Proteomics
Abstract As an increasing number of available genomes triggers a gold rush in modern biology, the scientific challenge shifts towards understanding the total of the encoded information, most notably the proteins, their structures, functions and interactions. Currently this work is in its early stage...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Whitelegge, Julian P. [verfasserIn] le Contre, Johannes [verfasserIn] |
|---|
| Format: |
E-Artikel |
|---|---|
| Sprache: |
Englisch |
| Erschienen: |
2001 |
|---|
| Schlagwörter: |
|---|
| Übergeordnetes Werk: |
Enthalten in: American Journal of Pharmacogenomics - Springer International Publishing, 2001, 1(2001), 1 vom: März, Seite 29-35 |
|---|---|
| Übergeordnetes Werk: |
volume:1 ; year:2001 ; number:1 ; month:03 ; pages:29-35 |
| Links: |
|---|
| DOI / URN: |
10.2165/00129785-200101010-00004 |
|---|
| Katalog-ID: |
SPR033297800 |
|---|
| LEADER | 01000caa a22002652 4500 | ||
|---|---|---|---|
| 001 | SPR033297800 | ||
| 003 | DE-627 | ||
| 005 | 20230519084349.0 | ||
| 007 | cr uuu---uuuuu | ||
| 008 | 201007s2001 xx |||||o 00| ||eng c | ||
| 024 | 7 | |a 10.2165/00129785-200101010-00004 |2 doi | |
| 035 | |a (DE-627)SPR033297800 | ||
| 035 | |a (SPR)00129785-200101010-00004-e | ||
| 040 | |a DE-627 |b ger |c DE-627 |e rakwb | ||
| 041 | |a eng | ||
| 100 | 1 | |a Whitelegge, Julian P. |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Proteomics |
| 264 | 1 | |c 2001 | |
| 336 | |a Text |b txt |2 rdacontent | ||
| 337 | |a Computermedien |b c |2 rdamedia | ||
| 338 | |a Online-Ressource |b cr |2 rdacarrier | ||
| 520 | |a Abstract As an increasing number of available genomes triggers a gold rush in modern biology, the scientific challenge shifts towards understanding the total of the encoded information, most notably the proteins, their structures, functions and interactions. Currently this work is in its early stages but the near future will bring a merger of biology, engineering and informatics with a far broader impact on society than pure genomics has had so far. The challenge of characterizing the structures and functions of all proteins in a given cell demands technological advances beyond the classical methodologies of protein biochemistry. Mass spectrometry techniques for high-throughput protein identification, including peptide mass fingerprinting, sequence tagging and mass spectrometry on full-length proteins are providing the driving force behind proteomics endeavors. New technologies are needed to move high-resolution protein structure determination to an industrial scale. Nonetheless, improvements in techniques for the separation of intrinsic membrane proteins are enabling proteomics efforts towards identifying drug targets within this important class of biomolecules. Beyond the acquisition of data on sequences, structures and interactions, however, the major work in drug discovery remains: the screening of large candidate compound libraries combined with clever medicinal chemistry that guarantees selective action and defined delivery of the drug. | ||
| 650 | 4 | |a Intact Protein |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Peptide Mass Fingerprinting |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Protein Chip |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Intrinsic Membrane Protein |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Protein Structure Determination |7 (dpeaa)DE-He213 | |
| 700 | 1 | |a le Contre, Johannes |e verfasserin |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |t American Journal of Pharmacogenomics |d Springer International Publishing, 2001 |g 1(2001), 1 vom: März, Seite 29-35 |w (DE-627)SPR033297754 |7 nnns |
| 773 | 1 | 8 | |g volume:1 |g year:2001 |g number:1 |g month:03 |g pages:29-35 |
| 856 | 4 | 0 | |u https://dx.doi.org/10.2165/00129785-200101010-00004 |z lizenzpflichtig |3 Volltext |
| 912 | |a GBV_USEFLAG_A | ||
| 912 | |a SYSFLAG_A | ||
| 912 | |a GBV_SPRINGER | ||
| 912 | |a SSG-OLC-PHA | ||
| 951 | |a AR | ||
| 952 | |d 1 |j 2001 |e 1 |c 03 |h 29-35 | ||
| author_variant |
j p w jp jpw c j l cj cjl |
|---|---|
| matchkey_str |
whiteleggejulianplecontrejohannes:2001----:rto |
| hierarchy_sort_str |
2001 |
| publishDate |
2001 |
| allfields |
10.2165/00129785-200101010-00004 doi (DE-627)SPR033297800 (SPR)00129785-200101010-00004-e DE-627 ger DE-627 rakwb eng Whitelegge, Julian P. verfasserin aut Proteomics 2001 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract As an increasing number of available genomes triggers a gold rush in modern biology, the scientific challenge shifts towards understanding the total of the encoded information, most notably the proteins, their structures, functions and interactions. Currently this work is in its early stages but the near future will bring a merger of biology, engineering and informatics with a far broader impact on society than pure genomics has had so far. The challenge of characterizing the structures and functions of all proteins in a given cell demands technological advances beyond the classical methodologies of protein biochemistry. Mass spectrometry techniques for high-throughput protein identification, including peptide mass fingerprinting, sequence