User:Millstea

My Annotations

Status	Page	Date/Time	GO Term (Aspect)	Reference	Evidence	Notes	Links
acceptable	ARATH:CESA8	2012-04-13 23:09:04 CDT	GO:0016760 cellulose synthase (UDP-forming) activity (F)	PMID:9165747	ECO:0000315 mutant phenotype evidence used in manual assertion	CesA8 mutants have a reduced cellulose content and resulting irregular xylem shape. This suggests that this cellulose synthase isoform is involved in secondary wall synthesis of Arabidopsis thaliana.Fig. 6 demonstrates the results through electron microscopy of thinned cellular walls in mutants.Fig. 7 also illustrates how mutants (irx is synonym for CesA8) are weaker/more susceptible to bending.	challenge
acceptable	SYNE7:ALDEC	2012-04-14 09:06:38 CDT	GO:0071771 aldehyde decarbonylase activity (F)	PMID:20671186	ECO:0000315 mutant phenotype evidence used in manual assertion	Aldehyde decarbonylase, purified from Synechococcus elongatus PCC 7942 was able to decarbonylate fatty aldehydes when expressed in E.coli. According to Fig. 1, when introduced along with acyl-[acp] reductase, the host organism was conferred the ability to produce alkane.	challenge
requireschanges	HELTU:O81985	2012-04-14 16:40:54 CDT	GO:0047207 1,2-beta-fructan 1F-fructosyltransferase activity (F)	PMID:9753774	ECO:0000315 mutant phenotype evidence used in manual assertion	Fig. 6 illustrates transferred fructosyltransferase activity after incorporating the fft-1 gene product into transgenic Petunia that does not naturally have fructosyltransferase function.	challenge
acceptable	HELTU:O81986	2012-04-14 17:02:48 CDT	GO:0050306 sucrose 1F-fructosyltransferase activity (F)	PMID:12226250	ECO:0000314 direct assay evidence used in manual assertion	Fig.2 shows the sucrose (substrate) dependent rate of GF2 by 1-SST from the plant tubers. Fig. 3 is a representation of the efficiency of this same conversion with an added step to eliminate the possibility of any 1-FFT impurities.	challenge
requireschanges	ASPTE:B3IUN8	2012-04-14 20:35:33 CDT	GO:0047613 aconitate decarboxylase activity (F)	PMID:18584171	ECO:0000315 mutant phenotype evidence used in manual assertion	The CAD1 gene was cloned from and then expressed in S. cerevisiae where activity was verified. Fig. 3 shows how the recombinant activity (measured by direct detection of itaconic acid product) was detected by HPLC.	challenge
acceptable	YEAST:ALG5	2012-04-15 00:04:56 CDT	GO:0004581 dolichyl-phosphate beta-glucosyltransferase activity (F)	PMID:8076653	ECO:0000315 mutant phenotype evidence used in manual assertion	Mutations of ALG5 result in loss of enzyme function and underglycosylation of proteins. Fig. 2 shows ALG5 where complementations restored the ability to glycosylate carboxypeptidase Y. Also, Table 2 further illustrates that mutated ALG5 genes resulted in loss of function to synthesize DolP-Glc.	challenge

acceptable:4
unacceptable:0
requires_changes:2
flagged:0

Annotations challenged by Millstea

Status	Author,Group	Page	GO Term (Aspect)	Reference	Evidence	Links	Page history
acceptable	Ke607259, Team Barbara McClintock	ECOLI:LACY	GO:0008643 - carbohydrate transport (P)	PMID:22202176	ECO:0000315 mutant phenotype evidence used in manual assertion	challenge	C: 1

0 annotations fixed by Millstea

My Annotations

Status	Page	Date/Time	GO Term (Aspect)	Reference	Evidence	Notes	Links
requireschanges	PELCA:Q60154	2012-03-31 13:59:18 CDT	GO:0004148 dihydrolipoyl dehydrogenase activity (F)	PMID:1898934	ECO:0000021 physical interaction evidence	Codes for a subunit(dihydrolipoamide dehydrogenase)that dimerizes to become the E3 subunit dihydrolipoamide dehydrogenase (DHLDH) in the acetoin dehydrogenase complex that catalyzes the conversion of acetoin to acetyl-CoA and acetaldehyde. Table 6 indicates DHLDH is only present in high activity in acetoin utilizing cultures. Fig. 4 illustrates growth of P. carbinolicus in double immunodiffusion tests that gave strong cross-reactions only between organisms capable of utilizing and degrading acetoin	challenge

acceptable:0
unacceptable:0
requires_changes:1
flagged:0

Annotations challenged by Millstea

Status	Author,Group	Page	GO Term (Aspect)	Reference	Evidence	Links	Page history

0 annotations fixed by Millstea