24;24;23;17)Groß M & Jaenicke R (1993)
Biophysical Chemistry 45, 245-252
A kinetic model explaining the effects of hydrostatic pressure on nucleation and growth of lysozyme crystals
29 (29;28;27;27;27;26;26;25;24;24;22;17;17)Wilkins DK, Dobson CM & Groß M * (2000)
European Journal of Biochemistry, 267, 2609-2616
Biophysical studies of the development of amyloid fibrils from a peptide fragment of cold shock protein B
28 (26;25;24;22;20;19;18;16)Groß M & Jaenicke R (1990)
FEBS Letters 267, 239- 241
Pressure-induced dissociation of tight couple ribosomes
28 (25;25;24;24;24;22;21;21;19;17;16;15;14)Groß M, Kosmowsky IJ, Lorenz R, Molitoris HP & Jaenicke R * (1994)
Electrophoresis 15, 1559-1565
Response of bacteria and fungi to high-pressure stress as investigated by two- dimensional polyacrylamide gel electrophoresis
19 (15;15;11;10;9;8;8;7 ...)Groß M (2000)
Current Protein and Peptide Science 1, 339-347
Proteins that convert from alpha helix to beta sheet: Implications for folding and disease
18 (16;16;14;12;10;9;6;5 ...)Groß M (1996)
FEBS Letters 390, 249-252
Linguistic analysis of protein folding
17 (17;17;14;13;13;12;12;11;8)Gross M (2004): Current Protein and Peptide Science 5, No. 4, 213-223
Emergency services: An bird's eye perspective on the many different functions of stress proteins
12 (12;12;8;7;4 ... )
* Total number of citations according to ISI Science Citation Index / WOK determined
on 22.12.2014. Figures in () are from 21.12.2012, 21.12.2011, 23.12.2010,23.12.2009,19.12.2008, 19.12.2007, 21.12.2006, 20.12.2005, 22.12.2004, 23.12.2003, 3.1.2003, 27.12.2001 and 27.12.2000, respectively.
If two papers have the same number of citations, the more recent one is given
the higher ranking.
Some number-crunching (2011 figures): According to the definition proposed by Jorge Hirsch in 2005, my "h-index" stands at 17 (i.e. there are 17 papers with at least 17 citations). As the total number of papers is 32, the 16th defines the median number of citations, which is currently 25. Across all 32 papers, the total number of citations is 1378 and the average number 43.1.
In 2010, some citations mysteriously disappeared, probably due to changes to the database system which may no longer pick up certain types of citations including errors. In those cases, the earlier, higher citation count was kept.
last update:
22.12.2014