tagging and mass spectrometry on full-length proteins are providing the driving force behind proteomics endeavors. New technologies are needed to move high-resolution protein structure determination to an industrial scale. Nonetheless, improvements in techniques for the separation of intrinsic membrane proteins are enabling proteomics efforts towards identifying drug targets within this important class of biomolecules. Beyond the acquisition of data on sequences, structures and interactions, however, the major work in drug discovery remains: the screening of large candidate compound libraries combined with clever medicinal chemistry that guarantees selective action and defined delivery of the drug. Intact Protein (dpeaa)DE-He213 Peptide Mass Fingerprinting (dpeaa)DE-He213 Protein Chip (dpeaa)DE-He213 Intrinsic Membrane Protein (dpeaa)DE-He213 Protein Structure Determination (dpeaa)DE-He213 le Contre, Johannes verfasserin aut Enthalten in American Journal of Pharmacogenomics Springer International Publishing, 2001 1(2001), 1 vom: März, Seite 29-35 (DE-627)SPR033297754 nnns volume:1 year:2001 number:1 month:03 pages:29-35 https://dx.doi.org/10.2165/00129785-200101010-00004 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA AR 1 2001 1 03 29-35 |
| spelling |
10.2165/00129785-200101010-00004 doi (DE-627)SPR033297800 (SPR)00129785-200101010-00004-e DE-627 ger DE-627 rakwb eng Whitelegge, Julian P. verfasserin aut Proteomics 2001 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract As an increasing number of available genomes triggers a gold rush in modern biology, the scientific challenge shifts towards understanding the total of the encoded information, most notably the proteins, their structures, functions and interactions. Currently this work is in its early stages but the near future will bring a merger of biology, engineering and informatics with a far broader impact on society than pure genomics has had so far. The challenge of characterizing the structures and functions of all proteins in a given cell demands technological advances beyond the classical methodologies of protein biochemistry. Mass spectrometry techniques for high-throughput protein identification, including peptide mass fingerprinting, sequence tagging and mass spectrometry on full-length proteins are providing the driving force behind proteomics endeavors. New technologies are needed to move high-resolution protein structure determination to an industrial scale. Nonetheless, improvements in techniques for the separation of intrinsic membrane proteins are enabling proteomics efforts towards identifying drug targets within this important class of biomolecules. Beyond the acquisition of data on sequences, structures and interactions, however, the major work in drug discovery remains: the screening of large candidate compound libraries combined with clever medicinal chemistry that guarantees selective action and defined delivery of the drug. Intact Protein (dpeaa)DE-He213 Peptide Mass Fingerprinting (dpeaa)DE-He213 Protein Chip (dpeaa)DE-He213 Intrinsic Membrane Protein (dpeaa)DE-He213 Protein Structure Determination (dpeaa)DE-He213 le Contre, Johannes verfasserin aut Enthalten in American Journal of Pharmacogenomics Springer International Publishing, 2001 1(2001), 1 vom: März, Seite 29-35 (DE-627)SPR033297754 nnns volume:1 year:2001 number:1 month:03 pages:29-35 https://dx.doi.org/10.2165/00129785-200101010-00004 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA AR 1 2001 1 03 29-35 |
| allfields_unstemmed |
10.2165/00129785-200101010-00004 doi (DE-627)SPR033297800 (SPR)00129785-200101010-00004-e DE-627 ger DE-627 rakwb eng Whitelegge, Julian P. verfasserin aut Proteomics 2001 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract As an increasing number of available genomes triggers a gold rush in modern biology, the scientific challenge shifts towards understanding the total of the encoded information, most notably the proteins, their structures, functions and interactions. Currently this work is in its early stages but the near future will bring a merger of biology, engineering and informatics with a far broader impact on society than pure genomics has had so far. The challenge of characterizing the structures and functions of all proteins in a given cell demands technological advances beyond the classical methodologies of protein biochemistry. Mass spectrometry techniques for high-throughput protein identification, including peptide mass fingerprinting, sequence tagging and mass spectrometry on full-length proteins are providing the driving force behind proteomics endeavors. New technologies are needed to move high-resolution protein structure determination to an industrial scale. Nonetheless, improvements in techniques for the separation of intrinsic membrane proteins are enabling proteomics efforts towards identifying drug targets within this important class of biomolecules. Beyond the acquisition of data on sequences, structures and interactions, however, the major work in drug discovery remains: the screening of large candidate compound libraries combined with clever medicinal chemistry that guarantees selective action and defined delivery of the drug. Intact Protein (dpeaa)DE-He213 Peptide Mass Fingerprinting (dpeaa)DE-He213 Protein Chip (dpeaa)DE-He213 Intrinsic Membrane Protein (dpeaa)DE-He213 Protein Structure Determination (dpeaa)DE-He213 le Contre, Johannes verfasserin aut Enthalten in American Journal of Pharmacogenomics Springer International Publishing, 2001 1(2001), 1 vom: März, Seite 29-35 (DE-627)SPR033297754 nnns volume:1 year:2001 number:1 month:03 pages:29-35 https://dx.doi.org/10.2165/00129785-200101010-00004 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA AR 1 2001 1 03 29-35 |
