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XML文書の解析はうまくいきますが、特定のタグ(「AbstractText」)の間にあるテキストが無作為に切り捨てられ、何もわかりません。繰り返しますが、これはここだけしか現れず、必ずしもこのタグの場合ではありません。解析のための私のコードは下にあり、また切り詰められたテキストの例です。解析XML - 取得された文字列が先頭に切り捨てられます。 Swift
var abstractBool = false
var abstract = ""
func parser(_ parser: XMLParser, didStartElement elementName: String, namespaceURI: String?, qualifiedName qName: String?, attributes attributeDict: [String : String] = [:]) {
switch elementName {
case "AbstractText":
abstractBool = true
}
}
func parser(_ parser: XMLParser, foundCharacters string: String) {
if abstractBool{
abstract = string
}
}
func parser(_ parser: XMLParser, didEndElement elementName: String,
namespaceURI: String?, qualifiedName qName: String?) {
switch elementName {
case "AbstractText":
abstractBool = false
}
}
リモートサーバから
生のXML:
私は抽出することができるよ何<Abstract>
<AbstractText>
Protein kinase C (PKC) has been shown to activate the mammalian target of
rapamycin complex 1 (mTORC1) signaling pathway, a central hub in the
regulation of cell metabolism, growth and proliferation. However, the
mechanisms by which PKCs activate mTORC1 are still ambiguous. Our previous
study revealed that activation of classical PKCs (cPKC) results in the
perinuclear accumulation of cPKC and phospholipase D2 (PLD2) in recycling
endosomes in a PLD2-dependent manner. Here, we report that mTORC1 activation
by phorbol 12,13-myristate acetate (PMA) requires both classic, cPKC, and
novel PKC (nPKC) isoforms, specifically PKCη, acting through distinct
pathways. The translocation of mTOR to perinuclear lysosomes was detected
after treatment of PKC activators, which was not colocalized with PKCα- or
RAB11-positive endosomes and was not inhibited by PLD inhibitors. We found
that PKCη inhibition by siRNA or bisindolylmaleimide I effectively decreased
mTOR accumulation in lysosomes and its activity. Also, we identified that
PKCη plays a role upstream of the v-ATPase/Ragulator/Rag pathway in response
to PMA. These data provides a spatial aspect to the regulation of mTORC1 by
sustained activation of PKC, requiring co-ordinated activation of two
distinct elements, the perinuclear accumulation of cPKC- and PLD-containing
endosomes and the nPKC-dependent translation of of mTOR in the perinuclear
lysosomes. The close proximity of these two distinct compartments shown in
this study suggests the possibility that transcompartment signaling may be a
factor in the regulation of mTORC1 activity and also underscores the
importance of PKCη as a potential therapeutic target of mTORC-related
disorders.
</AbstractText>
</Abstract>
文字列の次のフロント・エンド・切り捨てられた部分である:
scompartment signaling may be a factor in the regulation of mTORC1 activity
and also underscores the importance of PKCη as a potential therapeutic target
of mTORC-related disorders.
あなたのPSはiOSには適用されません。macOSだけです。 – rmaddy
コメントありがとうございます。質問に「iOS」というタグが付いているので、PSを削除しました。 –