Dynamic protein complexes:: Insights from mass spectrometry

[1] β2-microglobulin can be refolded into a native state from ex vivo amyloid fibrils [J]. EUROPEAN JOURNAL OF BIOCHEMISTRY, 1998, 258 (01): : 61 - 67

[2] Mass spectrometry of ribosomes and ribosomal subunits [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1998, 95 (13) : 7391 - 7395

[3] Viral capsid mobility: A dynamic conduit for inactivation [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2001, 98 (05) : 2274 - 2277

[4] Unfolding and disassembly of the chaperonin GroEL occurs via a tetradecameric intermediate with a folded equatorial domain [J]. BIOCHEMISTRY, 2000, 39 (15) : 4250 - 4258

[5] Coyle JE, 1999, NAT STRUCT BIOL, V6, P683

[6] Analysis of transcription complexes and effects of ligands by microelectrospray ionization mass spectrometry [J]. NATURE BIOTECHNOLOGY, 1999, 17 (12) : 1214 - 1218

[7] Removal of the N-terminal hexapeptide from human β2-microglobulin facilitates protein aggregation and fibril formation [J]. PROTEIN SCIENCE, 2000, 9 (05) : 831 - 845

[8] Observation of the noncovalent assembly and disassembly pathways of the chaperone complex MtGimC by mass spectrometry [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2000, 97 (26) : 14151 - 14155

[9] A NOVEL GENETIC SYSTEM TO DETECT PROTEIN PROTEIN INTERACTIONS [J]. NATURE, 1989, 340 (6230) : 245 - 246

[10] Commitment to folded and aggregated states occurs late in interleukin-1β folding [J]. BIOCHEMISTRY, 2000, 39 (50) : 15633 - 15642

[1] β2-microglobulin can be refolded into a native state from ex vivo amyloid fibrils [J]. EUROPEAN JOURNAL OF BIOCHEMISTRY, 1998, 258 (01): : 61 - 67

[2] Mass spectrometry of ribosomes and ribosomal subunits [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1998, 95 (13) : 7391 - 7395

[3] Viral capsid mobility: A dynamic conduit for inactivation [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2001, 98 (05) : 2274 - 2277

[4] Unfolding and disassembly of the chaperonin GroEL occurs via a tetradecameric intermediate with a folded equatorial domain [J]. BIOCHEMISTRY, 2000, 39 (15) : 4250 - 4258

[5] Coyle JE, 1999, NAT STRUCT BIOL, V6, P683

[6] Analysis of transcription complexes and effects of ligands by microelectrospray ionization mass spectrometry [J]. NATURE BIOTECHNOLOGY, 1999, 17 (12) : 1214 - 1218

[7] Removal of the N-terminal hexapeptide from human β2-microglobulin facilitates protein aggregation and fibril formation [J]. PROTEIN SCIENCE, 2000, 9 (05) : 831 - 845

[8] Observation of the noncovalent assembly and disassembly pathways of the chaperone complex MtGimC by mass spectrometry [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2000, 97 (26) : 14151 - 14155

[9] A NOVEL GENETIC SYSTEM TO DETECT PROTEIN PROTEIN INTERACTIONS [J]. NATURE, 1989, 340 (6230) : 245 - 246

[10] Commitment to folded and aggregated states occurs late in interleukin-1β folding [J]. BIOCHEMISTRY, 2000, 39 (50) : 15633 - 15642