| allfieldsGer |
10.2165/00129785-200101010-00004 doi (DE-627)SPR033297800 (SPR)00129785-200101010-00004-e DE-627 ger DE-627 rakwb eng Whitelegge, Julian P. verfasserin aut Proteomics 2001 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract As an increasing number of available genomes triggers a gold rush in modern biology, the scientific challenge shifts towards understanding the total of the encoded information, most notably the proteins, their structures, functions and interactions. Currently this work is in its early stages but the near future will bring a merger of biology, engineering and informatics with a far broader impact on society than pure genomics has had so far. The challenge of characterizing the structures and functions of all proteins in a given cell demands technological advances beyond the classical methodologies of protein biochemistry. Mass spectrometry techniques for high-throughput protein identification, including peptide mass fingerprinting, sequence tagging and mass spectrometry on full-length proteins are providing the driving force behind proteomics endeavors. New technologies are needed to move high-resolution protein structure determination to an industrial scale. Nonetheless, improvements in techniques for the separation of intrinsic membrane proteins are enabling proteomics efforts towards identifying drug targets within this important class of biomolecules. Beyond the acquisition of data on sequences, structures and interactions, however, the major work in drug discovery remains: the screening of large candidate compound libraries combined with clever medicinal chemistry that guarantees selective action and defined delivery of the drug. Intact Protein (dpeaa)DE-He213 Peptide Mass Fingerprinting (dpeaa)DE-He213 Protein Chip (dpeaa)DE-He213 Intrinsic Membrane Protein (dpeaa)DE-He213 Protein Structure Determination (dpeaa)DE-He213 le Contre, Johannes verfasserin aut Enthalten in American Journal of Pharmacogenomics Springer International Publishing, 2001 1(2001), 1 vom: März, Seite 29-35 (DE-627)SPR033297754 nnns volume:1 year:2001 number:1 month:03 pages:29-35 https://dx.doi.org/10.2165/00129785-200101010-00004 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA AR 1 2001 1 03 29-35 |
| allfieldsSound |
10.2165/00129785-200101010-00004 doi (DE-627)SPR033297800 (SPR)00129785-200101010-00004-e DE-627 ger DE-627 rakwb eng Whitelegge, Julian P. verfasserin aut Proteomics 2001 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract As an increasing number of available genomes triggers a gold rush in modern biology, the scientific challenge shifts towards understanding the total of the encoded information, most notably the proteins, their structures, functions and interactions. Currently this work is in its early stages but the near future will bring a merger of biology, engineering and informatics with a far broader impact on society than pure genomics has had so far. The challenge of characterizing the structures and functions of all proteins in a given cell demands technological advances beyond the classical methodologies of protein biochemistry. Mass spectrometry techniques for high-throughput protein identification, including peptide mass fingerprinting, sequence tagging and mass spectrometry on full-length proteins are providing the driving force behind proteomics endeavors. New technologies are needed to move high-resolution protein structure determination to an industrial scale. Nonetheless, improvements in techniques for the separation of intrinsic membrane proteins are enabling proteomics efforts towards identifying drug targets within this important class of biomolecules. Beyond the acquisition of data on sequences, structures and interactions, however, the major work in drug discovery remains: the screening of large candidate compound libraries combined with clever medicinal chemistry that guarantees selective action and defined delivery of the drug. Intact Protein (dpeaa)DE-He213 Peptide Mass Fingerprinting (dpeaa)DE-He213 Protein Chip (dpeaa)DE-He213 Intrinsic Membrane Protein (dpeaa)DE-He213 Protein Structure Determination (dpeaa)DE-He213 le Contre, Johannes verfasserin aut Enthalten in American Journal of Pharmacogenomics Springer International Publishing, 2001 1(2001), 1 vom: März, Seite 29-35 (DE-627)SPR033297754 nnns volume:1 year:2001 number:1 month:03 pages:29-35 https://dx.doi.org/10.2165/00129785-200101010-00004 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA AR 1 2001 1 03 29-35 |
| language |
English |
| source |
Enthalten in American Journal of Pharmacogenomics 1(2001), 1 vom: März, Seite 29-35 volume:1 year:2001 number:1 month:03 pages:29-35 |
