000 | 03309nam a22004575i 4500 | ||
---|---|---|---|
001 | 978-94-007-4716-6 | ||
003 | DE-He213 | ||
005 | 20140220082934.0 | ||
007 | cr nn 008mamaa | ||
008 | 120731s2013 ne | s |||| 0|eng d | ||
020 |
_a9789400747166 _9978-94-007-4716-6 |
||
024 | 7 |
_a10.1007/978-94-007-4716-6 _2doi |
|
050 | 4 | _aR-RZ | |
072 | 7 |
_aMBGR _2bicssc |
|
072 | 7 |
_aMED000000 _2bisacsh |
|
082 | 0 | 4 |
_a610 _223 |
100 | 1 |
_aSeidler, Norbert W. _eauthor. |
|
245 | 1 | 0 |
_aGAPDH: Biological Properties and Diversity _h[electronic resource] / _cby Norbert W. Seidler. |
264 | 1 |
_aDordrecht : _bSpringer Netherlands : _bImprint: Springer, _c2013. |
|
300 |
_aXIV, 295 p. 96 illus., 8 illus. in color. _bonline resource. |
||
336 |
_atext _btxt _2rdacontent |
||
337 |
_acomputer _bc _2rdamedia |
||
338 |
_aonline resource _bcr _2rdacarrier |
||
347 |
_atext file _bPDF _2rda |
||
490 | 1 |
_aAdvances in Experimental Medicine and Biology, _x0065-2598 ; _v985 |
|
520 | _aGAPDH (glyceraldehyde 3-phosphate dehydrogenase) is more than just a glycolytic enzyme. An unprecedented amount of literature demonstrates that GAPDH has an astounding multiplicity of function. This diversity is not simply due to cell compartmentation (i.e. redistributing glycolytic energy to where it is needed), although this feature is undoubtedly important and discussed in the book. GAPDH integrates glycolysis with other cellular processes. This concept of integration cannot be understated. But, there is more. GAPDH actively participates in numerous non-glycolytic cellular events that fall into very broad categories including the cell infrastructure and the transmission of genetic information. Some of GAPDH’s biological properties are completely non-intuitive given the current undergraduate textbook understanding of this glycolytic enzyme. For example, GAPDH binds to select phospholipids and catalyzes organelle biogenesis. It has fusogenic properties, enabling it to be actively involved in nuclear envelop reassembly, autophagy and membrane trafficking. Human macrophages exhibit surface-localized GAPDH with receptor function. As scientists, we are trained to consider GAPDH as a soluble cytosolic dehydrogenase enzyme. The literature observations - as described in this book - tell us something quite different. Besides oxidoreductase activity, GAPDH exhibits peroxidase, uracil DNA glycosylase, nitrosylase, mono-ADP-ribosylase, esterase and phosphotransferase activity. GAPDH binds membrane transport proteins, G-proteins, poly-nucleotides, adenines, specific lipids, select carbohydrates, cytoskeletal proteins, nuclear import and export proteins, diverse ATPases, molecular chaperones and other molecules. | ||
650 | 0 | _aMedicine. | |
650 | 0 | _aChemistry. | |
650 | 0 | _aBiochemistry. | |
650 | 1 | 4 | _aBiomedicine. |
650 | 2 | 4 | _aBiomedicine general. |
650 | 2 | 4 | _aBiochemistry, general. |
650 | 2 | 4 | _aChemistry/Food Science, general. |
710 | 2 | _aSpringerLink (Online service) | |
773 | 0 | _tSpringer eBooks | |
776 | 0 | 8 |
_iPrinted edition: _z9789400747159 |
830 | 0 |
_aAdvances in Experimental Medicine and Biology, _x0065-2598 ; _v985 |
|
856 | 4 | 0 | _uhttp://dx.doi.org/10.1007/978-94-007-4716-6 |
912 | _aZDB-2-SBL | ||
999 |
_c99456 _d99456 |