| sourceStr |
Enthalten in American Journal of Pharmacogenomics 1(2001), 1 vom: März, Seite 29-35 volume:1 year:2001 number:1 month:03 pages:29-35 |
| format_phy_str_mv |
Article |
| institution |
findex.gbv.de |
| topic_facet |
Intact Protein Peptide Mass Fingerprinting Protein Chip Intrinsic Membrane Protein Protein Structure Determination |
| isfreeaccess_bool |
false |
| container_title |
American Journal of Pharmacogenomics |
| authorswithroles_txt_mv |
Whitelegge, Julian P. @@aut@@ le Contre, Johannes @@aut@@ |
| publishDateDaySort_date |
2001-03-01T00:00:00Z |
| hierarchy_top_id |
SPR033297754 |
| id |
SPR033297800 |
| language_de |
englisch |
| fullrecord |
<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">SPR033297800</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230519084349.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">201007s2001 xx |||||o 00| ||eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.2165/00129785-200101010-00004</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)SPR033297800</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(SPR)00129785-200101010-00004-e</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Whitelegge, Julian P.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Proteomics</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2001</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">Computermedien</subfield><subfield code="b">c</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield><subfield code="b">cr</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Abstract As an increasing number of available genomes triggers a gold rush in modern biology, the scientific challenge shifts towards understanding the total of the encoded information, most notably the proteins, their structures, functions and interactions. Currently this work is in its early stages but the near future will bring a merger of biology, engineering and informatics with a far broader impact on society than pure genomics has had so far. The challenge of characterizing the structures and functions of all proteins in a given cell demands technological advances beyond the classical methodologies of protein biochemistry. Mass spectrometry techniques for high-throughput protein identification, including peptide mass fingerprinting, sequence tagging and mass spectrometry on full-length proteins are providing the driving force behind proteomics endeavors. New technologies are needed to move high-resolution protein structure determination to an industrial scale. Nonetheless, improvements in techniques for the separation of intrinsic membrane proteins are enabling proteomics efforts towards identifying drug targets within this important class of biomolecules. Beyond the acquisition of data on sequences, structures and interactions, however, the major work in drug discovery remains: the screening of large candidate compound libraries combined with clever medicinal chemistry that guarantees selective action and defined delivery of the drug.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Intact Protein</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Peptide Mass Fingerprinting</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Protein Chip</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Intrinsic Membrane Protein</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Protein Structure Determination</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">le Contre, Johannes</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="t">American Journal of Pharmacogenomics</subfield><subfield code="d">Springer International Publishing, 2001</subfield><subfield code="g">1(2001), 1 vom: März, Seite 29-35</subfield><subfield code="w">(DE-627)SPR033297754</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:1</subfield><subfield code="g">year:2001</subfield><subfield code="g">number:1</subfield><subfield code="g">month:03</subfield><subfield code="g">pages:29-35</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">https://dx.doi.org/10.2165/00129785-200101010-00004</subfield><subfield code="z">lizenzpflichtig</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SYSFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_SPRINGER</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-PHA</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">1</subfield><subfield code="j">2001</subfield><subfield code="e">1</subfield><subfield code="c">03</subfield><subfield code="h">29-35</subfield></datafield></record></collection>
|
| author |
Whitelegge, Julian P. |
| spellingShingle |
Whitelegge, Julian P. misc Intact Protein misc Peptide Mass Fingerprinting misc Protein Chip misc Intrinsic Membrane Protein misc Protein Structure Determination Proteomics |
| authorStr |
Whitelegge, Julian P. |
| ppnlink_with_tag_str_mv |
@@773@@(DE-627)SPR033297754 |
| format |
electronic Article |
| delete_txt_mv |
keep |
| author_role |
aut aut |
| collection |
springer |
| remote_str |
true |
| illustrated |
Not Illustrated |
| topic_title |
Proteomics Intact Protein (dpeaa)DE-He213 Peptide Mass Fingerprinting (dpeaa)DE-He213 Protein Chip (dpeaa)DE-He213 Intrinsic Membrane Protein (dpeaa)DE-He213 Protein Structure Determination (dpeaa)DE-He213 |
| topic |
misc Intact Protein misc Peptide Mass Fingerprinting misc Protein Chip misc Intrinsic Membrane Protein misc Protein Structure Determination |
| topic_unstemmed |
misc Intact Protein misc Peptide Mass Fingerprinting misc Protein Chip misc Intrinsic Membrane Protein misc Protein Structure Determination |
| topic_browse |
misc Intact Protein misc Peptide Mass Fingerprinting misc Protein Chip misc Intrinsic Membrane Protein misc Protein Structure Determination |
| format_facet |
Elektronische Aufsätze Aufsätze Elektronische Ressource |
| format_main_str_mv |
Text Zeitschrift/Artikel |
| carriertype_str_mv |
cr |
| hierarchy_parent_title |
American Journal of Pharmacogenomics |
| hierarchy_parent_id |
SPR033297754 |
| hierarchy_top_title |
American Journal of Pharmacogenomics |
| isfreeaccess_txt |
false |
| familylinks_str_mv |
(DE-627)SPR033297754 |
| title |
Proteomics |
| ctrlnum |
(DE-627)SPR033297800 (SPR)00129785-200101010-00004-e |
| title_full |
Proteomics |
| author_sort |
Whitelegge, Julian P. |
| journal |
American Journal of Pharmacogenomics |
| journalStr |
American Journal of Pharmacogenomics |
| lang_code |
eng |
| isOA_bool |
false |
| recordtype |
marc |
| publishDateSort |
2001 |
| contenttype_str_mv |
txt |
| container_start_page |
29 |
| author_browse |
Whitelegge, Julian P. le Contre, Johannes |
| container_volume |
1 |
| format_se |
Elektronische Aufsätze |
| author-letter |
Whitelegge, Julian P. |
| doi_str_mv |
10.2165/00129785-200101010-00004 |
| author2-role |
verfasserin |
| title_sort |
proteomics |
| title_auth |
Proteomics |
| abstract |
Abstract As an increasing number of available genomes triggers a gold rush in modern biology, the scientific challenge shifts towards understanding the total of the encoded information, most notably the proteins, their structures, functions and interactions. Currently this work is in its early stages but the near future will bring a merger of biology, engineering and informatics with a far broader impact on society than pure genomics has had so far. The challenge of characterizing the structures and functions of all proteins in a given cell demands technological advances beyond the classical methodologies of protein biochemistry. Mass spectrometry techniques for high-throughput protein identification, including peptide mass fingerprinting, sequence tagging and mass spectrometry on full-length proteins are providing the driving force behind proteomics endeavors. New technologies are needed to move high-resolution protein structure determination to an industrial scale. Nonetheless, improvements in techniques for the separation of intrinsic membrane proteins are enabling proteomics efforts towards identifying drug targets within this important class of biomolecules. Beyond the acquisition of data on sequences, structures and interactions, however, the major work in drug discovery remains: the screening of large candidate compound libraries combined with clever medicinal chemistry that guarantees selective action and defined delivery of the drug. |
| abstractGer |
Abstract As an increasing number of available genomes triggers a gold rush in modern biology, the scientific challenge shifts towards understanding the total of the encoded information, most notably the proteins, their structures, functions and interactions. Currently this work is in its early stages but the near future will bring a merger of biology, engineering and informatics with a far broader impact on society than pure genomics has had so far. The challenge of characterizing the structures and functions of all proteins in a given cell demands technological advances beyond the classical methodologies of protein biochemistry. Mass spectrometry techniques for high-throughput protein identification, including peptide mass fingerprinting, sequence tagging and mass spectrometry on full-length proteins are providing the driving force behind proteomics endeavors. New technologies are needed to move high-resolution protein structure determination to an industrial scale. Nonetheless, improvements in techniques for the separation of intrinsic membrane proteins are enabling proteomics efforts towards identifying drug targets within this important class of biomolecules. Beyond the acquisition of data on sequences, structures and interactions, however, the major work in drug discovery remains: the screening of large candidate compound libraries combined with clever medicinal chemistry that guarantees selective action and defined delivery of the drug. |
| abstract_unstemmed |
Abstract As an increasing number of available genomes triggers a gold rush in modern biology, the scientific challenge shifts towards understanding the total of the encoded information, most notably the proteins, their structures, functions and interactions. Currently this work is in its early stages but the near future will bring a merger of biology, engineering and informatics with a far broader impact on society than pure genomics has had so far. The challenge of characterizing the structures and functions of all proteins in a given cell demands technological advances beyond the classical methodologies of protein biochemistry. Mass spectrometry techniques for high-throughput protein identification, including peptide mass fingerprinting, sequence tagging and mass spectrometry on full-length proteins are providing the driving force behind proteomics endeavors. New technologies are needed to move high-resolution protein structure determination to an industrial scale. Nonetheless, improvements in techniques for the separation of intrinsic membrane proteins are enabling proteomics efforts towards identifying drug targets within this important class of biomolecules. Beyond the acquisition of data on sequences, structures and interactions, however, the major work in drug discovery remains: the screening of large candidate compound libraries combined with clever medicinal chemistry that guarantees selective action and defined delivery of the drug. |
| collection_details |
GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA |
| container_issue |
1 |
| title_short |
Proteomics |
| url |
https://dx.doi.org/10.2165/00129785-200101010-00004 |
| remote_bool |
true |
| author2 |
le Contre, Johannes |
| author2Str |
le Contre, Johannes |
| ppnlink |
SPR033297754 |
| mediatype_str_mv |
c |
| isOA_txt |
false |
| hochschulschrift_bool |
false |
| doi_str |
10.2165/00129785-200101010-00004 |
| up_date |
2024-07-03T17:47:29.333Z |
| _version_ |
1803580970720296960 |
| fullrecord_marcxml |
<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">SPR033297800</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230519084349.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">201007s2001 xx |||||o 00| ||eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.2165/00129785-200101010-00004</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)SPR033297800</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(SPR)00129785-200101010-00004-e</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Whitelegge, Julian P.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Proteomics</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2001</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">Computermedien</subfield><subfield code="b">c</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield><subfield code="b">cr</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Abstract As an increasing number of available genomes triggers a gold rush in modern biology, the scientific challenge shifts towards understanding the total of the encoded information, most notably the proteins, their structures, functions and interactions. Currently this work is in its early stages but the near future will bring a merger of biology, engineering and informatics with a far broader impact on society than pure genomics has had so far. The challenge of characterizing the structures and functions of all proteins in a given cell demands technological advances beyond the classical methodologies of protein biochemistry. Mass spectrometry techniques for high-throughput protein identification, including peptide mass fingerprinting, sequence tagging and mass spectrometry on full-length proteins are providing the driving force behind proteomics endeavors. New technologies are needed to move high-resolution protein structure determination to an industrial scale. Nonetheless, improvements in techniques for the separation of intrinsic membrane proteins are enabling proteomics efforts towards identifying drug targets within this important class of biomolecules. Beyond the acquisition of data on sequences, structures and interactions, however, the major work in drug discovery remains: the screening of large candidate compound libraries combined with clever medicinal chemistry that guarantees selective action and defined delivery of the drug.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Intact Protein</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Peptide Mass Fingerprinting</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Protein Chip</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Intrinsic Membrane Protein</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Protein Structure Determination</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">le Contre, Johannes</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="t">American Journal of Pharmacogenomics</subfield><subfield code="d">Springer International Publishing, 2001</subfield><subfield code="g">1(2001), 1 vom: März, Seite 29-35</subfield><subfield code="w">(DE-627)SPR033297754</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:1</subfield><subfield code="g">year:2001</subfield><subfield code="g">number:1</subfield><subfield code="g">month:03</subfield><subfield code="g">pages:29-35</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">https://dx.doi.org/10.2165/00129785-200101010-00004</subfield><subfield code="z">lizenzpflichtig</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SYSFLAG_A</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_SPRINGER</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-PHA</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">1</subfield><subfield code="j">2001</subfield><subfield code="e">1</subfield><subfield code="c">03</subfield><subfield code="h">29-35</subfield></datafield></record></collection>
|
| score |
7.4013977 |